Biolink reports that the "Faculty of 1000 Medicine", also known as the "Faculty of 1000 Medicine", is an international authority composed of 2,500 of the world's top medical professors, including those from Harvard University and Cambridge University in the United Kingdom. Seven of the most popular recent biochemistry papers are as follows.
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L.Q. Chen et al. "Sugar transporters for intercellular exchange and nutrition of pathogens," Nature, 468:527-32, 2010. Evaluations by Julian Schroeder,
UCSD; Akiko Sugio and Saskia Hogenhout, The John Innes Centre, UK; John Patrick,
Univ Newcastle, Australia; David Alpers, Wash U Sch of Med; Bruno Stieger, Univ Hosp Zurich; Tapio Palva, Univ Helsinki; H Ekkehard Neuhaus, Univ Kaiserslautern, Germany. free F1000 Evaluation
A previously unknown group of sugar transport proteins has been identified - initially in plants, but due to the apparently widespread distribution of homologous proteins, they have also been identified in animals.
In plants, these SWEET receptors correspond to those transport proteins that have long been sought to supply glucose to nectar, seeds and pollen development. Some of these transport proteins are used by pathogens to supply sugars for replication. Postnatal homologous proteins also regulate glucose transport and may also be involved in sugar efflux from the small intestine, liver, epididymis, and mammary cells.
M.M. Reddy, et al. "Identification of candidate IgG biomarkers for Alzheimer's disease via combinatorial library screening," Cell Evaluated by Angela Vincent, Univ of Oxford, UK; Robert Powers, Univ of Nebraska; Soumitra Ghosh and Kavita Shah, Purdue Univ; Ivan Gerling, Univ Tennessee Health Sci Cen; David Holtzman, Wash Univ School of Med. Free F1000 Evaluation
Scientists in the United States may have discovered a new way to use blood tests to search for clues to Alzheimer's disease; this discovery, if proven, could be extended to other diseases.
If this works for Alzheimer's disease, it shows that this is a fairly universal platform that could work for many different diseases," said Thomas Kodadek of the Scripps ResearchInstitute. Kodadek noted, "Now we need to put this approach in the hands of disease experts and deal with diseases where early diagnosis and detection are key to treatment."
Alzheimer's disease is the most common form of dementia and is currently untreatable. 5 million people in the U.S. suffer from this disease, so there are many people who may not see much use for this disease detection method.
But the pharmaceutical industry may use this information to more accurately identify patients undergoing clinical trials. Kodadek tried a new method of identifying disease signals in the blood, using molecules called peptoids to detect antibodies in the bloodstream of animals and patients suffering from specific diseases.
After isolating more immunoglobulins (Immunoglobulin, a major antibody type) from rats with a physical condition similar to multiple sclerosis (multiplesclerosis) than healthy rats, he transferred the subjects to humans, testing six Alzheimer's patients, six Parkinson's disease patients, and six healthy people.
These tests found that three molecules captured three times as much immunoglobulin in Alzheimer's patients as in healthy individuals with Parkinson's or controls.
A.P. Carter et al. "Crystal structure of the dynein motor domain," Science, 331:1159-65, 2011. evaluated by Terrence Frey, San Diego State Univ.; Linda Amos, MRC Lab of Molecular Bio, UK; Giampietro Schiavo, Imperial Cancer Research Fund, UK; Sharyn Endow, Duke Univ. Medical Center; Peter Stathopulos and Mitsuhiko Ikura, Ontario Cancer Inst, Canada. Free F1000 Evaluation
The first crystal structure of dynein, the largest cellular scaffold kinetic protein, was obtained, providing some clues to the data on the "travel" of this giant protein along microtubules.
G. Xu et al. "Crystal structure of inhibitor of kappaB kinase beta," Nature, doi:10.1038/nature09853, 2011. evaluated by Andrew Beenken and Moosa Mohammadi, NYU Langonne Medical Center; John Kyriakis, Tufts Medical Center. free F1000 Evaluation
In this article researchers reveal for the first time the crystal structure of a kinase inhibitor, KB kinase inhibitor, that plays an important role in inflammation, immunity and apoptosis. The researchers found that its structure is very similar to that of scissors. The new findings may help scientists to develop anti-inflammatory drugs that target this kinase.
