Information

What are this designs which I found on curry leaves?


Curry leaves is the plant name where I found designs, but what are the designs present on the leaf?

Location: Argentina


For tips on performing your experiment and presenting your project, see our free science fair guide. Browse our Science Fair Kits category for more project ideas and easy-to-use products.

Bacteria:

Use petri dishes and agar to grow bacteria.

  • What effect do household cleaners have on a bacteria culture? What about temperature? What is the best or worst environment in your house for bacteria growth?
  • Are there substances in your kitchen (garlic, red pepper, curry, tea tree oil, etc.) that have natural antibacterial properties?
  • Use the Gram stain method for testing whether Gram-positive or Gram-negative bacteria is more common in your house. Do common antibiotics interact differently with Gram-positive and Gram-negative bacteria?
  • Studying mold growth conditions also makes an interesting experiment. What types of food mold the quickest? How does temperature affect mold growth? Are there some practical ways to slow down the growth of mold? Experiment with different types of preservatives to see how they prevent mold growth.
  • Does bacteria grow in a predictable pattern? Try an experiment by making thumbprint, fingerprint, or handprint bacteria cultures using agar and petri dishes.
  • How much bacteria grows in the mouth and what effects do common cleaning techniques have on bacteria growth? Consider brushing with a dry toothbrush, comparing different toothpastes, mouthwashes, and flossing as well as time spent cleaning teeth to find which methods work best to keep the mouth clean.
  • Is a dog’s mouth really cleaner than a human’s?
  • Use GloGerms to simulate the behavior of germs. Experiment to find the best ways to eliminate germs from hands and surfaces. (Test water temperature, soaps, length of time spent washing, etc.)
  • See a sample step-by-step project and more project ideas in our Bacteria Science Project Guide.

Botany:

  • Design an experiment to experiment with leaf color pigments. (You might compare pigments of different species of leaves or leaves at different times of year.)
  • How do plants react to more or less light? What effect does wind or pressure have on plants?
  • What happens when different types of soil or fertilizers are used on the same type of plant?
  • How do heat and cold affect sprouting?
  • How do different soil types affect the ability of roots to anchor the plant?
  • Does light wavelength affect plant growth?
  • What is the effect of acid rain on plant growth?
  • Set up an experiment to measure the rate of photosynthesis and see the effects of temperature, light intensity, or concentration of CO2.
  • Design an experiment to discover the effects of abnormal radiation on plant growth, using irradiated seeds that are treated at different radiation levels.
  • Try growing seeds from different fruit that you’ve eaten. Which ones grow best?

Human Body & Anatomy:

  • Test reflexes, hearing, lung capacity, or vision. Does one age group seem to have better results than another?
  • Does your nose have anything to do with taste?
  • How does age affect peripheral vision?
  • How does the pH level of hair products affect hair quality? (Use pH strips for testing.)
  • Can petting an animal lower your heart rate? Is there a difference between petting your own pet and petting an animal that you are not attached to?
  • Does the heart rate of an animal decrease while it is being petted?
  • Is there a difference between video games that make the player be physically active versus nonphysical video games on the player’s heart rate or blood pressure?

Insects:

    What household foods are most effective at attracting ants or other insects? What bait will probably attract the greatest number of different insect species?
  • What happens to insects in winter?
  • Which characteristic (fragrance, color, flavor) has the most influence in attracting a species of bee or butterfly to a flower?
  • Do bees recognize patterns? Can this help them find their food sources?
  • Design an experiment to explore how ants communicate with scent (pheremones).

Soil, Water, Acid Rain, and the Environment:

  • Do the organisms found at different levels of a pond differ significantly? You might try re-creating a pond “cross section” of life.
  • Where do you find the most polluted water locally? What about water with the highest and lowest pH? (Use a water test kit.) Does this have an effect on the organisms (fish, insects, algae, protozoa, frogs, etc.) that live in or next to it?
  • Investigate which pH and chemical levels are most common in your area. How do garden soils with different amounts of nitrogen, phosphorus, potash, or pH compare? (Use a soil analyzer.)
  • Which de-icing agent used on roads in winter has the least negative environmental impact?
  • You can make artificial acid rain by taking distilled water and slowly adding sulfuric acid (one drop at a time) until the pH of the water reads about 4.0.
  • You may also be able to collect rain water and test its pH level to see if it is acidic enough (pH

Zoology:

  • Study brine shrimp or protozoa what happens if you add mild pollutants to their habitat? (See our brine shrimp project.) Do different species (such as amoeba and euglena) react differently? (For testing specific species, you may want to get a live culture.)
  • What effect does temperature have on brine shrimp or Triops? Compare hatching, growth, and population rates in a warmer environment vs. a colder one.
  • How do earthworms help improve soil quality?

LC-MS–MS characterisation of curry leaf flavonols and antioxidant activity

Curry leaf (Murraya koenegii) is a common flavouring agent in Indian foods. This study characterised the flavonol profile of curry leaf extracted with different solvents and the relative antioxidant capacity of these extracts by quantifying phenolic constituents. Flavonols were extracted using ethanol, methanol, or acetone prior to identification and quantification using liquid chromatography coupled to atmospheric pressure chemical ionisation (APCI) mass spectrometry in tandem mode (LC-MS–MS) with negative ion detection. Major curry leaf flavonols included myricetin-3-galactoside, quercetin-O-pentohexoside, quercetin-3-diglucoside, quercetin-3-O-rutinoside, quercetin-3-glucoside, quercetin-3-acetylhexoside, quercetin-O-xylo-pentoside, kaempferol-O-glucoside, and kaempferol-aglucoside. Lag-time and TBARS tests demonstrated that curry leaf phenolics prevent cupric-ion induced oxidation of LDL. The best extraction yield was obtained with 80% ethanol. Acetone extracts provided better antioxidant activity expressed as increased lag-time formation, than did ethanol or methanol extracts. Curry leaf is a rich source of flavonols that have biological activity in vitro and further studies are warranted in regards to the potential health benefits and identification of the novel flavonols whose identities remain unknown.

Research highlights

► Curry leaf flavonols were extracted with acetone, methanol, and ethanol. ► Flavonols were identified and quantified by using HPLC, APCI, and LC-MS–MS. ► Curry leaf contains myricetin, quercetin, quercetin, and kaempferol glycosides. ► Curry leaf contains kaempferol and quercetin aglycones. ► Extraction solvent affects curry flavonol profile and LDL antioxidant activity.


Science Fair Project on Turmeric

Do you want to create an amazing science fair project for your next exhibition? You are in the right place. Read the below given article to get a complete idea on turmeric: 1. History of Turmeric 2. Cultivation of Turmeric 3. Curing 4. Uses.

Science Fair Project # 1. History of Turmeric:

Curcuma domestica Valet Syn. C. longa Auct. non Linn. English—Turmeric Hindi—Haldi, Bengali—Halud Punjabi—Haldar, halja’, Tamil—Manjal Telugu—Pasupu Malayalam— Mannal, marinalu, Kannada—Anshina Marathi—Halede Gujarati—Halada Sanskrit—Haridra, nisa Persian—Zard-chobah, dar-zard Family—Zingiberaceae.

Turmeric has been cultivated in India from very ancient times. It prefers sandy and clayey loams for its cultivation. The crop cannot stand water-logging or alkalinity in the soils. The largest supplies of turmeric are obtained from Guntur district of Andhra Pradesh. Orissa is the next important growing area for turmeric where production is concentrated in the districts of Ganjam, Phulbani and Koraput.

In Maharashtra, the main centres of turmeric production are in Gujarat, Thane and Khandesh districts. Tiruchirapally, Salem and Coimbatore districts of Tamil Nadu are also important turmeric growing areas. Other important states for this crop are-Uttar Pradesh, Madhya Pradesh, Karnataka, West Bengal, Rajasthan and the Punjab.

The total average under turmeric in India has been estimated variously from 60,000 to 100,000 acres, and the production is nearly 100,000 tonnes of rhizomes per annum. A large part is consumed within the country, but a portion is exported to the U.K., Pakistan, Sri Lanka and U.S.A.

