Vitamin B12 - strong and healthy hair

Advantages: improved appearance of hair, helps with hair loss, faster hair growth

Disadvantages: you need to be careful with the dose

Sometimes, in response to a topical application of vitamins B6 and B12 may experience an allergic reaction. A hypervitaminosis of Vitamin B12 (Cyanocobalamin injection) as a symptom urticaria, and together with these allergic disorders result in itching, sometimes - in the head region.

However, in most cases, expressed negative impact directly on the hair a slight excess of these vitamins will not help.

And then I realized that in no case should not be confused with these vitamins. They did not hurt so much together as a lapse. Vitamin B 6 is not absorbed with B 12 and B 1, etc. That is, it is not economical and pointless.

Recipe mask:

1 tbsp of burdock oil

1 tbsp castor oil

The ampoule 12 

1 tsp of coconut oil (it seemed to me that it dries hair, but then I have significantly reduced the dose, and all was well)

2 tbsp hair balm

Then all you need to rinse shampoo.

Vitamins in capsules is a good replenishment to hair. but should be used wisely and not to exceed the dose. But your hair is not even with them will be healthier if you eat poorly absorbed and bad habits. I take a month and really got better hair. Stopped so hard to fall and the pleasing appearance.

Vitamin B12 injection - really helps!

Advantages: improved appearance, helping hair loss, strong and healthy hair, hair growth accelerates

My hair started falling out 5 years ago because of nerves, doing a variety of masks, used sera from falling out, took vitamins and tried more, all this was just enough for the period of their application.

Two months ago, I saw on the Internet a prescription shampoo from hair loss, cyanocobalamin was a part of all the vitamins that I applied for hair loss. I started after each washing of hair to rub into the roots of one ampoule. The result is visible after three to four applications !!!

take three tablespoons of shampoo, one ampoule of cyanocobalamin (Vitamin B12 injection), one vial of pyridoxine (B6). Mix everything until smooth.

My hair shampoo and then we put it on the hair structure, the blowing well and leave for 10-15 minutes, then wash off. The result is stunning!

Result: The hair is healthy and thick, it became much less fall! The result was very pleased.

Vitamin B12 - affordable price, is indispensable for vegetarians

Advantages: affordable price, is indispensable for vegetarians

I saw reviews girls who use ampoule of vitamin topically. I can say only one thing - with this method of application of water-soluble vitamins do not work. They simply can not penetrate deep into the hair and the skin layers, and to act at the cellular level. All this self-delusion.

I pricked myself with B12 deficiency anemia on the advice of a doctor, because I have problems with the intestines and how much I would have no food meat, eggs, liver, B12 level remains low (below 100). After a course of injections of B12 levels, hemoglobin rose from 97 to 125, health returned to normal and significantly reduced pain from neuralgia.

We strongly advise all vegetarians take preventive courses of cyanocobalamin (vial per month), because you can not get Vitamin B12 from herbs, fruits, vegetables and nuts.

If suddenly someone wants to appoint himself injections of vitamin (which I do not advise), then hand over blood test for B12 in any laboratory and do not forget about possible allergies. Also, in any case not cyanocobalamin colitis simultaneously with other vitamins (B12 rahrushaet them), especially B1 (probability of an anaphylactic shock is increased by several times).

Minimal Genome

Bioinformatics Dr. Doping tells about the common ancestor genes, turning off the genes of Escherichia coli bacteria and competition.

What are the different approaches to defining the minimal genome? As implemented experimental gene research methods that are required?

There are several approaches to the definition of what is the minimum genome. First - it is evolutionary. It is based on the natural philosophy that if a certain gene is present in all organisms, you probably can not do without this gene. Here there is actually a deceit. Because when I say that the same gene is present in various organisms, the question arises, and how do I know that this is one and the same gene and that is all one and the same gene, when it is in three different genomes. The evolutionary definition is: we believe that this is one and the same gene, if they had a common ancestor and the history of this gene is exactly the same kind of history, that is, there were no duplications, and the genes differed only as a result of speciation.

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If you grow bacteria on a medium, the only source of carbon which is, for example, fructose, and you have killed conveyor fructose or killed enzyme which catalyses the first reaction of fructose nutrition, everything in your environment, except fructose, nothing, and the possibility you broke it. And if you are in the same environment pour glucose, it will be wonderful to live and thrive. So here we must say that we will let them grow a rich environment in which there is everything that she might need, and look on minimal genome such an environment. So people do, and it is also reasonable definition. It is softer than evolutionary. That is, the genes that are absolutely universal, evolutionarily lower than genes that are required for such an individual is turned off.

