Zobrazeno 1 - 10 of 56 pro vyhledávání: '"John W. Burgner"'
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Molecular insight into 2-phosphoglycolate activation of the phosphatase activity of bisphosphoglycerate mutase
Autor: Anfal S. Aljahdali, Faik N. Musayev, John W. Burgner, Mohini S. Ghatge, Vibha Shekar, Yan Zhang, Abdelsattar M. Omar, Martin K. Safo
Publikováno v: Acta Crystallographica Section D Structural Biology. 78:472-482
Bisphosphoglycerate mutase (BPGM) is an erythrocyte-specific multifunctional enzyme that is responsible for the regulation of 2,3-bisphosphoglycerate (2,3-BPG) in red blood cells through its synthase and phosphatase activities; the latter enzymatic f
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccd22cc0a33fa0732bd83c045ad82f58
https://doi.org/10.1107/s2059798322001802
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4
Nitrosative stress sensing in Porphyromonas gingivalis: structure of and heme binding by the transcriptional regulator HcpR
Autor: J.N. Scarsdale, Faik N. Musayev, John W. Burgner, Carlos R. Escalante, Janina P. Lewis, B.R. Belvin
Publikováno v: Acta Crystallographica Section D Structural Biology. 75:437-450
Although the HcpR regulator plays a vital step in initiation of the nitrosative stress response in many Gram-negative anaerobic bacteria, the molecular mechanisms that it uses to mediate gas sensing are not well understood. Here, a 2.6 Å resolution
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::597ea6c01d0209e3ec4d792b233794be
https://doi.org/10.1107/s205979831900264x
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5
Akademický článek
The interdomain linker of AAV-2 Rep68 is an integral part of its oligomerization domain: role of a conserved SF3 helicase residue in oligomerization.
Autor: Francisco Zarate-Perez, Martino Bardelli, John W Burgner, Maria Villamil-Jarauta, Kanni Das, Demet Kekilli, Jorge Mansilla-Soto, R Michael Linden, Carlos R Escalante
Publikováno v: PLoS Pathogens, Vol 8, Iss 6, p e1002764 (2012)
The four Rep proteins of adeno-associated virus (AAV) orchestrate all aspects of its viral life cycle, including transcription regulation, DNA replication, virus assembly, and site-specific integration of the viral genome into the human chromosome 19
Externí odkaz: https://doaj.org/article/8383382c475e49a99b405c2aa629f43c
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6
Conformational changes involving ammonia tunnel formation and allosteric control in GMP synthetase
Autor: John W. Burgner, Alexander T. Zwierko, Ravidra Gudihal, Rebecca S. Linger, Anthony M. Pedley, Justin C. Oliver, V. Jo Davisson
Publikováno v: Archives of Biochemistry and Biophysics. 545:22-32
GMP synthetase is the glutamine amidotransferase that catalyzes the final step in the guanylate branch of de novo purine biosynthesis. Conformational changes are required to efficiently couple distal active sites in the protein; however, the nature o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::429b9d53b0a1a8981812f6816cefd8dd
https://doi.org/10.1016/j.abb.2014.01.004
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7
Structure of Factor H-binding Protein B (FhbB) of the Periopathogen, Treponema denticola
Autor: Daniel H. Conrad, Annie Heroux, Jessica K. Bell, John W. Burgner, John V. McDowell, Daniel P. Miller, Richard T. Marconi
Publikováno v: Journal of Biological Chemistry. 287:12715-12722
Periodontitis is the most common disease of microbial etiology in humans. Periopathogen survival is dependent upon evasion of complement-mediated destruction. Treponema denticola, an important contributor to periodontitis, evades killing by the alter
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c8a4e1a97b3f3b0c36611098999ace9f
https://doi.org/10.1074/jbc.m112.339721
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8
Folding dynamics of phenylalanine hydroxylase depends on the enzyme’s metallation state: the native metal, iron, protects against aggregate intermediates
Autor: Judith A. Ronau, Mahdi M. Abu-Omar, Aristobulo Loaiza, Lake N. Paul, Alexander E. Ribbe, John W. Burgner, Lia Stanciu
Publikováno v: European Biophysics Journal. 40:959-968
Phenylalanine hydroxylase (PAH), a non-heme iron enzyme, is responsible for the phenylalanine conversion to tyrosine. Its malfunction causes phenylketonuria (PKU). To better understand how protein structure and folding profiles are affected by the me
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f997b7649826bfee8f3fd9854ff2f1b6
https://doi.org/10.1007/s00249-011-0711-6
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9
Identification of the structural motif responsible for trimeric assembly of the C-terminal regulatory domains of polycystin channels PKD2L1 and PKD2
Autor: Dinesh Yernool, John W. Burgner, Anoop Narayanan, Katrina L. Molland
Publikováno v: Biochemical Journal. 429:171-183
Polycystin 2-type cation channels PKD2 and PKD2L1 interact with polycystin 1-type proteins PKD1 and PKD1L3 respectively, to form receptor–cation-channel complexes. The PKD2L1–PKD1L3 complex perceives sour taste, whereas disruption of the PKD2–P
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f70fed7f543ea51481f794958fb974ed
https://doi.org/10.1042/bj20091843
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10
Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling
Autor: John W. Burgner, Robert L. Geahlen, Yajie Zhang, Hyunju Oh, Carol Beth Post, Robert A. Burton
Publikováno v: Proceedings of the National Academy of Sciences. 105:11760-11765
The Syk protein-tyrosine kinase plays a major role in signaling through the B cell receptor for antigen (BCR). Syk binds the receptor via its tandem pair of SH2 domains interacting with a doubly phosphorylated immunoreceptor tyrosine-based activation
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b516921604466c80019ab5a08954748
https://doi.org/10.1073/pnas.0708583105
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