Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Leslie D. Burtnick"'
Autor:
Caroline L. Bellac, Antoine Dufour, Michael J. Krisinger, Anantasak Loonchanta, Amanda E. Starr, Ulrich auf dem Keller, Philipp F. Lange, Verena Goebeler, Reinhild Kappelhoff, Georgina S. Butler, Leslie D. Burtnick, Edward M. Conway, Clive R. Roberts, Christopher M. Overall
Publikováno v:
Cell Reports, Vol 9, Iss 2, Pp 618-632 (2014)
Resolution of inflammation reduces pathological tissue destruction and restores tissue homeostasis. Here, we used a proteomic protease substrate discovery approach, terminal amine isotopic labeling of substrates (TAILS), to analyze the role of the ma
Externí odkaz:
https://doaj.org/article/54232a9bc7164ad28c7741c5076d0c8e
Autor:
Dávid Szatmári, Bo Xue, Balakrishnan Kannan, Leslie D Burtnick, Beáta Bugyi, Miklós Nyitrai, Robert C Robinson
Publikováno v:
PLoS ONE, Vol 13, Iss 8, p e0201826 (2018)
Gelsolin is a severing and capping protein that targets filamentous actin and regulates filament lengths near plasma membranes, contributing to cell movement and plasma membrane morphology. Gelsolin binds to the plasma membrane via phosphatidylinosit
Externí odkaz:
https://doaj.org/article/ab42201a92cd4bdb83d17d0db395c289
Autor:
Robert Robinson, Inge Everaert, Leslie D. Burtnick, Adriaan Verhelle, Ariane De Ganck, Claude Cuvelier, Tino Hochepied, Jan Gettemans, Wim Derave, Wouter Van Overbeke, Anantasak Loonchanta, Jody J. Haigh, Olivier Zwaenepoel, Jantana Wongsantichon
Publikováno v:
Human Molecular Genetics. 24:2492-2507
Hereditary gelsolin amyloidosis is an autosomal dominantly inherited amyloid disorder. A point mutation in the GSN gene (G654A being the most common one) results in disturbed calcium binding by the second gelsolin domain (G2). As a result, the foldin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e429f228e030d07db18bb2bb265bf15d
https://doi.org/10.1093/hmg/ddv010
https://doi.org/10.1093/hmg/ddv010
Autor:
Reinhild Kappelhoff, Antoine Dufour, Michael J. Krisinger, Christopher M. Overall, Verena Goebeler, Edward M. Conway, Ulrich auf dem Keller, Leslie D. Burtnick, Clive R. Roberts, Philipp F. Lange, Anantasak Loonchanta, Caroline L. Bellac, Amanda E. Starr, Georgina S. Butler
Publikováno v:
Cell Reports, 9 (2)
Cell Reports, Vol 9, Iss 2, Pp 618-632 (2014)
Cell Reports, Vol 9, Iss 2, Pp 618-632 (2014)
Resolution of inflammation reduces pathological tissue destruction and restores tissue homeostasis. Here, we used a proteomic protease substrate discovery approach, terminal amine isotopic labeling of substrates (TAILS), to analyze the role of the ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e44c1c783b48c73aee265fb5d75071b2
https://doi.org/10.1016/j.celrep.2014.09.006
https://doi.org/10.1016/j.celrep.2014.09.006
Publikováno v:
Cytoskeleton. 70:775-795
The gelsolin homology (GH) domain has been found to date exclusively in actin-binding proteins. In humans, three copies of the domain are present in CapG, five copies in supervillin, and six copies each in adseverin, gelsolin, flightless I and the vi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b904ad3bcd9b547c19fda78bcf7fb9ae
https://doi.org/10.1002/cm.21149
https://doi.org/10.1002/cm.21149
Publikováno v:
Cytoskeleton. 70:360-384
Gelsolin superfamily members are Ca(2+) -dependent, multidomain regulators of the actin cytoskeleton. Calcium binding activates gelsolin by inducing molecular gymnastics (large-scale conformational changes) that expose actin interaction surfaces by r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f24d8da403b0a3d67f3dec31bcf140cb
https://doi.org/10.1002/cm.21117
https://doi.org/10.1002/cm.21117
Autor:
Jonathan M. Grimes, Leslie D. Burtnick, E Y Jones, Edward K. Koepf, P J McLaughlin, Robert Robinson, David I. Stuart
The structure of gelsolin has been determined by crystallography and comprises six structurally related domains that, in a Ca2+-free environment, pack together to form a compact globular structure in which the putative actin-binding sequences are not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3844984e0a504c3cf5e6eff38c9e6940
https://doi.org/10.1016/s0092-8674(00)80527-9
https://doi.org/10.1016/s0092-8674(00)80527-9
Autor:
Soerge Kelm, Nathan R. Zaccai, Robert Robinson, E. Yvonne Jones, Andrew May, Leslie D. Burtnick, Reinhard Brossmer, Paul R. Crocker
The Siglec family of receptors mediates cell-surface interactions through recognition of sialylated glycoconjugates. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0b7a9debd3993e0c589c513240c4e70
https://doi.org/10.1016/j.jmb.2006.10.084
https://doi.org/10.1016/j.jmb.2006.10.084
Publikováno v:
Cytoskeleton. 67:456-465
Heat shock proteins act as cytoplasmic chaperones to ensure correct protein folding and prevent protein aggregation. The presence of stoichiometric amounts of one such heat shock protein, Hsp27, in supersaturated solutions of unmodified G-actin leads
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::976be8165bf94ba723a90569135ed041
https://doi.org/10.1002/cm.20458
https://doi.org/10.1002/cm.20458
Autor:
Robert Robinson, Sakesit Chumnarnsilpa, Balakrishnan Kannan, Wei Lin Lee, Mårten Larsson, Leslie D. Burtnick, Shalini Nag
Publikováno v:
Proceedings of the National Academy of Sciences. 106:13719-13724
Adseverin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins. Adseverin comprises 6 homologous domains (A1–A6), which share 60% identity with the 6 domains from gelsolin (G1–G6). Adseverin is truncate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8a35e465e7e42458ee60ec84cf2ada0
https://doi.org/10.1073/pnas.0812383106
https://doi.org/10.1073/pnas.0812383106