Experiments are now minimal genomes of most runs by Craig Venter, who was involved in the human genome, and then switched to the genomes of bacteria. Applied the idea that in doing so he is trying to sell, I, frankly, not very much. Because he has this idea that we are here to make a minimum genome, and then we will optionally add to it some pieces and do commissioned by the bacteria, "design", which we need. I do not really understand why it is technologically justified because we actually can do it now. We can take the E. coli - we have a set of technological strains - and they can do the same. But Venter says that there will not be anything extra. On the other hand, it certainly will not be anything extra, but at the same time will be quite of dead.

GPCR

GPCR are the transmitters of signals inside the cells, allowing the cells of various organs and systems of the body communicate with each other and receive information about the environment. There are about 800 different GPCR, which are located in the membranes of human cells and recognize a wide range of extracellular simulators comprising ions, hormones, neurotransmitters, peptides, etc. Examples of well known molecules for which receptors respond are epinephrine, serotonin, dopamine, histamine, caffeine, opioids, cannabinoids, chemokines and many others. Receptors transmit signals through the activation of GTP-binding proteins (G-proteins), which in turn trigger intracellular complex chain of reactions leading to certain cellular and physiological responses. We can find it in the drugs: Cerebrolysin, Cortexin and in Peptide Complex for immune system.

The processes of GPCR-controlled, give us the opportunity to see and feel the smells, react to danger, have pain or feel euphoria, maintain blood pressure and regulate heart rate, ie, all that is necessary for the functioning of the body. Sometimes signaling processes are broken, leading to numerous and often severe disease. Many diseases may be cured but by acting on receptors drugs. In fact, about half of all modern drugs aimed at receptors associated with G-proteins. Thus, research aimed at determining the structure of GPCR receptors and signaling mechanisms should allow a better understanding of the causes of many diseases, as well as give impetus to the development of more effective drugs with minimal side effects.

History of GPCR research has more than 100 years. The receptor, which responds to the light - rhodopsin - was, for example, discovered and isolated in 1870 by the German scientist Wilhelm Kühne. By the early 70-ies of XX century, it was known that muscle cells can activate or inhibit the effects by certain molecules. Part of the mechanism of intracellular reactions, too, was known, and it was clear that the molecules, stimulating the cells do not penetrate into the cells. Thus, it was postulated the existence of a receptor substance which reacts to extracellular molecules and sends a signal into the cell.

The search for this elusive substance and the receptor engaged Robert Lefkovitz using adrenaline (a hormone stimulating cells) with a built a radioactive isotope of iodine. These studies determine that some adrenaline protein binds to a cell surface or receptor. The fact that the signal is transmitted inside the cell by activation of G-proteins, was by this time already discovered Rodbell and Gillmanom (for which the two scientists won the Nobel Prize for Medicine in 1994). Thus, proteins that respond to extracellular stimuli were identified receptor conjugated with G-proteins, and several of these receptors have been identified. However, the isolation and identification of the amino acid sequences of GPCR was a big problem, because all the receptors, with the exception of rhodopsin, the cells produced in very low numbers. For the first time to isolate and determine the sequence of the beta-adrenergic receptor (a receptor that responds to adrenaline) failed in 1986, then again in the laboratory Lefkovitz with Brian Kobilka who carried out the study postdoctoral. Cloning has brought a big surprise: amino acid sequence analysis showed that adrenoceptor has seven transmembrane alpha helices and is very similar to the visual receptor rhodopsin, studies of the structure which were more advanced thanks to the work of several laboratories, including Soviet scientists under the direction of Yuri Ovchinnikov.

These studies have shown that receptors with very different functions may be close relatives, and that perhaps there are other receptors with a similar structure. Indeed, the human genome sequencing has revealed more than 800 genes that encode GPCR. It became clear that signaling via GPCR is a universal mechanism of communication between the cells and the cells with the environment.

