Zobrazeno 1 - 10
of 132
pro vyhledávání: '"Jeffrey W Keillor"'
Publikováno v:
PLoS ONE, Vol 13, Iss 5, p e0197956 (2018)
Transglutaminases (TGases) are enzymes that catalyse protein cross-linking through a transamidation reaction between the side chain of a glutamine residue on one protein and the side chain of a lysine residue on another. Generally, TGases show low su
Externí odkaz:
https://doaj.org/article/f3111e0383054e9ea66fb1eb70d74673
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e44159 (2012)
Transglutaminase type 2 (TG2) is a ubiquitously expressed member of the transglutaminase family, capable of mediating a transamidation reaction between a variety of protein substrates. TG2 also has a unique role as a G-protein with GTPase activity. I
Externí odkaz:
https://doaj.org/article/2d76fbbf5684427e8648108ce2c39b5f
Autor:
Hadil F Al-Jallad, Vamsee D Myneni, Sarah A Piercy-Kotb, Nicolas Chabot, Amina Mulani, Jeffrey W Keillor, Mari T Kaartinen
Publikováno v:
PLoS ONE, Vol 6, Iss 1, p e15893 (2011)
Transglutaminase activity, arising potentially from transglutaminase 2 (TG2) and Factor XIIIA (FXIIIA), has been linked to osteoblast differentiation where it is required for type I collagen and fibronectin matrix deposition. In this study we have us
Externí odkaz:
https://doaj.org/article/391e9309bc0b4d7599052a630beb9019
Publikováno v:
PLoS ONE, Vol 6, Iss 1, p e16665 (2011)
Transglutaminase 2 (TG2) is a hypoxia-responsive protein that is a calcium-activated transamidating enzyme, a GTPase and a scaffolding/linker protein. Upon activation TG2 undergoes a large conformational change, which likely affects not only its enzy
Externí odkaz:
https://doaj.org/article/16e99df9435843f5bd5cbda98d3ed2cb
Autor:
Xian-Yang Qin, Yutaka Furutani, Kento Yonezawa, Nobutaka Shimizu, Miyuki Kato-Murayama, Mikako Shirouzu, Yali Xu, Yumiko Yamano, Akimori Wada, Luc Gailhouste, Rajan Shrestha, Masataka Takahashi, Jeffrey W. Keillor, Ting Su, Wenkui Yu, Shinya Fujii, Hiroyuki Kagechika, Naoshi Dohmae, Yohei Shirakami, Masahito Shimizu, Takahiro Masaki, Tomokazu Matsuura, Harukazu Suzuki, Soichi Kojima
Publikováno v:
Cell Death and Disease, Vol 14, Iss 6, Pp 1-15 (2023)
Abstract Transglutaminase 2 (TG2) is a multifunctional protein that promotes or suppresses tumorigenesis, depending on intracellular location and conformational structure. Acyclic retinoid (ACR) is an orally administered vitamin A derivative that pre
Externí odkaz:
https://doaj.org/article/6988d4bd40ae412bb6f755ac1f920c89
Autor:
Pauline Navals, Alana M. M. Rangaswamy, Petr Kasyanchyk, Maxim V. Berezovski, Jeffrey W. Keillor
Publikováno v:
Biomolecules, Vol 14, Iss 4, p 496 (2024)
TG2 is a unique member of the transglutaminase family as it undergoes a dramatic conformational change, allowing its mutually exclusive function as either a cross-linking enzyme or a G-protein. The enzyme’s dysregulated activity has been implicated
Externí odkaz:
https://doaj.org/article/64ea9546ac7147b4a2259c38a6b2c1c6
Autor:
Eric W. J. Gates, Kian Mansour, Sahar Ebrahimi Samani, Sammir Shad, Mari T. Kaartinen, Jeffrey W. Keillor
Publikováno v:
Molecules, Vol 28, Iss 4, p 1634 (2023)
Factor XIIIa (FXIIIa) is a transglutaminase of major therapeutic interest for the development of anticoagulants due to its essential role in the blood coagulation cascade. While numerous FXIIIa inhibitors have been reported, they failed to reach clin
Externí odkaz:
https://doaj.org/article/e92054fde8f9454ab0c53c53e73e74ef
Autor:
Ariel Buchler, Uzair S. Ismailani, Nicole MacMullin, Faduma Abdirahman, Myriam Adi, Christina Bi, Catherine Jany, Jeffrey W. Keillor, Benjamin H. Rotstein
Publikováno v:
Journal of Medicinal Chemistry. 66:6682-6696
Autor:
Lavleen Mader, Sarah K. I. Watt, Harish R. Iyer, Linh Nguyen, Harpreet Kaur, Jeffrey W. Keillor
Publikováno v:
RSC Medicinal Chemistry. 14:277-298
This systematic structure–activity relationship study provides key insights into warhead design and application for optimizing efficiency, selectivity, and pharmacokinetic stability of hTG2 inhibitors.
Publikováno v:
Organic & Biomolecular Chemistry. 21:2204-2212
A kinetic study of the reaction mechanism of the thiol addition reaction of the acryloyl piperidine ‘warhead’ reveals its intrinsic reactivity and thiol sensitivity, which are relevant to inhibitor design.