Science Fair Project # 2. Cultivation of Turmeric:

The crop is propagated vegetatively by means of corms (swollen under-ground stems). The preparatory cultivation requires deep ploughing several times (six time or so).

It needs a fine tilth and heavy application of manure. The field is prepared into narrow beds with facilities for irrigation and drainage. The corms are planted from April to July in these beds, 6-9 inches apart in the furrows and 16 inches apart between the furrows.

After planting the beds are levelled and covered with a mulch of leaves. The corms develop aerial shoots above the ground in a month or so. One or two weeding’s are given, and the beds are earthed up. By November, the leafy growth is complete and the corms beneath the soil begin to thicken and to develop uniformly deep colour.

In the month of February the leaves turn yellow and dry up, which is an indication of maturity of the underground corms. Harvesting is done in March which continues till the end of April.

A great care has to be taken in harvesting operations. The whole clump consisting of both primary and secondary branches known as “fingers”, and the main thickened portion, the ”bulb”, are to be lifted up without injuring the corms.

The leaves and roots are then cut off, and the bulb and fingers separated from each other. Very small quantities are sold in this raw form. In India, the bulb of the crop is marketed as dry cured turmeric (haldi).

Science Fair Project # 3. Curing with Turmeric:

The raw produce of turmeric has to be cured properly before the commercial dry turmeric can be obtained. Curing consists mainly of three phases – 1. boiling, 2. drying and 3. polishing. After harvesting, the raw green turmeric is heaped up covered with turmeric leaves, and kept in this condition for some time.

The entire produce is then transferred to an earthen pot or larger iron pan which is filled up with water, the water level is kept 2-3 inches above the level of the turmeric. After covering the bulk with dry turmeric leaves, it is boiled over fire. As soon as the rhizomes become soft to touch, they are removed from the vessel, thinly spread out and dried in the sun.

After 5-7 days of drying, the produce becomes fit for sale and storage. When it is quite dry, it is cleaned to remove roots and other parts, and then rubbed well between hands. The dry turmeric is also polished by special appliances. Now the produce is sorted out into bulbs, fingers and splits, and graded into large and small sizes according to need.

The plant of turmeric is a robust perennial with a short stem and tufted leaves. The pale- yellow flowers are found in dense spikes, topped by a tuft of pinkish bracts. The rhizomes, which yield the colourful condiment, are short and thick with blunt tubers. They are cleaned, washed and dried in the sun, it is very aromatic, with a musky odour and yellow colour. It has a pungent bitter taste.


Just some little tips that I think would help you get started -

  1. Most curries are based on Onion and Tomato. A generic recipe would be - "Pour a little oil in a frying pan. Add spices till they start to crackle. Add chopped onions and saute till golden brown. Add chopped tomatoes and saute for a few minutes. Add dry spices/powders. Add vegetables/chicken/meat and cook". This is the most basic Indian recipe, and others build from here.
  2. Ginger Garlic paste is readily available, and is handy when you don't want to peel and crush garlic cloves.
  3. Garam Masala powder is always added last
  4. India is a huge country, and every region has its own distinct flavour. In general, North and South Indian food are totally different. The curries usually come from Punjab in North India, so searching for "Punjabi Recipes" is likely to get you better results. The most popular South Indian dishes are "Idlis" and "Dosas".

I would think the place to start is with a good book. Your questions about spices and equipment should be covered there.

At our house, we like cookbooks by Madhur Jaffrey. She has a quick and easy one that's really good, and makes it possible to make an after-work dinner that tastes like you cooked it all day (though you'll need a pressure cooker for that kind of speed). She has a bunch of others, though (her first came out in the early 70s), including two or three James Beard award-winners. I think she'd be a great place to start.

In my experience, standard kitchen equipment is all you'll need if you're not going to get into building a real tandoor oven or something crazy.

I enjoyed this book a lot.

It's clearly a short introductory book with nice tips and techniques and every recipe is a flawless winner.

Also, (important to me) the recipes has good photographs that guide you on the appearance of the dish . sometimes when cooking something I never saw before, I keep thinking .."should this be like so, or is overcooked? . Is this the supposed shape of hungarian tagliatelle :) ? . etc.

Look for a local company that sells bulk spices.

Spices can get expensive and for some dishes you often use just a small amount. In Indian cuisine, you often toast the whole spices first, then either grind the spices or leave whole in some dishes. Look for a good spice grinder (a coffee grinder works as well). Some of the common spices are: cumin seed, coriander seeds, black mustard seeds, nigella seeds, cardamom pod, fenugreek, saffron or turmeric.

There are several simple basics to Indian cooking. One is to remember that each dish (sabhji) is usually based around 1 lentil/bean or two vegetables. The second is to remember that anything with lentils or beans is for long cooking. Indian food requires patience.

Aside from that, there are several things that you can only really learn from making food and making mistakes. Cumin goes in at the start with the onions and hot oil. Turmeric only goes in with the liquids.

There is also a basic ratio of spices, but it's not easy to remember which goes where. The ratio is 4:2:1, more or less. Cumin, mustard, salt and black pepper go in the first category. Turmeric, curry, chilli and coriander seed go in the second. Cloves, cardamom, and cinnamon are in the third.

The best advice is to read ten different recipes for anything, and then choose what seems best.


THE BEST SPIKELESS SHOES 2021 - RESULTS

ProductStabilityComfortElementsTractionTotal
Adidas Tour 360 XT-SL TEX

Best Spikeless Shoes of 2021 – FAQ

Q: How much should I spend on a shoe?

A: While it’s possible to find a well-designed, fully featured golf shoe for around $80, the majority of top performers sell for around $150. Golfers who play just a few times a year may be able to find a suitable option for less. Never skimp on comfort to save a buck.

Q: What is the main feature I should look for when buying a spikeless shoe?

A: Comfort is by far the most important factor, followed by traction. Stability is also an important consideration but different golfers require different levels of stability. Only after you have those three considerations covered should style factor into the decision.

Q: Is BOA/DISC technology better than laces?

A: Use of BOA and DISC technology is less prevalent in spikeless designs. Some golfers prefer modern closure systems to traditional laces but it’s certainly not a universal preference. Users of BOA and DISC report a tendency for their shoes to loosen throughout a round. Although it’s not a big deal to re-tighten, who wants to worry about it? Also consider that if a shoelace breaks, it’s easily replaceable whereas warranty replacements for other closure systems can take some time.


Quantitative Chiral Analysis by Molecular Rotational Spectroscopy

Brooks H. Pate , . Melanie Schnell , in Chiral Analysis (Second Edition) , 2018

17.4.1 An example—the predominant enantiomer of menthone in buchu oil

The potential for chiral analysis by rotational spectroscopy performed directly on complex chemical mixtures is illustrated by the determination of the dominant configuration of menthone in a commercial sample of buchu oil ( betulina). The rotational spectrum of the volatile species in buchu oil is obtained using a head space sampling technique where the buchu oil is heated to 65 o C and the vapor over the sample is entrained in the neon gas flow for injection into the spectrometer. The broadband rotational spectrum of the vapor over the buchu oil is shown in Fig. 17.16 . The expanded scale section of the spectrum shows the instrument noise level and gives an idea of the transition line density in the measurement. The rotational spectra of 15 different known components of buchu oil have been identified in this spectrum. Using the results from GC–MS analysis of buchu oil samples, these species have 0.06%–22% relative abundance in the oil [89,90] . Given the transition density of the spectrum, a chiral tag approach to sample analysis would seem impossible. A major advantage of three-wave mixing approaches is that they can be applied without increasing the spectral complexity.

Figure 17.16 . The extension of three-wave mixing measurements to complex chemical mixtures is illustrated using buchu oil as the sample.

The broadband spectrum of the head space vapor over the oil sample is shown. Fifteen different molecular components of the oil are detected from this spectrum. The bottom panel shows an expanded scale of the spectrum to show the instrument noise floor (red line) and to show that the measured spectrum is still completely spectrally resolved.