In order to fully understand the operation mechanism of GPCR, it had knowledge of their spatial structure with atomic resolution. Such structures can be obtained only by means of X-ray diffraction requires the cultivation of a highly ordered crystal. GPCR however, were famous for their resistance to crystallization, in spite of the persistent work of many laboratories in the world. The first GPCR structure was Palchevsky in 2000 crystallized the same rhodopsin, which is the most stable and the least mobile of all the GPCR. It took another 7 years before the first structure of the human receptor that responds to adrenaline was determined.

I was fortunate to participate in these studies. In 2006 I began working in the laboratory of Ray Stevens at the Scripps Institute in La Jolla, which has collaborated with Brian Kobilka in determining the structure of the beta-adrenergic receptors. Kobilka worked on stabilization adrenoceptor by molecular engineering, the Stevens laboratory tried to crystallize it. A few months later I was able to crystallize the receptor is modified using a special crystallization method in lipid cubic phase with the use of cholesterol, which I improved during the past several years. The structure of the beta-adrenoceptor has been published in the journal Science in 2007 and was named one of the 10 scientific advances of the year. Over the past 5 years, 15 different GPCR structures were identified - mainly laboratories Kobilka and Stevens. Finally, in 2011 Kobilka was possible to fix the crystal whole signaling complex between the activated beta-adrenoceptor and G-protein and determine its structure, making it possible to see close signal of transduction from the receptor to the G-protein.

Thus, thanks to the heroic efforts of Lefkovitz, Kobilkz and other scientists over the last 40 years, we have learned about the existence of a unique and diverse family of receptors conjugated with G-proteins, which control all the vital processes in the human body. Structural studies of the past five years have brought the knowledge of three-dimensional structures of these receptors, it possible to understand how extracellular ligands recognized by the receptors, and how is the transmission of signals to the G-proteins. These pioneering work laid the foundation for a more detailed investigation, which in the future will help to learn the necessary nuances that distinguish these receptors from each other and allow them to selectively respond only to certain ligands, a better understanding of the pharmaceutical signal details the different types of ligands to determine the possible effects of receptor dimerization, effects allosteric ligands, as well as details of an ectopic signaling mechanism through arrestin. All this may lead to a new generation of medicine, where drugs would be more effective, cease to cause side effects and will be selected according to the genetic information of the GPCR of the particular patient.

FAQ: NMR of Biomolecules

7 facts about the possibilities of NMR to study biomolecules

Just a few years after the NMR method has established itself as a powerful tool for the study of simple organic compounds, the first attempts to measure the spectrum of the protein were performed. The first work relates to the 1957-th year, and the spectra were obtained at the time, of course, little information. Since then, for little more than half a century, the NMR spectroscopy of biomolecules has come a long way, becoming second only to X-ray crystallography, a method for determining the structure of proteins, the key experimental method for studying the dynamics of biomolecules and to gain a leading position in the field of rational design of new biologically active compounds.