M.A. Fisher et al. "De novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell Evaluated by Etienne Joly, CNRS, France; Donald Doyle, Georgia Inst of Technology; Ulrich Muller. Muller. Free F1000 Evaluation
Scientists in the United States claim to have used artificial genes for the first time to synthesize artificial proteins that sustain the growth of living cells and function like proteins found in nature, a breakthrough that could help scientists develop new biological systems.
Michael Hecht, a professor of chemistry at Princeton University who led the research, said it was a major breakthrough in synthetic biology. Scientists in the burgeoning field of synthetic biology hope to design and construct biological "parts" and systems that don't exist in nature, with one of the ultimate goals being to synthesize a complete genome using chemicals. New research suggests that the creation of artificial genomes that can sustain cellular life may be within reach.
Almost all previous research in synthetic biology has emphasized recombination of the "parts" of life extracted from natural organisms. But according to Hecht, the latest research shows that the molecular "parts" that make up life are not limited to genes and proteins that already exist in nature, and that macromolecules synthesized in the laboratory can also provide biological functions. Although scientists have shown that proteins can be designed to fold and even accelerate reactions, the new research represents the cutting edge of artificial protein manufacturing.
Biological macromolecules proteins are the material basis of life and are intimately linked to life and to all forms of life activities. There are many types of proteins in the human body, with different properties and functions, but all consist of more than 20 amino acids combined in different proportions. If a protein is made up of 100 (or more) amino acids, then there could be many more different protein sequences, Hecht said. The team wanted to figure out why there are only 100,000 different proteins in the human body, even though more proteins than that could be produced.
So Hecht's team set out to make artificial proteins that are encoded by gene sequences that don't exist in nature. Eventually, they synthesized about a million amino acid sequences and got them to fold into a stable three-dimensional structure.
Michael Fisher, another leader of the research team and a visiting scholar at the University of California, Berkeley, said the most interesting part of the study was that the information encoded by these artificial genes was completely new and not derived from information encoded by natural genes, and there was no relationship between the two.
The team inserted the synthetic artificial proteins into different mutant bacterial strains in which certain specific natural genes had been deleted beforehand, so they would die under certain circumstances. The experiments proved that the bacterial strains that would have died were "saved" by the novel artificial proteins that could sustain life. These artificial proteins are not related to any known biological sequence, but they can sustain life growth," Hecht said. This is an exciting conclusion because it demonstrates that unnatural proteins can also sustain the life of natural organism systems."
J.F. Dishinger et al. "Ciliary entry of the kinesin-2 motor KIF17 is regulated by importin-beta2 and RanGTP," Nat Cell Biol, 12: Evaluated by Yuh Min Chook, Univ of Texas; Monica Bettencourt-Dias, Inst Gulbenkian de Ciencia, Portugal; Michael Rape, Berkeley Univ; Jonathan Bird and Thomas Friedman, NIDCD NIH. free F1000 Evaluation
In this article, researchers demonstrate that the proteins GTPase Ran and importin-β2, which are involved in protein nuclear transport, are involved in targeted protein transport to primary cilia.
P. Sarkies et al. "Epigenetic instability due to defective replication of structured DNA," Mol Cell, 40:703-13, 2010. by Matthew Bochman and Virginia Zakian, Princeton Univ; Alan Lehmann, Univ of Sussex, UK; Antony Carr, Univ of Sussex, UK. free F1000 Evaluation
In this article, researchers found that defects in the DNA polymerase REV1 can lead to loss of epigenetic marks on certain DNA loci such as histones on telomeres. The new findings reveal the mechanism by which a single mutation leads to widespread epigenetic destabilization.
"Founded in January 2002, Faculty of 1000 Biology is an online research evaluation system that bases its recommendations on the scientific significance of the paper itself rather than the journal in which it is published. The system provides a quick review of recently published bioscience papers based on the opinions of more than 2,300 senior scientists worldwide, with the goal of helping researchers select and identify valuable research. Based on their contribution to current biomedical and clinical practice in the world and their scientific value, the experts of this institution recommend and review the best medical papers with less than two thousandths of the total number of SCI articles worldwide every year, and give the title of "F1000 papers" to the medical community, covering all disciplines of medicine, which is a high academic honor.