The component of interest in this example is menthone which makes up 10% of the buchu oil. The rotational spectrum of menthone has been previously analyzed and it is known to exist in three conformational isomers in the pulsed jet expansion. The simulated spectra of these three isomers using the reported fitted rotational constants [65] are shown in Fig. 17.17 to indicate the presence and transition intensity of menthone in the head space measurement.

Figure 17.17 . Menthone is one of the components of buchu oil and makes up about 10% of the mixture of volatiles.

This figure shows spectral simulations of three conformers (A, B, and C) of menthone compared to the buchu oil broadband rotational spectrum. The spectrum simulations used the experimental fitted constants from Ref. [65] . This comparison illustrates an important feature of rotational spectroscopy. Instruments all use a high-accuracy time standard (Rb-disciplined quartz oscillators and the 1 pps GPS reference are the most common time base references) so that the measured transition frequencies reproduce from instrument-to-instrument to very high accuracy. This feature makes the use of previously measured library spectra very powerful in the analysis of complex chemical mixtures by rotational spectroscopy.

The determination of the dominant enantiomer of menthone is made using three-wave mixing rotational spectroscopy. The spectrometer used in this measurement is described in Ref. [91] . The transition cycle used in the measurement is shown in Fig. 17.18 . The phase of the chiral three-wave signal is calibrated using a commercial sample of (−)-menthone with 98.8 EE. The three-wave pulse sequence is then applied to head space sample and the results are shown in Fig. 17.18 . The first pulse of the cycle (5059.36 MHz) uses an a-type transition to create the initial sample polarization. The spectrum observed after application of just this pulse is compared to the full broadband spectrum in the top of Fig. 17.18 . Several transitions, including the one for the menthone measurement cycle, are observed. These additional transitions are excited by the bandwidth of the first excitation pulse.

Figure 17.18 . This figure shows the three-wave mixing measurement performed on the buchu oil sample.

The level diagram for the measurement cycle is shown on the left. The middle panel shows the spectrum of buchu oil after application of the first drive pulse of the three-wave mixing sequence. In this case, several nearby peaks are observed in addition to the menthone peak (indicated with the asterisk). These transitions fall within the spectral bandwidth of the drive pulse. The spectrum in the region of the chiral sum-frequency transition after the application of the low frequency coherence transfer pulse is shown on the right. In this case, the double-resonance nature of the measurement has provided full chemical selectivity and only the chiral sum-frequency signal is observed.

The enantiomer-sensitive three-wave measurement is completed by applying the low-frequency pulse (854.69 MHz) using a c-type transition to transfer the initial coherence into the detected transition (at the sum frequency: 5914.05 MHz). The spectrum in the region of the detected sum frequency signal at 5914.05 MHz, a strong b-type transition, is shown in the bottom panel where it is also compared to the full spectrum from the buchu oil head space vapor. The ability of the doubly-resonant three-wave mixing pulse sequence to isolate the chiral response for a single component (menthone) in a complex mixture is demonstrated.

The determination of the dominant enantiomer of menthone present in buchu oil is obtained from the phase of the chiral signal at 5914.05 MHz. The digitally filtered FID signal in a 1 MHz bandwidth around 5914.05 MHz is shown in Fig. 17.19 . The bottom panel shows an expanded scale where the digitized signal can be clearly seen. There are three phase measurements shown here. Two of them are from the (−)–menthone commercial reference sample and were taken before (red) and after (green) the buchu oil measurement. These show that there is long term phase stability in the instrument. The measurement of the phase of the menthone chiral signal in buchu oil (blue) is out-of-phase with the reference measurement and indicates that the sample has (+)-menthone as the dominant enantiomer—as is known for this essential oil [91] . Note that these time-domain signals have been renormalized so that they can be compared and that the buchu oil measurement has lower signal-to-noise ratio than the reference sample measurements due to its 10% abundance in the oil.

Figure 17.19 . The absolute configuration of the higher-abundance enantiomer of menthone in buchu oil is determined by comparison of the phase of the three-wave mixing signal to a reference measurement using a commercial sample of (−)-menthone with high enantiopurity.

In this case, the signal from the menthone in buchu oil is found to be out-of-phase with respect to the reference measurement showing that (+)-menthone is the dominant enantiomer in the essential oil.


What Are The Available Treatments For Hair Loss?

Treatment for hair loss may include:

  • Medications like minoxidil (Rogaine) that is approved for both men and women, finasteride (Propecia) for men, and other drugs like spironolactone and oral contraceptives for women.
  • Hair transplant surgery or restoration surgery that includes taking skin patches with multiple hair follicles and implanting them onto bald patches.
  • Laser therapy to improve hair density.

While these treatments may help you deal with hair loss, there is a high chance of recurrence if the cause is hereditary. Also, most of the medications used to treat hair loss come with side effects like reduced libido, scalp irritation, and an increased risk of prostate cancer in men. The other treatment methods like hair transplant surgery and laser therapy may be heavy on your pocket and may have side effects like scarring.

Hence, instead of investing your time and money in such treatments, if you have mild hair fall, it is better to opt for natural alternatives that are completely safe for your scalp and skin. Listed below are some excellent home remedies that are proven to help with hair fall.


14 Mosquito Repellent Plants

Many of these plants are aromatic. For example, lavender emits a delicious scent to humans that evokes a sense of relaxation, but mosquitoes find the smell repulsive.

1. Basil

It’s hard not to love basil it gives us delicious pesto sauce and tomato basil salads. While being a top culinary herb, basil also keeps mosquitoes away like a boss.

As you already know, basil is highly aromatic, and its aroma drives the mosquitoes away. You don’t need to crush up the leaves or prepare them in any way. The scent alone is all that is required. Also, basil is toxic to mosquito larvae, so put one or two plants near areas that typically have standing water to stop mosquitoes from laying eggs.

2. Lavender

Lavender is a beloved herb due to its pleasant scent. You might love to smell lotion or candles that contain lavender after a long day at work. Lavender plants also drive mosquitoes far away at the same time. It also keeps other flying pests, such as moths, fleas, flies, and spiders at bay.

Lavender attracts butterflies and bees to your garden. You can apply lavender directly to your skin. Try using lavender oil on your body before you go to sleep because it not only helps mosquitos away, but it can deter bed bugs as well.

3. Bee Balm

You might recognize this plant by the name of wild bergamot and horsemint. It’s a natural mosquito-repelling plant that attracts all of the bees and butterflies to your yard, along with hummingbirds. Bee balm is typically used in jellies, teas, and garnishments for salads.

Planting bee balm also adds some pretty color to your yard. Medicinally, it’s safe for your skin, and it’s useful as an oil. You also can dry the leaves to make tea to fight off fungal infections.

4. Lemon Balm

Instead of bee balm, you can plant lemon balm in your garden beds. This member of the mint family is often used to help reduce stress, alleviate stomach trouble, and more. Not only does this ornamental herb taste great, but it also helps to fight off mosquitoes as well as fleas.

Be sure to keep lemon balm contained because it’s an invasive species that, like mint, can take over your garden bed when planted. Plant lemon balm in containers so that you can reap the benefits without it taking over your entire garden.

5. Lemongrass

Lemongrass has a high level of citral, which is an oil that is used in mosquito repellents. You can use it to repel flies while being toxic to mosquito larvae. Of course, lemongrass is also delicious in a range of dishes – from tom kha gai soup to lemongrass tea.

6. Citronella

Most people know about citronella plants. It’s most commonly found in commercial insect repellents and citronella candles. Citronella has a strong scent that masks the smell of other attractants, such as the smell of carbon dioxide coming from your body.

This plant is rather large, but it can still do well in containers. It’s low maintenance, so you don’t have to do too much work to keep away the mosquitoes. Watch out for frost because this plant will die if the temperatures drop too low.

7. Peppermint

Mint is known to overtake a garden bed quickly, so it’s best if you keep peppermint in a separate container rather than the ground itself. Peppermint oil is excellent for repelling mosquitoes, but it also can help relieve discomfort from itchy mosquito bites during the summer. This herb also helps to repel spiders.