• 1.Protein, which was measured for the first NMR spectrum was ribonuclease A. The spectrum is a simple set of "mounds", from which no structural or other useful information at the time to get it was not possible. 20 years later, in the late 70's, it was already created a powerful methodology for the Fourier NMR spectroscopy, and the first two-dimensional NMR spectroscopy methods. Creating a two-dimensional spectroscopy techniques enabled the real powerful impetus to the study of complex compounds, such as proteins and nucleic acids. Of course, the main contribution to the development of this area belongs to the Nobel Prize winner, the Swiss scientist Richard Ernst. several complementary techniques such as the so-called NOESY spectroscopy were created, that is, the nuclear Overhauser effect spectroscopy (Nuclear Overhauser Effect) - a method to detect the internuclear contacts. If protons are close together in space, in such a two-dimensional spectrum shows cross-peaks in the positions corresponding to the two interacting protons through space.
• 2.Two-dimensional spectra of the COSY, the so-called correlation spectroscopy: If protons interact with each other through the valence electrons in the system, having a non-zero constant spin-spin interaction, ie they are not separated by more than three chemical bonds from each other, that we in this spectrum we see corresponding cross peaks. And also it created a number of complementary techniques, for example, TOCSY - for detecting all protons belonging to the same amino acid residue protein. It turns out that if we analyze the two-dimensional spectrum of a relatively small protein with a molecular weight of, say, up to ten thousand Daltons, these techniques COSY, TOCSY and NOESY able to give us sufficient information to classify the signals, that is, to identify each of the protons of the protein. Such information that we obtain from these spectra, it is sufficient to calculate the structure of the protein. In 1983, a group of scientists under the leadership of Nobel laureate Kurt Vyutrih first structure is a relatively small protein has been calculated, but it was a breakthrough - until that time the only way to determine the structure of biomolecules was X-ray crystallography. Finally, there was an alternative method. Firstly, this method allows to determine the structure of the solution, rather than in the crystal and, secondly, the physical basis of this method is fundamentally different from the X-ray analysis.
• 3.Further NMR methodology has become quite rapidly. It has been found that very useful information for studying biomolecules can provide not only protons and heavier nuclei, for example, such as carbon-13. Its natural content is relatively small - about 1%, but it is possible to grow a protein enriched isotope carbon-13 medium and thus to increase the magnetic content of the active carbon isotope to almost 100%. The same applies to the nitrogen-15 isotope, a natural content of which is still three times less. Preparation of labeled stable and magnetically active isotopes C-13 and N-15 proteins techniques has created a so-called heteronuclear spectroscopy, that is, the spectral correlation of these techniques heavy nuclei carbon or nitrogen and protons associated with them. And, finally, the combination of classical methods TOCSY, COSY and of NOESY, which are mentioned above, heteronuclear methods allowed to establish methods of multidimensional NMR spectroscopy. For example, in a three-dimensional (3D) spectroscopy data spaced along three axes: one axis of the heavy nucleus (nitrogen-15 or carbon-13), second - proton bound a chemical bond with the heavy nucleus, and the third axis - any other proton interacting with the previous through space or through a spin-spin couplin
• 4.These approaches helped establish the methodology to study not only capable of small proteins, as it was in the early development of the NMR spectroscopy of biomolecules, and proteins to the 20, 30 kDa and higher. Now the restriction on the molecular weight of the object being studied is rapidly expanding. In recent years, studies in which researchers from different countries publish data on reference signals of proteins or protein complexes up to megadaltonic size. This, of course, extremely expands the possibilities of NMR. Very important is the fact that NMR spectroscopy can not only get information about the structure - it quite successfully obtained by X-ray analysis, but you can get very valuable information on the dynamic properties of protein systems, and here the NMR method is unique. That is, we can get up to atomic resolution information on how, what characteristic frequencies, ie, how quickly and with what amplitude move certain pieces of the protein molecule. Moreover, these characteristic times movements are investigated and from picoseconds up to hours, i.e. until NMR spectroscopy in real time. To improve your mental ability – buy Russian nootropics – Cogitum, Semax, Cortexin, Phenotropil.
• 5.And finally, the third area, which is extremely important - it is the possibility of NMR method for monitoring the interaction of various molecules, for example, studying the interaction of small molecules with biomolecules. These biomolecules may be target proteins - ie those which are affected by one or another medication, and low molecular weight compounds may be drugs that we use, or those compounds which have the potential to become them. And because of the extremely high information content of the NMR method for determining the ability of small molecules to bind to proteins, this method has become a very rapidly developing in recent years in the application to search for drugs. There approaches called NMR screening, aimed at the identification of compounds, or even smaller molecular fragments future drugs that bind to the pocket or other protein target. And by NMR can be positioned a variety of molecular fragments, and then articulated them get pretty high-affinity compound that has the potential to be a good remedy.
• 6.Most major pharmaceutical companies since the late 90-ies of the XX century, and in the last decade, it happens quickly, it began to use the technique of NMR screening. Almost all of them, this methodology is widely used. If you look at a list of biologically active compounds, which are at a particular stage of pre-clinical or clinical trials, it appears that at least a third of them selected by the methods of NMR screening. It should be noted the two different directions of application of NMR to drug discovery. The first direction is associated with the identification of the most biotarget signals, that is, of a protein that is the target of the drug. Such protein must certainly be studied by NMR, in particular it should have received information on reference signals. And then there are a number of NMR techniques which allow to precisely position the binding pocket of low molecular weight compounds, potential drugs with the target protein. Methodology molecular fragments (fragment-based drug design, FBDD), using the information obtained by NMR for meaningful articulation of small molecular fragments into a larger molecule which has the potential to become a medicine.
• 7.The second area involves not obtain information about assigning NMR signals of the target protein. Moreover, such a protein can be extremely high from the standpoint of NMR and inconvenient to measure its spectra. But such a protein can be studied by NMR screening techniques. For this latter approach is used, based on the monitoring of the properties of low molecular weight compounds. It is possible by detecting a particular property of the low molecular weight fragment say that it binds or does not bind to biological target. By building in a reasonable manner, step-by-step scheme of the fragment structure changes and detecting the properties of binding to biotarget by NMR, we can approach the structure more effective compounds. Such a compound would in its properties approach for potential drug, i.e. have effective binding constant with target protein and other properties specific to the drug. Then, however, it needs to have a long way to his in-depth preclinical and clinical trials, but that's another story in which, however NMR methods occupy not the last place.

