Zobrazeno 1 - 9
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pro vyhledávání: '"T. Scott Chen"'
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 5, p e1004248 (2015)
We describe a method to predict protein-protein interactions (PPIs) formed between structured domains and short peptide motifs. We take an integrative approach based on consensus patterns of known motifs in databases, structures of domain-motif compl
Externí odkaz:
https://doaj.org/article/894ded1395b44302ae8197901d301530
Publikováno v:
Methods in Molecular Biology ISBN: 9781493967964
PMC
PMC
Peptide reagents with high affinity or specificity for their target protein interaction partner are of utility for many important applications. Optimization of peptide binding by screening large libraries is a proven and powerful approach. Libraries
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51dc45c45477be4d7fb7909df5fa64b8
https://europepmc.org/articles/PMC5553629/
https://europepmc.org/articles/PMC5553629/
Publikováno v:
Journal of Molecular Biology. 425:171-185
Many native proteins are multi-specific and interact with numerous partners, which can confound analysis of their functions. Protein design provides a potential route to generating synthetic variants of native proteins with more selective binding pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce41db1939817390bdd6ffea630ca767
https://doi.org/10.1016/j.jmb.2012.11.009
https://doi.org/10.1016/j.jmb.2012.11.009
Autor:
T. Scott Chen, Amy E. Keating
Publikováno v:
Protein Science. 21:949-963
Given the importance of protein-protein interactions for nearly all biological processes, the design of protein affinity reagents for use in research, diagnosis or therapy is an important endeavor. Engineered proteins would ideally have high specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d84f0fa04b4c9e7015788f1b9b9ae024
https://doi.org/10.1002/pro.2096
https://doi.org/10.1002/pro.2096
Publikováno v:
Journal of Molecular Biology. 398:747-762
Interactions among Bcl-2 family proteins are important for regulating apoptosis. Prosurvival members of the family interact with proapoptotic BH3 (Bcl-2-homology-3)-only members, inhibiting execution of cell death through the mitochondrial pathway. S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d522d40c3880a90cf57c93175607d98
https://doi.org/10.1016/j.jmb.2010.03.058
https://doi.org/10.1016/j.jmb.2010.03.058
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 5, p e1004248 (2015)
PLoS Computational Biology
PLoS Computational Biology
We describe a method to predict protein-protein interactions (PPIs) formed between structured domains and short peptide motifs. We take an integrative approach based on consensus patterns of known motifs in databases, structures of domain-motif compl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::723c375a6ff1bbebd7482c3db6de70c5
http://europepmc.org/articles/PMC4418708?pdf=render
http://europepmc.org/articles/PMC4418708?pdf=render
Autor:
Jeremy Ryan, T. Scott Chen, Sanjib Dutta, Christos Kougentakis, Anthony Letai, Amy E. Keating
Publikováno v:
PMC
The Bcl-2 family of proteins plays a critical role regulating apoptosis, and pro-survival Bcl-2 family members are important therapeutic targets due to their overexpression in different cancers. Pro-apoptotic Bcl-2 homology 3 (BH3)-only proteins anta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96339918b367bac10925dd7001d681c7
https://pubmed.ncbi.nlm.nih.gov/25555991
https://pubmed.ncbi.nlm.nih.gov/25555991
Publikováno v:
ACS chemical biology. 8(4)
Pro-survival members of the Bcl-2 protein family inhibit cell death by binding short helical BH3 motifs in pro-apoptotic proteins. Mammalian pro-survival proteins Bcl-x(L), Bcl-2, Bcl-w, Mcl-1, and Bfl-1 bind with varying affinities and specificities
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c92cbf78e38b0af9dc215235d9d2c47
https://pubmed.ncbi.nlm.nih.gov/23363053
https://pubmed.ncbi.nlm.nih.gov/23363053
Publikováno v:
Journal of the American Chemical Society. 130(29)
We report a new method for detection of protein-protein interactions in vitro and in cells. One protein partner is fused to Escherichia coli biotin ligase (BirA), while the other protein partner is fused to BirA's "acceptor peptide" (AP) substrate. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79b12ab5722d7523b068c9ef1a696878
https://pubmed.ncbi.nlm.nih.gov/18582056
https://pubmed.ncbi.nlm.nih.gov/18582056