8. Rosemary

This herb is a popular culinary seasoning that is most commonly used in chicken dishes. While it tastes great, rosemary also helps keep several different types of insects away from your family. You can burn rosemary in a fire for an aromatic insect repellent, but be careful not to get too close to the smoke. Another choice is to use rosemary oil on your skin.

9. Sage

You might recognize sage for its culinary purposes or its uses as a spiritual cleanser in different cultures. Bundles of sage are often burned in certain rituals to get rid of spirits.

Another use for sage is to burn it to keep the mosquitoes away from you. Throw some sage leaves on your backyard fire pit or in your fireplace. Not only will it fill your home with a lovely aroma as well as repelling mosquitoes from the area.

You might also want to try sage because it can repel ticks. Ticks are a danger to you and your pet’s health, so keeping them away from your family is a top priority. At the same time, sage can attract hummingbirds. You can use it as an oil on your skin if you prefer.

10. Catnip

Chances are you recognize this plant because it makes cats go crazy, but it does more than that. Catnip contains a chemical called nepetalactone, which is a mosquito repellent. It’s also the same chemical that makes our cats act like an addict looking for a quick fix.

Many people claim that catnip is more effective than DEET, which is a chemical in most insect repellents. Evidence shows us that DEET is terrible for our health, so why not use a natural alternative that works as well?

Because of its potent chemical compounds, placing a few catnip plants in your garden will keep mosquitoes away for a long time. Cats also like to rub and roll in it, so make sure you plant this plant in a cat-friendly area. Cats have no moral objections to destroying your garden beds to reach their catnip.

11. Garlic

If garlic can keep vampires away, then surely it can keep mosquitoes away as well. Their pungent smell deters most insects. You can consume garlic to create a mild effect that is reported to help repel mosquitoes.

Another choice is to squeeze or rub the juice from the garlic bulbs directly onto your skin. That might keep mosquitoes away, but it also might keep your friends and family away as well.

12. Floss Flower

Floss flowers – also known as Mexican paintbrush or blueweed – are often overlooked, but they contain a chemical called coumarin, which is used in mosquito repellents. They’re fantastic additions to your garden bed because of the funky fuzzy flowers. It adds a unique addition to your flower bed or as an edging plant. You can find floss flowers in blue, pink, white, and purple.

These flowers also deter flies, rabbits, and deers, which all can cause severe damage in your garden beds. At the same time, floss flowers attract butterflies and hummingbirds both beneficial pollinators. However, the chemical isn’t safe for your skin, so don’t try to rub them on your arms.

13. Marigold

Most garden beds contain some marigolds because they’re a popular edging plant for landscaping and vegetable gardens. Marigolds are an annual flower with a strong fragrance that tastes great in salads, herb butters, and soups because of their light and citrusy taste.

The reason why marigolds work to deter mosquitoes is that they contain pyrethrum. That is a compound used in many repellents, sometimes referred to as nature’s insecticide. Pyrethrum repels deer and rabbis while also attracting butterflies and bees. Marigolds are also safe for the skin.

14. Geraniums

Geraniums are another flower that has a slight lemon scent, and it can be used to keep many different pests away from your home and garden. They are a mosquito repellent plant and they also repel flies. Geraniums have beautiful, large blooms in many different vibrant colors that make them perfect for decorating and landscaping.

Scented geraniums contain small amounts of citronella, so that helps deter mosquitos even more. At the same time, the scent can attract butterflies to your garden, which are helpful pollinators for other flowers and plants.


References

Crichton, R. in Iron Metabolism: from Molecular Mechanisms to Cinical Consequences 17–58 (John Wiley and Sons, 2009).

Inoue, S. & Kawanishi, S. Hydroxyl radical production and human DNA damage induced by ferric nitrilotriacetate and hydrogen peroxide. Cancer Res. 47, 6522–6527 (1987).

Dizdaroglu, M., Rao, G., Halliwell, B. & Gajewski, E. Damage to the DNA bases in mammalian chromatin by hydrogen peroxide in the presence of ferric and cupric ions. Arch. Biochem. Biophys. 285, 317–324 (1991).

Dizdaroglu, M. & Jaruga, P. Mechanisms of free radical-induced damage to DNA. Free Radic. Res. 46, 382–419 (2012).

Campbell, J. A. Effects of precipitated silica and of iron oxide on the incidence of primary lung tumours in mice. Br. Med. J. 2, 275–280 (1940).

Richmond, H. G. Induction of sarcoma in the rat by iron-dextran complex. Br. Med. J. 1, 947–949 (1959).

Hann, H. W., Stahlhut, M. W. & Blumberg, B. S. Iron nutrition and tumor growth: decreased tumor growth in iron-deficient mice. Cancer Res. 48, 4168–4170 (1988).

Hann, H. W., Stahlhut, M. W. & Menduke, H. Iron enhances tumor growth. Observation on spontaneous mammary tumors in mice. Cancer 68, 2407–2410 (1991).

Stevens, R. G., Graubard, B. I., Micozzi, M. S., Neriishi, K. & Blumberg, B. S. Moderate elevation of body iron level and increased risk of cancer occurrence and death. Int. J. Cancer 56, 364–369 (1994).

Stevens, R. G., Jones, D. Y., Micozzi, M. S. & Taylor, P. R. Body iron stores and the risk of cancer. New Engl. J. Med. 319, 1047–1052 (1988).

van Asperen, I. A., Feskens, E. J., Bowles, C. H. & Kromhout, D. Body iron stores and mortality due to cancer and ischaemic heart disease: a 17-year follow-up study of elderly men and women. Int. J. Epidemiol. 24, 665–670 (1995).

Knekt, P. et al. Body iron stores and risk of cancer. Int. J. Cancer 56, 379–382 (1994).

Wu, T., Sempos, C. T., Freudenheim, J. L., Muti, P. & Smit, E. Serum iron, copper and zinc concentrations and risk of cancer mortality in US adults. Ann. Epidemiol. 14, 195–201 (2004).

Nelson, R. L. Iron and colorectal cancer risk: human studies. Nutr. Rev. 59, 140–148 (2001).

Kabat, G. C., Miller, A. B., Jain, M. & Rohan, T. E. Dietary iron and haem iron intake and risk of endometrial cancer: a prospective cohort study. Br. J. Cancer 98, 194–198 (2008).

Mursu, J., Robien, K., Harnack, L. J., Park, K. & Jacobs, D. R. Jr. Dietary supplements and mortality rate in older women: the Iowa Women's Health Study. Arch. Intern. Med. 171, 1625–1633 (2011).

Ward, M. H. et al. Heme iron from meat and risk of adenocarcinoma of the esophagus and stomach. Eur. J. Cancer Prev. 21, 134–138 (2012).

Cross, A. J., Pollock, J. R. & Bingham, S. A. Haem, not protein or inorganic iron, is responsible for endogenous intestinal N-nitrosation arising from red meat. Cancer Res. 63, 2358–2360 (2003).

Choi, J. Y. et al. Iron intake, oxidative stress-related genes (MnSOD and MPO) and prostate cancer risk in CARET cohort. Carcinogenesis 29, 964–970 (2008).

Hong, C. C. et al. Genetic variability in iron-related oxidative stress pathways (Nrf2, NQ01, NOS3, and HO-1), iron intake, and risk of postmenopausal breast cancer. Cancer Epidemiol. Biomarkers Prev. 16, 1784–1794 (2007).

Pietrangelo, A. Hereditary hemochromatosis: pathogenesis, diagnosis, and treatment. Gastroenterology 139, 393–408 (2010).

Bradbear, R. A. et al. Cohort study of internal malignancy in genetic hemochromatosis and other chronic nonalcoholic liver diseases. J. Natl Cancer Inst. 75, 81–84 (1985).

Milman, N. et al. Clinically overt hereditary hemochromatosis in Denmark 1948-1985: epidemiology, factors of significance for long-term survival, and causes of death in 179 patients. Ann. Hematol. 80, 737–744 (2001).