FAQ: G-protein coupled receptors (GPCR)

7 facts about the largest family of receptors

G-protein-coupled receptors (from the English G-protein-coupled receptors, GPCR.) are the largest family of receptors in the genomes of most organisms responsible for three of the five "classical" sense of humans and most animals and many alarm systems in the body. They are about 50% of existing drugs, but their therapeutic potential is just beginning to get used.

• 1.Until the autumn of 2012 nonspecialists have not heard a word - G-protein coupled receptors. It is now on everyone's lips. In short, the Nobel Prize in Chemistry in 2012 received the Robert Lefkowitz and Brian Kobilka "for studies of G-protein-coupled receptors." Lefkowitz in the late 1960s opened the first representative of the family - beta-adrenoceptor and later his disciple Kobilka identified the gene of this receptor, and found similarities with another, seemingly quite unrelated protein - the photoreceptor rhodopsin, located in the retina of the eye and allows us to see. It was quite a bold decision - to combine these and many more receptors in the same family. Even much later, it was confirmed that they have a common spatial structure.
  
  In 2007, Kobilka achieved triumph - the exact spatial structure of the β2-adrenergic receptor was obtained. This proved to be very difficult to do - GPCR-receptors required an entirely new method for obtaining crystals suitable for X-ray analysis. In 2011, he said "the finishing touch" to his many years of work - showed how the activated receptor located in the cell membrane, interacts with G-proteins located "below" the membrane (in the cytoplasm).
• 2.Why is it important to know that GPCR-receptors - a membrane protein, and what is so special in the cell membrane?
  
  The membrane - is the main shell of life, because no living organism can not do without it. Even many viruses, about which they are still possible to argue, living or not, have a membrane. The fact that it shares the "inner world" of the cell and the rest of the space, allowing the most important reactions take place in a very limited space is relatively small depending on what is happening around. Intercellular communication, allowing the cells to form a community (in bacteria) or organisms (from multicellular eukaryotes), is also based on the membrane. This is not just a semipermeable film of lipids and complex hybrid of the lipid bilayer and the "floating" in its membrane proteins - ion channels, receptors and others. A third of the protein in the body - diaphragm.
• However, membrane proteins to study the very complexity in contrast to globular proteins, well-behaved "feel" of the solution. In particular, in order to GPCR-receptor I have the correct shape and working properly, it must be located in the membrane. For a long time it was the stumbling block in the study of the structure of the G-protein-coupled receptors: in the cage of their very small, and therefore it is necessary to receive them and explore in bioengineering applications where serious difficulties arise in obtaining (expression), and delivery to the membrane-like environment and protein delivery "crystal" required for X-ray analysis, and interpretation of the diffraction data.
  
  An important breakthrough in structural biology of GPCR-receptor managed to make our compatriot Vadim Cherezov, which in collaboration with Kobilka in 2007 was able to get a crystal genetically engineered variant of .beta.2-adrenergic receptor, using a cubic phase lipid technology. Since this method been adopted by many laboratories around the world.
• 3.The membrane environment determines how membrane proteins are arranged: there are fragments of the protein chains are hydrophobic (ie, "afraid" of water and "love" to communicate with non-polar molecules - such as membrane lipids). In addition, they are packed in the α-helix, roughly perpendicular to the plane of the membrane. GPCR-receptors contain seven such segments, and therefore of the structure resembles a "snake" which makes seven bends to cross the membrane.
  This fact prompted Kobilka in his time at the thought that adrenoceptor and a photoreceptor of the retina - Rhodopsin - have the general structure: analyzing the genetic sequences of these proteins, he discovered these same seven chains of hydrophobic amino acid residues in both receptors. Interestingly, when, at first glance, is very similar to the structure of these receptors respond to a wide range of chemical and physical signals.
• 4.The G-protein-coupled receptors are three major families:
  
  1. Rhodopsin family (A): here includes the photoreceptor rhodopsin, and the receptors of monoamines (epinephrine, muscarinic, dopamine, histamine, serotonin), peptides (angiotensin, bradykinin, chemokines, opioids, neuropeptides), hormones, cannabinoids, as well as odors (about 300 of these receptors). Such as are Neiromidin (Ipidacrine), Adrenaline (Epinephrine) injection, Dexamethasone.
  
