1. SWEET proteins found A new class of proteins, dubbed SWEETs, function as glucose transporters, shuttling sugar molecules out of plant, worm and human cells. In some plants, SWEET proteins are co-opted by bacterial pathogens to deliver nutrition to the invaders. 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 2. Identifying the unknown
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Image: flickr, AJC1 | Researchers present a novel method for identifying antibody biomarkers for diseases without known antigens. The technique, which involves searching for antibodies that bind to various synthetic molecules, may prove useful for identifying diagnostic markers in a wide variety of diseases. M.M. Reddy, et al., "Identification of candidate IgG biomarkers for Alzheimer's disease via combinatorial library screening," Cell, 144:132-42, 2011. 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 3. Motor protein visualized The first crystal structure of the largest of the cytoskeletal motor proteins, dynein, offers some hints as to how this mammoth protein walks along microtubules tracks. An asymmetrical ring of six ATP binding domains linked to a long coiled stalk that binds to microtubules is powered by energy from the hydrolysis of ATP. 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 4. Inflammatory scissors In another crystal structure first, the core of a kinase inhibitor that plays a major role in inflammation, immunity, and apoptosis -- the inhibitor of kB kinase (IKK) -- is revealed. The structure, which resembles scissors or pruning shears, could potentially help researchers develop anti-inflammatory drugs that target the enzyme. 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 5. Artificial proteins to the rescue
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Image: flickr, CdePaz | By coercing poorly-growing E. coli mutants to express more than a million laboratory-designed proteins, researchers identified 18 novel proteins that were able to compensate for the crippling mutations and enable the cells to grow. Their novel approach brings synthetic biologists one step closer to constructing fully artificial genomes. M.A. Fisher et al., "De novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growth," PLoS One, 6(1):e15364, 2011. Evaluated by Etienne Joly, CNRS, France; Donald Doyle, Georgia Inst of Technology; Ulrich Muller. Free F1000 Evaluation 6. Two-timing transporters Proteins involved in the transport of proteins into the nucleus -- GTPase Ran and importin-β2 -- are also involved in targeting proteins to primary cilia, microtubule-based structures involved in cell signaling and motility, suggesting that both proteins play a global role in cilia and nuclear import. J.F. Dishinger et al., "Ciliary entry of the kinesin-2 motor KIF17 is regulated by importin-beta2 and RanGTP," Nat Cell Biol, 12:703-10, 2011. 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 7. Epigenome interrupted
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Image: flickr, AJC1 | Researchers found that loss of the DNA polymerase REV1, which helps the DNA replication machinery to move along sites of damaged DNA, also leads to the loss of epigenetic-marks on histones at certain DNA sites, particularly in telomeres. This finding suggests a possible scenario whereby one mutation can lead to widespread epigenetic instability. P. Sarkies et al., "Epigenetic instability due to defective replication of structured DNA," Mol Cell, 40:703-13, 2010. Evaluated by Matthew Bochman and Virginia Zakian, Princeton Univ; Alan Lehmann, Univ of Sussex, UK; Antony Carr, Univ of Sussex, UK. Free F1000 Evaluation The F1000 Top 7 is a snapshot of the highest ranked articles from a 30-day period on Faculty of 1000 in Biochemistry, as calculated on April 13, 2011. Faculty Members evaluate and rate the most important papers in their field. To see the latest rankings, search the database, and read daily evaluations, visit http://f1000.com. Related stories:
Top 7 in oncology
[12th April 2011]
Top 7 in genetics and genomics
[5th April 2011]
Top 7 in cancer biology
[29th March 2011] |