Elmberg, M. et al. Cancer risk in patients with hereditary hemochromatosis and in their first-degree relatives. Gastroenterology 125, 1733–1741 (2003).

Niederau, C. et al. Survival and causes of death in cirrhotic and in noncirrhotic patients with primary hemochromatosis. N. Engl. J. Med. 313, 1256–1262 (1985).

Hsing, A. W. et al. Cancer risk following primary hemochromatosis: a population-based cohort study in Denmark. Int. J. Cancer 60, 160–162 (1995).

Osborne, N. J. et al. HFE C282Y homozygotes are at increased risk of breast and colorectal cancer. Hepatology 51, 1311–1318 (2010).

Edgren, G. et al. Donation frequency, iron loss, and risk of cancer among blood donors. J. Natl Cancer Inst. 100, 572–579 (2008).

Andrews, N. C. Forging a field: the golden age of iron biology. Blood 112, 219–230 (2008). Excellent overall review of recent advances in iron biology.

Daniels, T. R. et al. The transferrin receptor and the targeted delivery of therapeutic agents against cancer. Biochim. Biophys. Acta 1820, 291–317 (2012). Summary of past and current strategies used to target TFR1 for anticancer therapy.

Brooks, D. et al. Phase Ia trial of murine immunoglobulin A antitransferrin receptor antibody 42/6. Clin. Cancer Res. 1, 1259–1265 (1995).

Taetle, R., Castagnola, J. & Mendelsohn, J. Mechanisms of growth inhibition by anti-transferrin receptor monoclonal antibodies. Cancer Res. 46, 1759–1763 (1986).

Ohgami, R. S. et al. Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Nature Genet. 37, 1264–1269 (2005).

Knutson, M. D. Steap proteins: implications for iron and copper metabolism. Nutr. Rev. 65, 335–340 (2007).

Leng, X., Wu, Y. & Arlinghaus, R. B. Relationships of lipocalin 2 with breast tumorigenesis and metastasis. J. Cell. Physiol. 226, 309–314 (2011).

Zhang, Y., Fan, Y. & Mei, Z. NGAL and NGALR overexpression in human hepatocellular carcinoma toward a molecular prognostic classification. Cancer Epidemiol. 36, e294–e299 (2012).

Leung, L. et al. Lipocalin2 promotes invasion, tumorigenicity and gemcitabine resistance in pancreatic ductal adenocarcinoma. PLoS ONE 7, e46677 (2012).

Saha, R., Saha, N., Donofrio, R. S. & Bestervelt, L. L. Microbial siderophores: a mini review. J. Basic Microbiol. 26 Jun 2012 (doi:10.1002/jobm.201100552).

Bao, G. et al. Iron traffics in circulation bound to a siderocalin (Ngal)-catechol complex. Nature Chem. Biol. 6, 602–609 (2010).

Devireddy, L. R., Hart, D. O., Goetz, D. H. & Green, M. R. A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production. Cell 141, 1006–1017 (2010). References 39 and 40 were the first to identify endogenous mammalian siderophores.

Fernandez, C. A. et al. The matrix metalloproteinase-9/neutrophil gelatinase-associated lipocalin complex plays a role in breast tumor growth and is present in the urine of breast cancer patients. Clin. Cancer Res. 11, 5390–5395 (2005).

Yang, J., McNeish, B., Butterfield, C. & Moses, M. A. Lipocalin 2 is a novel regulator of angiogenesis in human breast cancer. FASEB J 27, 45–50 (2012).

Berger, T., Cheung, C. C., Elia, A. J. & Mak, T. W. Disruption of the Lcn2 gene in mice suppresses primary mammary tumor formation but does not decrease lung metastasis. Proc. Natl Acad. Sci. USA 107, 2995–3000 (2010).

Cramer, E. P. et al. No effect of NGAL/lipocalin-2 on aggressiveness of cancer in the MMTV-PyMT/FVB/N mouse model for breast cancer. PLoS ONE 7, e39646 (2012).

Lee, H. J. et al. Ectopic expression of neutrophil gelatinase-associated lipocalin suppresses the invasion and liver metastasis of colon cancer cells. Int. J. Cancer 118, 2490–2497 (2006).

Sun, Y. et al. NGAL expression is elevated in both colorectal adenoma-carcinoma sequence and cancer progression and enhances tumorigenesis in xenograft mouse models. Clin. Cancer Res. 17, 4331–4340 (2011).

Bauer, M. et al. Neutrophil gelatinase-associated lipocalin (NGAL) is a predictor of poor prognosis in human primary breast cancer. Breast Cancer Res. Treat. 108, 389–397 (2008).

Wenners, A. S. et al. Neutrophil gelatinase-associated lipocalin (NGAL) predicts response to neoadjuvant chemotherapy and clinical outcome in primary human breast cancer. PLoS ONE 7, e45826 (2012).

Wu, K. J., Polack, A. & Dalla-Favera, R. Coordinated regulation of iron-controlling genes, H-ferritin and IRP2, by c-MYC. Science 283, 676–679 (1999).

Radulescu, S. et al. Luminal iron levels govern intestinal tumorigenesis after apc loss in vivo. Cell Rep. 2, 270–282 (2012). This paper provides a mechanistic explanation of how excess iron contributes to intestinal tumorigenesis.

Tsuji, Y., Kwak, E., Saika, T., Torti, S. V. & Torti, F. M. Preferential repression of the H subunit of ferritin by adenovirus E1A in NIH-3T3 mouse fibroblasts. J. Biol. Chem. 268, 7270–7275 (1993).

Kakhlon, O., Gruenbaum, Y. & Cabantchik, Z. I. Repression of ferritin expression modulates cell responsiveness to H-ras-induced growth. Biochem. Soc. Trans. 30, 777–780 (2002).

Kakhlon, O., Gruenbaum, Y. & Cabantchik, Z. I. Ferritin expression modulates cell cycle dynamics and cell responsiveness to H-ras-induced growth via expansion of the labile iron pool. Biochem. J. 363, 431–436 (2002).

Zhang, F., Wang, W., Tsuji, Y., Torti, S. V. & Torti, F. M. Post-transcriptional modulation of iron homeostasis during p53-dependent growth arrest. J. Biol. Chem. 283, 33911–33918 (2008).

Tong, W. H. et al. The glycolytic shift in fumarate-hydratase-deficient kidney cancer lowers AMPK levels, increases anabolic propensities and lowers cellular iron levels. Cancer Cell 20, 315–327 (2011).

Shpyleva, S. I. et al. Role of ferritin alterations in human breast cancer cells. Breast Cancer Res. Treat. 126, 63–71 (2011).

Liu, X. et al. Heavy chain ferritin siRNA delivered by cationic liposomes increases sensitivity of cancer cells to chemotherapeutic agents. Cancer Res. 71, 2240–2249 (2011).

Karin, M. Nuclear factor-κB in cancer development and progression. Nature 441, 431–436 (2006).

Torti, S. V. et al. The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene. J. Biol. Chem. 263, 12638–12644 (1988).

Kwak, E. L., Larochelle, D. A., Beaumont, C., Torti, S. V. & Torti, F. M. Role for NF-kappa B in the regulation of ferritin H by tumor necrosis factor-alpha. J. Biol. Chem. 270, 15285–15293 (1995).

Pham, C. G. et al. Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species. Cell 119, 529–542 (2004).

Ruddell, R. G. et al. Ferritin functions as a proinflammatory cytokine via iron-independent protein kinase C zeta/nuclear factor kappaB-regulated signaling in rat hepatic stellate cells. Hepatology 49, 887–900 (2009).

Alkhateeb, A. A., Han, B. & Connor, J. R. Ferritin stimulates breast cancer cells through an iron-independent mechanism and is localized within tumor-associated macrophages. Breast Cancer Res. Treat. 137, 733–744 (2013).