  2. Secretin family (B) receptors: these receptors neuropeptides such as calcitonin, glucagon, growth factors, and other secretin.
  
  3. Glutamate receptor family (C): the amino acid glutamate receptor (having a "meat taste") and other taste receptors as well as receptors of calcium ions.
  
  Total in the human genome contains nearly a thousand genes of GPCR receptors, which means that one in twenty protein in our body - it is just such a receptor.
• 5.One of the most well-studied of G-protein-coupled receptor is a retinal photoreceptor rhodopsin our eyes. In the cavity between the seven transmembrane α-helices, it contains a light-sensitive retinal pigment that is capable of absorbing a photon and change their conformation (the conversion takes place cystrans). This seemingly boring chemical detail allows us to enjoy the white (and not only) light: retinal, "straightened" changes the shape of the receptor, which is "activated" and begins to interact with G-proteins (in the case of rhodopsin, the protein called transducin). Activation of transducin eventually generates a signal to the brain along the optic nerve.
• Rhodopsin - the pigment cells - "sticks", working in the dark and "turn off" a bright light. Yet, as we know, there cells "cones", which contains three other opsin, rhodopsin related to, but different in color sensitivity: they see blue, green and red colors, defining vision trihromatichnoe primates. Therefore, "in the dark all cats are gray" - "color" opsins only work in bright light, and the rhodopsin - at dusk.
  
  Interestingly, the first was defined spatial structure is rhodopsin (this was in 2000), and not adrenoceptor. However, none of the authors of the work is not ranked in the list of Nobel Prize winners.
  By the way, a cofactor retinal allocated Sangiorgi Wald in 1933 from the retina of the drug, it is a product of transformation of vitamin A, which explains the phenomenon of "night blindness", which appears when vitamin deficiency. Retinal - a single molecule, which is attached to the receptor by chemical modification (without a receptor, of course, does not react to light). In 1967 Wald received the Nobel Prize in Physiology or Medicine "for his research on the physiology and biochemistry of vision"
• 6.In the absence of signal receptors are found in an inactive form. For lack of receptor signal - when it is not associated with the ligand-activator or agonist. Alternatively, the receptor can bind to the ligand-inactivator, or antagonist. So for rhodopsin and agonist and antagonist - it is one and the same molecule: retinal. Only in the dark retinal it is in cis-form and an antagonist, and the light it is transformed into the trans-form and becomes agonist. Thus rhodopsin and other opsins "feel" light.
  
  Receptor, "feeling" the signal is activated. At the molecular level, it denotes a restructuring, "inner" (cytoplasmic) receptor side is changed so that it begins to recognize the G-protein. G-protein composed of three subunits: α, β and γ. After joining the G-protein receptor α-subunit is disconnected from the complex and is sent to the "free floating" in the process which triggers a cascade of biochemical reactions, which is the meaning of all the foregoing receptor act. A next activated receptor activates G-protein molecule, multiple amplifying the original signal, which may be a single molecule or a (!) Photon.
  
  Obtaining the spatial structure of β-adrenergic receptor in activated form and in combination with G-protein was the "last straw", after which the Nobel Committee has decided to: "all, it's time to give."
• 7.Such noise due to biochemical and biophysical studies receptor family would not have been if those studies are not anticipated breakthrough in pharmacology, coupled with the development of new drugs acting on of GPCR-receptors. With malfunction of these receptors is associated a spectrum of very common diseases, including allergy, schizophrenia, hypertension, asthma, and many other psychoses. Even today, on the G-protein-coupled receptors act according to various estimates, about half of today's medicines, and this number promises to grow strongly in the light of the active structural investigations initiated over 30 years ago Kobilka and Lefkowitz.
  
  The fact that the modern paradigm in biochemistry says that knowing the structure, it is possible to enter in the function of "molecular machines", such as a receptor. This concept is based rational design of medicines: knowing what's inside "Castle" (receptor), and you can pick up the "key" (medicine). However, it is necessary to wipe a little rose-colored glasses: life is always more complicated schemes (especially marketing), and the development of new generations of drugs, although it facilitated a comprehensive study of receptors, still can not be reduced to it. So biologists for a long time will be something to do.

