Zobrazeno 1 - 10
of 17
pro vyhledávání: '"R. Matthew Ward"'
Autor:
Eric Venner, Andreas Martin Lisewski, Serkan Erdin, R Matthew Ward, Shivas R Amin, Olivier Lichtarge
Publikováno v:
PLoS ONE, Vol 5, Iss 12, p e14286 (2010)
High-throughput Structural Genomics yields many new protein structures without known molecular function. This study aims to uncover these missing annotations by globally comparing select functional residues across the structural proteome. First, Evol
Externí odkaz:
https://doaj.org/article/5c6f76c62a524c0cb33972e40d7150e1
Autor:
R Matthew Ward, Serkan Erdin, Tuan A Tran, David M Kristensen, Andreas Martin Lisewski, Olivier Lichtarge
Publikováno v:
PLoS ONE, Vol 3, Iss 5, p e2136 (2008)
Function prediction frequently relies on comparing genes or gene products to search for relevant similarities. Because the number of protein structures with unknown function is mushrooming, however, we asked here whether such comparisons could be imp
Externí odkaz:
https://doaj.org/article/d39e1689c3b440b2a32d399f57e0c181
Publikováno v:
Systems Biomedicine. 1:29-34
The advent of high-throughput sequencing, coupled with advances in computational methods, has enabled genome-wide dissection of genetics, evolution, and disease, with nucleotide resolution. The discoveries derived from genomics promise benefits to ba
Publikováno v:
Microbial Physiology. 21:36-44
Evolution hinges on the ability of organisms to adapt to their environment. A key regulator of adaptability is mutation rate, which must be balanced to maintain genome fidelity while permitting sufficient plasticity to cope with environmental changes
Publikováno v:
Journal of Molecular Biology. 396:1451-1473
By design, structural genomics (SG) solves many structures that cannot be assigned function based on homology to known proteins. Alternative function annotation methods are therefore needed and this study focuses on function prediction with three-dim
Publikováno v:
Proceedings of the National Academy of Sciences. 110
Structural Genomics aims to elucidate protein structures to identify their functions. Unfortunately, the variation of just a few residues can be enough to alter activity or binding specificity and limit the functional resolution of annotations based
Autor:
David Mittelman, R Matthew Ward
Publikováno v:
eLS
Evolvability is the potential for a biological system to produce variation that can be acted upon by natural selection. Processes that promote selectable variation can facilitate adaptation to dynamic environments. Microsatellite repeats – sequence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c2326c283e0438a32a073a2f0a56eda
https://doi.org/10.1002/9780470015902.a0024945
https://doi.org/10.1002/9780470015902.a0024945
Autor:
Subhajyoti De, R. Matthew Ward
Publikováno v:
Stress-Induced Mutagenesis ISBN: 9781461462798
Mutagenesis is a fundamental biological process by which changes in DNA sequences occur in vivo. On one hand, mutagenesis facilitates adaptation and drives evolution, and on the other hand it leads to diseases such as cancer. Recent advances in high-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5561b8051dad575129bd590a415ada1f
https://doi.org/10.1007/978-1-4614-6280-4_13
https://doi.org/10.1007/978-1-4614-6280-4_13
Autor:
Andreas Martin Lisewski, Serkan Erdin, Shivas R. Amin, Eric Venner, R. Matthew Ward, Olivier Lichtarge
Publikováno v:
PLoS ONE, Vol 5, Iss 12, p e14286 (2010)
PLoS ONE
PLoS ONE
High-throughput Structural Genomics yields many new protein structures without known molecular function. This study aims to uncover these missing annotations by globally comparing select functional residues across the structural proteome. First, Evol
Autor:
Olivier Lichtarge, David M. Kristensen, Andreas Martin Lisewski, Lydia E. Kavraki, Marek Kimmel, R. Matthew Ward, Brian Y. Chen, Viacheslav Y. Fofanov
The annotation of protein function has not kept pace with the exponential growth of raw sequence and structure data. An emerging solution to this problem is to identify 3D motifs or templates in protein structures that are necessary and sufficient de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70a336f91fa601e2e7b071db5196c445
https://europepmc.org/articles/PMC2242527/
https://europepmc.org/articles/PMC2242527/