Cortes, D. F. et al. Differential gene expression in normal and transformed human mammary epithelial cells in response to oxidative stress. Free Radic. Biol. Med. 50, 1565–1574 (2011).

Nemeth, E. et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306, 2090–2093 (2004). Ground-breaking study demonstrating that hepcidin binds to ferroportin and triggers its degradation.

Ganz, T. & Nemeth, E. Hepcidin and iron homeostasis. Biochim. Biophys. Acta 1823, 1434–1443 (2012).

Ward, D. M. & Kaplan, J. Ferroportin-mediated iron transport: expression and regulation. Biochim. Biophys. Acta 1823, 1426–1433 (2012).

Lonnerdal, B. Trace element transport in the mammary gland. Annu. Rev. Nutr. 27, 165–177 (2007).

Pinnix, Z. K. et al. Ferroportin and iron regulation in breast cancer progression and prognosis. Sci Transl Med 2, 43ra56 (2010). This paper demonstrates that levels of ferroportin affect breast cancer cell growth, are altered in patients with breast cancer and affect the prognosis of patients with breast cancer.

Jiang, X. P., Elliott, R. L. & Head, J. F. Manipulation of iron transporter genes results in the suppression of human and mouse mammary adenocarcinomas. Anticancer Res. 30, 759–765 (2010).

Miller, L. D. et al. An iron regulatory gene signature predicts outcome in breast cancer. Cancer Res. 71, 6728–6737 (2011).

Weiss, G. & Goodnough, L. T. Anemia of chronic disease. N. Engl. J. Med. 352, 1011–1023 (2005).

Weinberg, E. D. & Miklossy, J. Iron withholding: a defense against disease. J. Alzheimers Dis. 13, 451–463 (2008).

Weinberg, E. D. Iron withholding: a defense against infection and neoplasia. Physiol. Rev. 64, 65–102 (1984).

Maes, K. et al. In anemia of multiple myeloma, hepcidin is induced by increased bone morphogenetic protein 2. Blood 116, 3635–3644 (2010).

Hohaus, S. et al. Anemia in Hodgkin's lymphoma: the role of interleukin-6 and hepcidin. J. Clin. Oncol. 28, 2538–2543 (2010).

Hubert, N. & Hentze, M. W. Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl Acad. Sci. USA 99, 12345–12350 (2002).

Galy, B., Ferring-Appel, D., Kaden, S., Grone, H. J. & Hentze, M. W. Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum. Cell. Metab. 7, 79–85 (2008).

Maffettone, C., Chen, G., Drozdov, I., Ouzounis, C. & Pantopoulos, K. Tumorigenic properties of iron regulatory protein 2 (IRP2) mediated by its specific 73-amino acids insert. PLoS ONE 5, e10163 (2010). This work suggests that IRPs can modify tumour growth in ways that are independent of their effects on iron metabolism.

Chen, G., Fillebeen, C., Wang, J. & Pantopoulos, K. Overexpression of iron regulatory protein 1 suppresses growth of tumor xenografts. Carcinogenesis 28, 785–791 (2007).

Mantovani, A., Allavena, P., Sica, A. & Balkwill, F. Cancer-related inflammation. Nature 454, 436–444 (2008).

Recalcati, S. et al. Differential regulation of iron homeostasis during human macrophage polarized activation. Eur. J. Immunol. 40, 824–835 (2010).

Corna, G. et al. Polarization dictates iron handling by inflammatory and alternatively activated macrophages. Haematologica 95, 1814–1822 (2010).

Cohen, L. A. et al. Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway. Blood 116, 1574–1584 (2010).

Han, J. et al. Iron uptake mediated by binding of H-ferritin to the TIM-2 receptor in mouse cells. PLoS ONE 6, e23800 (2011).

Li, L. et al. Binding and uptake of H-ferritin are mediated by human transferrin receptor-1. Proc. Natl Acad. Sci. USA 107, 3505–3510 (2010).

Coffman, L. G. et al. Regulatory effects of ferritin on angiogenesis. Proc. Natl Acad. Sci. USA 106, 570–575 (2009). This paper demonstrates that extracellular ferritin can antagonize the activity of endogenous antiangiogenic proteins.

Tesfay, L., Huhn, A. J., Hatcher, H., Torti, F. M. & Torti, S. V. Ferritin blocks inhibitory effects of two-chain high molecular weight kininogen (HKa) on adhesion and survival signaling in endothelial cells. PLoS ONE 7, e40030 (2012).

Ackroyd, R., Shorthouse, A. J. & Stephenson, T. J. Gastric carcinoma in siblings with Friedreich's ataxia. Eur. J. Surg. Oncol. 22, 301–303 (1996).

Kidd, A. et al. Breast cancer in two sisters with Friedreich's ataxia. Eur. J. Surg. Oncol. 27, 512–514 (2001).

Lill, R. et al. The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism. Biochim. Biophys. Acta 1823, 1491–1508 (2012). Review of recent advances in mechanisms of iron–sulphur cluster biogenesis.

Babcock, M. et al. Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. Science 276, 1709–1712 (1997).

Shoichet, S. A. et al. Frataxin promotes antioxidant defense in a thiol-dependent manner resulting in diminished malignant transformation in vitro. Hum. Mol. Genet. 11, 815–821 (2002).

Thierbach, R. et al. Targeted disruption of hepatic frataxin expression causes impaired mitochondrial function, decreased life span and tumor growth in mice. Hum. Mol. Genet. 14, 3857–3864 (2005).

Schulz, T. J. et al. Induction of oxidative metabolism by mitochondrial frataxin inhibits cancer growth: Otto Warburg revisited. J. Biol. Chem. 281, 977–981 (2006).

Thierbach, R. et al. The Friedreich's ataxia protein frataxin modulates DNA base excision repair in prokaryotes and mammals. Biochem. J. 432, 165–172 (2010).

Keith, B., Johnson, R. S. & Simon, M. C. HIF1alpha and HIF2alpha: sibling rivalry in hypoxic tumour growth and progression. Nature Rev. Cancer 12, 9–22 (2012).

Semenza, G. L. HIF-1: upstream and downstream of cancer metabolism. Curr. Opin. Genet. Dev. 20, 51–56 (2010).

Wang, G. L. & Semenza, G. L. Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction. Blood 82, 3610–3615 (1993).

Tacchini, L., Bianchi, L., Bernelli-Zazzera, A. & Cairo, G. Transferrin receptor induction by hypoxia. HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation. J. Biol. Chem. 274, 24142–24146 (1999).

Lok, C. N. & Ponka, P. Identification of a hypoxia response element in the transferrin receptor gene. J. Biol. Chem. 274, 24147–24152 (1999).

Lee, P. J. et al. Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia. J. Biol. Chem. 272, 5375–5381 (1997).

Mukhopadhyay, C. K., Mazumder, B. & Fox, P. L. Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency. J. Biol. Chem. 275, 21048–21054 (2000).

Peyssonnaux, C. et al. Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs). J. Clin. Invest. 117, 1926–1932 (2007).

Mastrogiannaki, M. et al. HIF-2alpha, but not HIF-1alpha, promotes iron absorption in mice. J. Clin. Invest. 119, 1159–1166 (2009). This paper demonstrates the role of HIF2α in iron absorption.

Shah, Y. M., Matsubara, T., Ito, S., Yim, S. H. & Gonzalez, F. J. Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency. Cell. Metab. 9, 152–164 (2009).

Xue, X. et al. Hypoxia-inducible factor-2alpha activation promotes colorectal cancer progression by dysregulating iron homeostasis. Cancer Res. 72, 2285–2293 (2012).

Terada, N., Or, R., Szepesi, A., Lucas, J. J. & Gelfand, E. W. Definition of the roles for iron and essential fatty acids in cell cycle progression of normal human T lymphocytes. Exp. Cell Res. 204, 260–267 (1993).

Thelander, L. & Graslund, A. Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone. Destruction of the tyrosine free radical of the enzyme in an oxygen-requiring reaction. J. Biol. Chem. 258, 4063–4066 (1983).

