Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Mark E. Girvin"'
Publikováno v:
Heliyon, Vol 5, Iss 12, Pp e03018- (2019)
Fusion of host and viral membranes is a crucial step during infection by enveloped viruses. In the structurally-defined “class I″ viral glycoproteins, the formation of a highly stable α-helical bundle by the ectodomain of the fusion subunit (e.g
Externí odkaz:
https://doaj.org/article/88e0fc27349c42b0b3da94250547d8be
Autor:
Ganjam V. Kalpana, P. Rajesh Kumar, Steven C. Almo, Liming Qiu, Savita Bhutoria, Seetharama A. Acharya, Xiaoqin Zou, Sheeba Mathew, Lucas J. Adams, Richard Harris, Minh B. Nguyen, Updesh Dixit, Alasdair C. Steven, Xuhong Wu, Michael Brenowitz, Menachem Spira, Sean M. Cahill, Rajiv Pathak, Mark E. Girvin, David Cowburn
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
INI1/SMARCB1 binds to HIV-1 integrase (IN) through its Rpt1 domain and exhibits multifaceted role in HIV-1 replication. Determining the NMR structure of INI1-Rpt1 and modeling its interaction with the IN-C-terminal domain (IN-CTD) reveal that INI1-Rp
Autor:
Jerome M. Karp, Sean M. Cahill, Michael Brenowitz, Takashi Onikubo, Christopher D. Warren, David Shechter, Mark E. Girvin, David Cowburn, Tsutomu Matsui
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-16 (2017)
Nature Communications
Nature Communications
Nucleoplasmin (Npm) is a highly conserved histone chaperone responsible for the maternal storage and zygotic release of histones H2A/H2B. Npm contains a pentameric N-terminal core domain and an intrinsically disordered C-terminal tail domain. Though
Publikováno v:
Proceedings of the National Academy of Sciences. 113:14312-14317
We are just beginning to understand the allosteric regulation of the human cytosolic sulfotransferase (SULTs) family-13 disease-relevant enzymes that regulate the activities of hundreds, if not thousands, of signaling small molecules. SULT1A1, the pr
Publikováno v:
Heliyon
Heliyon, Vol 5, Iss 12, Pp e03018-(2019)
Heliyon, Vol 5, Iss 12, Pp e03018-(2019)
Fusion of host and viral membranes is a crucial step during infection by enveloped viruses. In the structurally-defined “class I″ viral glycoproteins, the formation of a highly stable α-helical bundle by the ectodomain of the fusion subunit (e.g
Native mass spectrometry detection of ligand-protein complexes allowed rapid detection of natural product binders of apo and calcium-bound S100A4 (a member of the metal binding protein S100 family), T cell/transmembrane, immunoglobulin (Ig), and muci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f98c2e959a4d91b6105ac71b3f1b569
https://europepmc.org/articles/PMC6195442/
https://europepmc.org/articles/PMC6195442/
Publikováno v:
Biochemistry. 54:1589-1599
Fusion of host and viral membranes is a critical step during infection by membrane-bound viruses. The HIV-1 glycoproteins gp120 (surface subunit) and gp41 (fusion subunit) represent the prototypic system for studying this process; in the prevailing m
Publikováno v:
Biomolecular NMR Assignments. 8:103-108
The type I phosphoribosyltransferase OMP synthase (EC 2.4.2.10) is involved in de novo synthesis of pyrimidine nucleotides forming the UMP precursor orotidine 5′-monophosphate (OMP). The homodimeric enzyme has a Rossman α/β core topped by a base-
Autor:
Richard Harris, Mark E. Girvin, Camille Padlan, Yisong Tao, Aristea S. Galanopoulou, Sergei Khrapunov, Michael Brenowitz, John M. Greally, Huiyong Cheng
Publikováno v:
Biochemistry. 55(31)
Methyl-CpG binding protein 2 (MeCP2) is a multifunctional protein that guides neuronal development through its binding to DNA, recognition of sites of methyl-CpG (mCpG) DNA modification, and interaction with other regulatory proteins. Our study explo
Autor:
Ming Zhou, Filippo Mancia, Gaetano T. Montelione, Wayne A. Hendrickson, Thomas Szyperski, Ann E. McDermott, Da-Neng Wang, Marco Punta, Burkhard Rost, Barry Honig, J. Love, Lawrence Shapiro, Mark E. Girvin, Masayori Inouye, Eric Gouaux, John F. Hunt, Roderick MacKinnon
Publikováno v:
Journal of Structural and Functional Genomics. 11:191-199
The New York Consortium on Membrane Protein Structure (NYCOMPS) was formed to accelerate the acquisition of structural information on membrane proteins by applying a structural genomics approach. NY-COMPS comprises a bioinformatics group, a centraliz