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WFRF:(Agar Thomas K.)
 

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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004379naa a2200913 4500
001oai:DiVA.org:kth-223782
003SwePub
008180307s2018 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-2237822 URI
024a https://doi.org/10.1038/NCHEMBIO.25762 DOI
040 a (SwePub)kth
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Aebersold, Ruedi4 aut
2451 0a How many human proteoforms are there?
264 1b NATURE PUBLISHING GROUP,c 2018
338 a print2 rdacarrier
500 a QC 2018307
520 a Despite decades of accumulated knowledge about proteins and their post-translational modifications (PTMs), numerous questions remain regarding their molecular composition and biological function. One of the most fundamental queries is the extent to which the combinations of DNA-, RNA-and PTM-level variations explode the complexity of the human proteome. Here, we outline what we know from current databases and measurement strategies including mass spectrometry-based proteomics. In doing so, we examine prevailing notions about the number of modifications displayed on human proteins and how they combine to generate the protein diversity underlying health and disease. We frame central issues regarding determination of protein-level variation and PTMs, including some paradoxes present in the field today. We use this framework to assess existing data and to ask the question, "How many distinct primary structures of proteins (proteoforms) are created from the 20,300 human genes?" We also explore prospects for improving measurements to better regularize protein-level biology and efficiently associate PTMs to function and phenotype.
650 7a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng
700a Agar, Jeffrey N.4 aut
700a Amster, I. Jonathan4 aut
700a Baker, Mark S.4 aut
700a Bertozzi, Carolyn R.4 aut
700a Boja, Emily S.4 aut
700a Costello, Catherine E.4 aut
700a Cravatt, Benjamin F.4 aut
700a Fenselau, Catherine4 aut
700a Garcia, Benjamin A.4 aut
700a Ge, Ying4 aut
700a Gunawardena, Jeremy4 aut
700a Hendrickson, Ronald C.4 aut
700a Hergenrother, Paul J.4 aut
700a Huber, Christian G.4 aut
700a Ivanov, Alexander R.4 aut
700a Jensen, Ole N.4 aut
700a Jewett, Michael C.4 aut
700a Kelleher, Neil L.4 aut
700a Kiessling, Laura L.4 aut
700a Krogan, Nevan J.4 aut
700a Larsen, Martin R.4 aut
700a Loo, Joseph A.4 aut
700a Loo, Rachel R. Ogorzalek4 aut
700a Lundberg, Emmau KTH,Science for Life Laboratory, SciLifeLab,Stanford Univ, Dept Genet, Stanford, CA 94305 USA4 aut0 (Swepub:kth)u12bylj1
700a MacCoss, Michael J.4 aut
700a Mallick, Parag4 aut
700a Mootha, Vamsi K.4 aut
700a Mrksich, Milan4 aut
700a Muir, Tom W.4 aut
700a Patrie, Steven M.4 aut
700a Pesavento, James J.4 aut
700a Pitteri, Sharon J.4 aut
700a Rodriguez, Henry4 aut
700a Saghatelian, Alan4 aut
700a Sandoval, Wendy4 aut
700a Schluter, Hartmut4 aut
700a Sechi, Salvatore4 aut
700a Slavoff, Sarah A.4 aut
700a Smith, Lloyd M.4 aut
700a Snyder, Michael P.4 aut
700a Thomas, Paul M.4 aut
700a Uhlen, Mathias4 aut
700a Van Eyk, Jennifer E.4 aut
700a Vidal, Marc4 aut
700a Walt, David R.4 aut
700a White, Forest M.4 aut
700a Williams, Evan R.4 aut
700a Wohlschlager, Therese4 aut
700a Wysocki, Vicki H.4 aut
700a Yates, Nathan A.4 aut
700a Young, Nicolas L.4 aut
700a Zhang, Bing4 aut
710a KTHb Science for Life Laboratory, SciLifeLab4 org
773t Nature Chemical Biologyd : NATURE PUBLISHING GROUPg 14:3, s. 206-214q 14:3<206-214x 1552-4450x 1552-4469
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-223782
8564 8u https://doi.org/10.1038/NCHEMBIO.2576

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