Thelander, L., Graslund, A. & Thelander, M. Continual presence of oxygen and iron required for mammalian ribonucleotide reduction: possible regulation mechanism. Biochem. Biophys. Res. Commun. 110, 859–865 (1983).

Martin, L. K. et al. A dose escalation and pharmacodynamic study of triapine and radiation in patients with locally advanced pancreas cancer. Int. J. Radiat. Oncol. Biol. Phys. 84, e475–e481 (2012).

Yu, Y. et al. Iron chelators for the treatment of cancer. Curr. Med. Chem. 19, 2689–2702 (2012). Recent summary of progress and challenges in the development of iron chelators as anticancer therapeutics.

Tanaka, H. et al. A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature 404, 42–49 (2000).

Shao, J. et al. In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase. Cancer Res. 64, 1–6 (2004).

Smith, P. et al. 2.6 A X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase. Biochemistry 48, 11134–11141 (2009).

Netz, D. J. et al. Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes. Nature Chem. Biol. 8, 125–132 (2012).

Veatch, J. R., McMurray, M. A., Nelson, Z. W. & Gottschling, D. E. Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect. Cell 137, 1247–1258 (2009).

Rudolf, J., Makrantoni, V., Ingledew, W. J., Stark, M. J. R. & White, M. F. The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol. Cell 23, 801–808 (2006).

Karanja, K. K., Cox, S. W., Duxin, J. P., Stewart, S. A. & Campbell, J. L. DNA2 and EXO1 in replication-coupled, homology-directed repair and in the interplay between HDR and the FA/BRCA network. Cell Cycle 11, 3983–3996 (2012).

Barber, L. J. et al. RTEL1 maintains genomic stability by suppressing homologous recombination. Cell 135, 261–271 (2008).

Stehling, O. et al. MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity. Science 337, 195–199 (2012). Identification of MMS19 as a scaffolding protein involved in the assembly of a subset of iron–sulphur cluster-containing proteins involved in genome integrity, and demonstration of the role of this pathway in the response to DNA damage.

Lorsbach, R. B. et al. TET1, a member of a novel protein family, is fused to MLL in acute myeloid leukemia containing the t(1011)(q22q23). Leukemia 17, 637–641 (2003).

Thomson, J. et al. Non-genotoxic carcinogen exposure induces defined changes in the 5-hydroxymethylome. Genome Biol. 13, R93 (2012).

Tahiliani, M. et al. Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1. Science 324, 930–935 (2009).

Malumbres, M. & Barbacid, M. Cell cycle, CDKs and cancer: a changing paradigm. Nature Rev. Cancer 9, 153–166 (2009).

Kulp, K. S., Green, S. L. & Vulliet, P. R. Iron deprivation inhibits cyclin-dependent kinase activity and decreases cyclin D/CDK4 protein levels in asynchronous MDA-MB-453 human breast cancer cells. Exp. Cell Res. 229, 60–68 (1996).

Nurtjahja-Tjendraputra, E., Fu, D., Phang, J. M. & Richardson, D. R. Iron chelation regulates cyclin D1 expression via the proteasome: a link to iron deficiency-mediated growth suppression. Blood 109, 4045–4054 (2007).

Ornstein, D. L. & Zacharski, L. R. Iron stimulates urokinase plasminogen activator expression and activates NF-kappa B in human prostate cancer cells. Nutr. Cancer 58, 115–126 (2007).

Tsukamoto, H. Iron regulation of hepatic macrophage TNFalpha expression. Free Radic. Biol. Med. 32, 309–313 (2002).

Pang, H. et al. Crystal structure of human pirin: an iron-binding nuclear protein and transcription cofactor. J. Biol. Chem. 279, 1491–1498 (2004).

Yu, Y. & Richardson, D. R. Cellular iron depletion stimulates the JNK and p38 MAPK signaling transduction pathways, dissociation of ASK1-thioredoxin, and activation of ASK1. J. Biol. Chem. 286, 15413–15427 (2011).

Polakis, P. Wnt signaling and cancer. Genes Dev. 14, 1837–1851 (2000).

Klaus, A. & Birchmeier, W. Wnt signalling and its impact on development and cancer. Nature Rev. Cancer 8, 387–398 (2008).

Brookes, M. J. et al. A role for iron in Wnt signalling. Oncogene 27, 966–975 (2008). One of the first papers demonstrating the connection between iron and WNT signalling.

Seril, D. N. et al. Dietary iron supplementation enhances DSS-induced colitis and associated colorectal carcinoma development in mice. Dig. Dis. Sci. 47, 1266–1278 (2002).

Ilsley, J. N. et al. Dietary iron promotes azoxymethane-induced colon tumors in mice. Nutr. Cancer 49, 162–169 (2004).

Song, S. et al. Wnt inhibitor screen reveals iron dependence of beta-catenin signaling in cancers. Cancer Res. 71, 7628–7639 (2011).

Coombs, G. S. et al. Modulation of Wnt/beta-catenin signaling and proliferation by a ferrous iron chelator with therapeutic efficacy in genetically engineered mouse models of cancer. Oncogene 31, 213–225 (2012).

Ebina, Y. et al. Nephrotoxicity and renal cell carcinoma after use of iron- and aluminum-nitrilotriacetate complexes in rats. J. Natl Cancer Inst. 76, 107–113 (1986).

Hamazaki, S., Okada, S., Ebina, Y., Fujioka, M. & Midorikawa, O. Nephrotoxicity of ferric nitrilotriacetate. An electron-microscopic and metabolic study. Am. J. Pathol. 123, 343–350 (1986).

Li, J. L., Okada, S., Hamazaki, S., Ebina, Y. & Midorikawa, O. Subacute nephrotoxicity and induction of renal cell carcinoma in mice treated with ferric nitrilotriacetate. Cancer Res. 47, 1867–1869 (1987).

Toyokuni, S., Mori, T. & Dizdaroglu, M. DNA base modifications in renal chromatin of Wistar rats treated with a renal carcinogen, ferric nitrilotriacetate. Int. J. Cancer 57, 123–128 (1994).

Jiang, L. et al. Deletion and single nucleotide substitution at G.:C in the kidney of gpt delta transgenic mice after ferric nitrilotriacetate treatment. Cancer Sci. 97, 1159–1167 (2006).

Hiroyasu, M. et al. Specific allelic loss of p16 (INK4A) tumor suppressor gene after weeks of iron-mediated oxidative damage during rat renal carcinogenesis. Am. J. Pathol. 160, 419–424 (2002).

Akatsuka, S. et al. Fenton reaction induced cancer in wild type rats recapitulates genomic alterations observed in human cancer. PLoS ONE 7, e43403 (2012). This study establishes a direct connection between iron-induced genomic alterations and cancer.

Xu, Y. et al. Receptor-type protein tyrosine phosphatase beta (RPTP-beta) directly dephosphorylates and regulates hepatocyte growth factor receptor (HGFR/Met) function. J. Biol. Chem. 286, 15980–15988 (2011).

Yacyshyn, O. K. et al. Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in human endothelial cells. Angiogenesis 12, 25–33 (2009).

Estrov, Z. et al. In vitro and in vivo effects of deferoxamine in neonatal acute leukemia. Blood 69, 757–761 (1987).

Yamasaki, T., Terai, S. & Sakaida, I. Deferoxamine for advanced hepatocellular carcinoma. N. Engl. J. Med. 365, 576–578 (2011).

Hatcher, H. C., Singh, R. N., Torti, F. M. & Torti, S. V. Synthetic and natural iron chelators: therapeutic potential and clinical use. Future Med. Chem. 1, 1643–1670 (2009).

Whitnall, M., Howard, J., Ponka, P. & Richardson, D. R. A class of iron chelators with a wide spectrum of potent antitumor activity that overcomes resistance to chemotherapeutics. Proc. Natl Acad. Sci. USA 103, 14901–14906 (2006).

Melotte, V. et al. The N-myc downstream regulated gene (NDRG) family: diverse functions, multiple applications. FASEB J. 24, 4153–4166 (2010).