From where do the phobias appear?

Psychologist Dr. Doping tells about the underlying causes of phobic disorders, the role of gamma-aminobutyric acid and disasterization.

Phobia - is an intense fear of specific objects or situations leading to steady their avoidance. For example, if a person experiences intense fear when visiting the dentist, but overcomes it and regularly treats teeth of the phobia as mental disorders are not talking: no avoidance and related life limitations.

Modern science is dominated by the so-called biopsychosocial conception of mental disorders, including phobias. It is easy to see that the word "biopsychosocial" consists of three parts, which represent the main causes of phobic disorders. Thus, a phobia is due to the joint effect of three factors: biological, psychological and social - which also interact with each other, strengthening or weakening the contribution of each individual, so called biopsychosocial model system.

Biological causes of phobias are complex and associated with biochemical features of the brain; particularly important role in the regulation of the excitation is given in the so-called brain GABA (gamma-aminobutyric acid). GABA - a neurotransmitter (a substance through which impulses are transmitted between neurons), has a calming effect on the nervous system. Thus, people who are prone to anxiety attacks GABA failure occurs which may be due to genetic factors, as well as prolonged stress or exposure to toxic substances.

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However, only one biological vulnerability can lead to phobias. Psychological causes phobias describes different psychological schools differently. For example, analysts believe that the formation of a phobia symbolized intrapersonal conflict that arose at a certain stage of psychosexual development (recall described by Freud "Case of Little Hans," in which the boy's fear of being bitten by a white horse is interpreted as the offset for fear of being punished by his father to the proximity of the desire to mother ). Another look at the psychological causes phobias provide cognitive theory ( "cognitive" - associated with thought processes).In these theories, the phobia is seen as a consequence of the distorted effects of impact assessments object of fear, such as the so-called "disasterization": "I can not stand it, it will kill me."

Social reasons are usually associated with weathered through traumatic and stressful situations that can speak launchers incentives for the development of phobias (dogs bite a child, transferred serious illness, media reports about the high risk of cancer and cardiovascular diseases). These start-up incentives can start the development of phobias only if there is the so-called "diathesis" (dispositions) by biological and psychological characteristics of the individual. Thus, the causes of phobias are systemic, and bringing them to any one factor would be unjustified and incompetent.

Cogitum - effective, restful sleep, clear words

Advantages: restful sleep, clear words

Passed Commission for kindergarten, at the doctor-neurologist turned out, speech is not appropriate to the age daughter. neurologist urged to take a course Cogitum Aventis, to improve the central nervous system, leading to an improvement in speech.

Medicine yellowish color, banana flavor, sweet taste. The consistency of the liquid, not sticky.

Daughter of the first day of admission, the following days were sleeping normally at night suddenly cried after Cogitum night calmer. Less irritable during the day (especially evident in the days of taking the medicine), when there is a break between meals, irritability little more manifest. She listened attentively when I read stories, showing pictures. Easily perceives an imaginary by me information during the story. Good imagination started to work, playing with toys alone, it represents different situations in life. easier repeats remembers new words. speech is, in principle, without global change, but it is better than it was: the word is pronounced clearly, it adds little to offer clear, not only to me.

Recommend Cogitum Aventis, the drug has a positive effect on the child's body.

Duration of use: month

Cogitum - helped the child to talk

Advantages: Well tolerated, effective

Disadvantages: uncomfortable ampoule

The main drawback of the drug - dose ampoules. since frequently prescribed Cogitum lesser dosage.

Our daughter has appointed a neurologist solution in 2.5 years. We were born prematurely, and around a little behind from their peers. By weight, motor and mental development. For one and a half years in the thought, and most of all I was going through it for speech development.

The course selected individually depending on the degree of complexity of the problem. Our child was scheduled for 30 days, at a dosage of half ampoules single dose.

My daughter endured "Cogitum" quite normal. A nice banana taste.

Improvements were noticeable already in the second week of reception. First, the child became an active interest in things around, and just went and pointed. All that saw called.

After month reception of "Cogitum" it was possible to learn poems.

In general, the drug is positive. Well tolerated, the taste is normal, children like. And the effect is visible very quickly. I recommend. If the doctor prescribes a course.