Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Piers Nash"'
Autor:
Aldo Vacaflores, Piers Nash, Jonathan Light, Jon C. D. Houtman, Rebekah R. Bartelt, Alayna K. Butcher, Madhana Pandian
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853(10):2560-2569
SH3 domains are evolutionarily conserved protein interaction domains that control nearly all cellular processes in eukaryotes. The current model is that most SH3 domains bind discreet PxxPxR motifs with weak affinity and relatively low selectivity. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60448937bc0e09aacbf2ba319f23ccef
Publikováno v:
Molecular & Cellular Proteomics. 13:3647-3662
Protein interaction domain (PID) linear peptide motif interactions direct diverse cellular processes in a specific and coordinated fashion. PID specificity, or the interaction selectivity derived from affinity preferences between possible PID-peptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87e52c0881cb6d5148fdf8c6a3ae81f2
https://doi.org/10.1074/mcp.o114.038695
https://doi.org/10.1074/mcp.o114.038695
Autor:
Stuti Agrawal, A. C. Heath, Joe Mambretti, Jim Chen, Robert L. Grossman, Zhenyu Zhang, Piers Nash, Renuka Arya, Fei Yeh
Publikováno v:
ICIN
This paper describes a Bioinformatics Software Defined Network Exchange (SDX) or BioSDX, which has been designed, deployed, and demonstrated by a multi-organizational research consortium to enable bioinformatics knowledge discovery supported by dynam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14106a0999b10d4414adcd6e000d5ced
https://doi.org/10.1109/icin.2017.7899403
https://doi.org/10.1109/icin.2017.7899403
Publikováno v:
PROTEOMICS. 12:1527-1546
Modular protein interaction domains (PIDs) that recognize linear peptide motifs are found in hundreds of proteins within the human genome. Some PIDs such as SH2, 14-3-3, Chromo, and Bromo domains serve to recognize posttranslational modification (PTM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e8eb4432836340d087aedaecabce5e8
https://doi.org/10.1002/pmic.201100599
https://doi.org/10.1002/pmic.201100599
Publikováno v:
Journal of Biological Chemistry. 285:37895-37908
Reversible ubiquitination orchestrated by the opposition of ubiquitin ligases and deubiquitinating enzymes mediates endocytic trafficking of cell surface receptors for lysosomal degradation. Ubiquitin-specific protease 8 (USP8) has previously been im
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eea1a11e3d6b70f84b1471c0d1559316
https://doi.org/10.1074/jbc.m110.129411
https://doi.org/10.1074/jbc.m110.129411
Publikováno v:
Journal of Biological Chemistry. 285:13990-14004
Reversible ubiquitination is essential for the endocytic sorting and down-regulation of G protein-coupled receptors, such as the chemokine receptor CXCR4. The deubiquitinating enzyme AMSH has been implicated in the endocytic sorting of both G protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d619c424c55f347b44069b6e758c08b
https://doi.org/10.1074/jbc.m109.061309
https://doi.org/10.1074/jbc.m109.061309
Autor:
Kazuya Machida, Bernard A. Liu, Christopher M. Thompson, Haimin Zhang, Bruce J. Mayer, Kevin Dierck, G. Herma Renkema, Piers Nash, Karl Jablonowski, Kalle Saksela, Martin R. Schiller, Peter Nollau, Dong-Guk Shin, Tony Pawson, Debra K. Newman, Satu Kärkkäinen
Publikováno v:
Molecular Cell. 26:899-915
Protein tyrosine phosphorylation controls many aspects of signaling in multicellular organisms. One of the major consequences of tyrosine phosphorylation is the creation of binding sites for proteins containing Src homology 2 (SH2) domains. To profil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3bf9f83621cc670c68521adc9fe4a80
https://doi.org/10.1016/j.molcel.2007.05.031
https://doi.org/10.1016/j.molcel.2007.05.031
Publikováno v:
Molecular Cell. 22(6):851-868
SH2 domains are interaction modules uniquely dedicated to the recognition of phosphotyrosine sites and are embedded in proteins that couple protein-tyrosine kinases to intracellular signaling pathways. Here, we report a comprehensive bioinformatics,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::850b6f2f2cb730471288cc1a857119f9
Autor:
Li Ying Liu, Yun Ming Sun, Peter C. Turner, Alexandra Lucas, Babajide Togonu-Bickersteth, Piers Nash, Xing Li, Grant McFadden, Colin Macaulay, Richard W. Moyer, Jakob Richardson, Kasinath Viswanathan, Erbin Dai, Steven H. Nazarian
Publikováno v:
Journal of Biological Chemistry. 281:8041-8050
The thrombolytic serine protease cascade is intricately involved in activation of innate immune responses. The urokinase-type plasminogen activator and receptor form complexes that aid inflammatory cell invasion at sites of arterial injury. Plasminog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9881b1415d7339c733fa5b49272027ad
https://doi.org/10.1074/jbc.m509454200
https://doi.org/10.1074/jbc.m509454200