Chen, Z. et al. The iron chelators Dp44mT and DFO inhibit TGF-beta-induced epithelial-mesenchymal transition via up-regulation of N-Myc downstream-regulated gene 1 (NDRG1). J. Biol. Chem. 287, 17016–17028 (2012).

Crepin, R. et al. Development of human single-chain antibodies to the transferrin receptor that effectively antagonize the growth of leukemias and lymphomas. Cancer Res. 70, 5497–5506 (2010).

Hatcher, H., Planalp, R., Cho, J., Torti, F. M. & Torti, S. V. Curcumin: from ancient medicine to current clinical trials. Cell. Mol. Life Sci. 65, 1631–1652 (2008).

Jiao, Y. et al. Iron chelation in the biological activity of curcumin. Free Radic. Biol. Med. 40, 1152–1160 (2006).

Jiao, Y. et al. Curcumin, a cancer chemopreventive and chemotherapeutic agent, is a biologically active iron chelator. Blood 113, 462–469 (2009).

Lin, L. et al. Antitumor agents. 250. Design and synthesis of new curcumin analogues as potential anti-prostate cancer agents. J. Med. Chem. 49, 3963–3972 (2006).

Adams, B. K. et al. Synthesis and biological evaluation of novel curcumin analogs as anti-cancer and anti-angiogenesis agents. Bioorg. Med. Chem. 12, 3871–3883 (2004).

Chen, X. et al. Chemoprevention of 7,12-dimethylbenz[a]anthracene (DMBA)-induced hamster cheek pouch carcinogenesis by a 5-lipoxygenase inhibitor, garcinol. Nutr. Cancer 64, 1211–1218 (2012).

Hanahan, D. & Weinberg, R. A. Hallmarks of cancer: the next generation. Cell 144, 646–674 (2011).

Cozzi, A. et al. Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity. J. Biol. Chem. 275, 25122–25129 (2000).

Cozzi, A. et al. Analysis of the biologic functions of H − and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of L-ferritin. Blood 103, 2377–2383 (2004).

Wang, W., Knovich, M. A., Coffman, L. G., Torti, F. M. & Torti, S. V. Serum ferritin: Past, present and future. Biochim. Biophys. Acta 1800, 760–769 (2010).

Jezequel, P. et al. Validation of tumor-associated macrophage ferritin light chain as a prognostic biomarker in node-negative breast cancer tumors: A multicentric 2004 national PHRC study. Int. J. Cancer 131, 426–437 (2012).

Carpagnano, G. E. et al. Could exhaled ferritin and SOD be used as markers for lung cancer and prognosis prediction purposes? Eur. J. Clin. Invest. 42, 478–486 (2012).

Kim, Y. et al. Targeting the Wnt/beta-catenin pathway with the antifungal agent ciclopirox olamine in a murine myeloma model. In Vivo 25, 887–893 (2011).

Chifman, J. et al. The core control system of intracellular iron homeostasis: a mathematical model. J. Theor. Biol. 300, 91–99 (2012).

Laubenbacher, R. et al. A systems biology view of cancer. Biochim. Biophys. Acta 1796, 129–139 (2009).

Hower, V. et al. A general map of iron metabolism and tissue-specific subnetworks. Mol. Biosyst 5, 422–443 (2009).

Sanchez, M., Galy, B., Muckenthaler, M. U. & Hentze, M. W. Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency. Nature Struct. Mol. Biol. 14, 420–426 (2007).

Abeysinghe, R. D. et al. p53-independent apoptosis mediated by tachpyridine, an anti-cancer iron chelator. Carcinogenesis 22, 1607–1614 (2001).

Lui, G. Y. et al. The iron chelator, deferasirox, as a novel strategy for cancer treatment: oral activity against human lung tumor xenografts and molecular mechanism of action. Mol. Pharmacol. 83, 179–190 (2013).

Liu, Y. T. et al. Chronic oxidative stress causes amplification and overexpression of ptprz1 protein tyrosine phosphatase to activate beta-catenin pathway. Am. J. Pathol. 171, 1978–1988 (2007).

Ba, Q. et al. Iron deprivation suppresses hepatocellular carcinoma growth in experimental studies. Clin. Cancer Res. 17, 7625–7633 (2011).

Fracanzani, A. L. et al. Increased cancer risk in a cohort of 230 patients with hereditary hemochromatosis in comparison to matched control patients with non-iron-related chronic liver disease. Hepatology 33, 647–651 (2001).

Hann, H. W., Stahlhut, M. W. & Hann, C. L. Effect of iron and desferoxamine on cell growth and in vitro ferritin synthesis in human hepatoma cell lines. Hepatology 11, 566–569 (1990).

Boult, J. et al. Overexpression of cellular iron import proteins is associated with malignant progression of esophageal adenocarcinoma. Clin. Cancer Res. 14, 379–387 (2008).

Yue, J. et al. Transferrin-conjugated micelles: enhanced accumulation and antitumor effect for transferrin-receptor-overexpressing cancer models. Mol. Pharm. 9, 1919–1931 (2012).

Brookes, M. J. et al. Modulation of iron transport proteins in human colorectal carcinogenesis. Gut 55, 1449–1460 (2006).

Eberhard, Y. et al. Chelation of intracellular iron with the antifungal agent ciclopirox olamine induces cell death in leukemia and myeloma cells. Blood 114, 3064–3073 (2009).

Torti, S. V. et al. Tumor cell cytotoxicity of a novel metal chelator. Blood 92, 1384–1389 (1998).

Zhou, H. et al. The antitumor activity of the fungicide ciclopirox. Int. J. Cancer 127, 2467–2477 (2010).

Greene, B. T. et al. Activation of caspase pathways during iron chelator-mediated apoptosis. J. Biol. Chem. 277, 25568–25575 (2002).

Turner, J. et al. Tachpyridine, a metal chelator, induces G2 cell-cycle arrest, activates checkpoint kinases, and sensitizes cells to ionizing radiation. Blood 106, 3191–3199 (2005).

Kovacevic, Z., Chikhani, S., Lovejoy, D. B. & Richardson, D. R. Novel thiosemicarbazone iron chelators induce up-regulation and phosphorylation of the metastasis suppressor N-myc down-stream regulated gene 1: a new strategy for the treatment of pancreatic cancer. Mol. Pharmacol. 80, 598–609 (2011).

Yu, Y., Suryo Rahmanto, Y. & Richardson, D. R. Bp44mT: an orally active iron chelator of the thiosemicarbazone class with potent anti-tumour efficacy. Br. J. Pharmacol. 165, 148–166 (2012).

Fukushima, T. et al. Iron chelation therapy with deferasirox induced complete remission in a patient with chemotherapy-resistant acute monocytic leukemia. Anticancer Res. 31, 1741–1744 (2011).

Yen, Y. et al. A phase I trial of 3-aminopyridine-2-carboxaldehyde thiosemicarbazone in combination with gemcitabine for patients with advanced cancer. Cancer Chemother. Pharmacol. 54, 331–342 (2004).

Knox, J. J. et al. Phase II study of Triapine in patients with metastatic renal cell carcinoma: a trial of the National Cancer Institute of Canada Clinical Trials Group (NCIC IND.161). Invest. New Drugs 25, 471–477 (2007).

Ma, B. et al. A multicenter phase II trial of 3-aminopyridine-2-carboxaldehyde thiosemicarbazone (3-AP, Triapine) and gemcitabine in advanced non-small-cell lung cancer with pharmacokinetic evaluation using peripheral blood mononuclear cells. Invest. New Drugs 26, 169–173 (2008).

Chao, J. et al. A phase I and pharmacokinetic study of oral 3-aminopyridine-2-carboxaldehyde thiosemicarbazone (3-AP, NSC #663249) in the treatment of advanced-stage solid cancers: a California Cancer Consortium Study. Cancer Chemother. Pharmacol. 69, 835–843 (2012).


Watch the video: How To Refresh Curry Leaf Plant. Cara Mendapat Daun Baru Pokok Kari (December 2021).