Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Paul Bajaj"'
Autor:
Ruzanna Shkhyan, Candace Flynn, Emma Lamoure, Arijita Sarkar, Benjamin Van Handel, Jinxiu Li, Jesse York, Nicholas Banks, Robert Van der Horst, Nancy Q. Liu, Siyoung Lee, Paul Bajaj, Kanagasabai Vadivel, Hans I.-Chen Harn, Jade Tassey, Thomas Lozito, Jay R. Lieberman, Cheng-Ming Chuong, Mark S. Hurtig, Denis Evseenko
Publikováno v:
Science Translational Medicine. 15
Adult mammals are incapable of multitissue regeneration, and augmentation of this potential may shift current therapeutic paradigms. We found that a common co-receptor of interleukin 6 (IL-6) cytokines, glycoprotein 130 (gp130), serves as a major nex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef607d91f2e813b92d0b8895ab74a986
https://doi.org/10.1126/scitranslmed.abq2395
https://doi.org/10.1126/scitranslmed.abq2395
Autor:
Kaillathe Padmanabhan, Sriram Krishnaswamy, Hans Brandstetter, Amy E. Schmidt, Duilio Cascio, S. Paul Bajaj, Kanagasabai Vadivel
Publikováno v:
Acta Crystallogr D Struct Biol
Coagulation factor VIIa (FVIIa) consists of a γ-carboxyglutamic acid (GLA) domain, two epidermal growth factor-like (EGF) domains and a protease domain. FVIIa binds three Mg2+ ions and four Ca2+ ions in the GLA domain, one Ca2+ ion in the EGF1 domai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::768553e62fbb6b3b4a9e8f6a22f86808
https://doi.org/10.1107/s2059798321003922
https://doi.org/10.1107/s2059798321003922
Autor:
Ruzanna Shkhyan, Candace Flynn, Emma Lamoure, Ben Van Handel, Arijita Sarkar, Jinxiu Li, Jesse York, Nicholas Banks, Robert Van der Horst, Nancy Q. Liu, Siyoung Lee, Paul Bajaj, Kanagasabai Vadivel, Hans I-Chen Harn, Thomas Lozito, Jay R. Lieberman, Cheng-Ming Chuong, Mark S. Hurtig, Denis Evseenko
Adult mammals are incapable of multi-tissue regeneration and augmentation of this potential may drastically shift current therapeutic paradigms. Here, we found that a common co-receptor of IL-6 cytokines, glycoprotein 130 (gp130), serves as a major n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::755a927b4e7c0cb3ff217eb67127cea6
https://doi.org/10.1101/2022.01.05.475124
https://doi.org/10.1101/2022.01.05.475124
Autor:
S. Paul Bajaj, Wallace G. Buchholz, Yogesh Kumar, William H. Velander, Anne K. Zaiss, Kanagasabai Vadivel, Frank M. Fabian, Ayman E.A. Ismail, Mark A. Arbing
Publikováno v:
Journal of Clinical Medicine
Volume 9
Issue 11
Journal of Clinical Medicine, Vol 9, Iss 3684, p 3684 (2020)
Volume 9
Issue 11
Journal of Clinical Medicine, Vol 9, Iss 3684, p 3684 (2020)
Current antifibrinolytic agents reduce blood loss by inhibiting plasmin active sites (e.g., aprotinin) or by preventing plasminogen/tissue plasminogen activator (tPA) binding to fibrin clots (e.g., &epsilon
aminocaproic acid and tranexamic acid)
aminocaproic acid and tranexamic acid)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0935886b2e9c1673280acf45caf7651a
https://pubmed.ncbi.nlm.nih.gov/33212896
https://pubmed.ncbi.nlm.nih.gov/33212896
Publikováno v:
J Thromb Haemost
Background Factor (F) IX/IXa inactivation by plasmin has been studied; however, whether plasmin converts FIXa to a fibrinolytic enhancer is not known. Objective Investigate plasmin proteolysis site(s) in FIXa that inactivates and transforms it into a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7249ec3a6e30607ba7c9601c0525779
https://europepmc.org/articles/PMC7363452/
https://europepmc.org/articles/PMC7363452/
Autor:
Gabriel B. Ferguson, Paul Bajaj, C. Thomas Vangsness, Ruzanna Shkhyan, Liming Wang, Denis Evseenko, Mila Scheinberg, Carlos Eduardo da Silveira Franciozi, Yifan Yu, Varghese John, Ling Wu, Sean Limfat, Mohammad Parvez Alam, Arthur Chernostrik, Nicholas W. Banks, Ben Van Handel, Jacob Bogdanov, Siyoung Lee, Kanagasabai Vadivel, Nancy Q. Liu, Frank A. Petrigliano, Ali Nsair
Publikováno v:
Annals of the Rheumatic Diseases. 77:760-769
ObjectiveHuman adult articular cartilage (AC) has little capacity for repair, and joint surface injuries often result in osteoarthritis (OA), characterised by loss of matrix, hypertrophy and chondrocyte apoptosis. Inflammation mediated by interleukin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdcd7cf806ca4e7d94c37aae01c54d5d
https://doi.org/10.1136/annrheumdis-2017-212037
https://doi.org/10.1136/annrheumdis-2017-212037
Autor:
Kanagasabai, Vadivel, Yogesh, Kumar, Matthew W, Bunce, Rodney M, Camire, Madhu S, Bajaj, S Paul, Bajaj
Publikováno v:
International biology review. 1(1)
Factor V (FV) B-domain contains an acidic region (FV-AR2) and a basic region (FV-BR), which interact with each other and maintain FV in a procofactor form; removal of either region via deletion/proteolysis results in an active FVa molecule. Tissue fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e46c09492632e49a1153732a0922b809
https://pubmed.ncbi.nlm.nih.gov/28845483
https://pubmed.ncbi.nlm.nih.gov/28845483
Autor:
Sathya-Moorthy Ponnuraj, Denis Evseenko, Rodney M. Camire, Harvey R. Herschman, Anne K. Zaiss, Yogesh Kumar, Kanagasabai Vadivel, Matthew W. Bunce, S. Paul Bajaj, Ling Wu, Madhu S. Bajaj
Publikováno v:
The Journal of biological chemistry, vol 289, iss 45
Tissue factor pathway inhibitor-2 (TFPI-2) is a homologue of TFPI-1 and contains three Kunitz-type domains and a basic C terminus region. The N-terminal domain of TFPI-2 is the only inhibitory domain, and it inhibits plasma kallikrein, factor XIa, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0778522137da0e304b8e562b469b4aae
https://doi.org/10.1074/jbc.m114.569665
https://doi.org/10.1074/jbc.m114.569665
Autor:
S. Paul Bajaj, Sayeh Agah, Kanagasabai Vadivel, Madhu S. Bajaj, Kaillathe Padmanabhan, Duilio Cascio, Charles T. Esmon, Sriram Krishnaswamy, Amanda S. Messer
Publikováno v:
Journal of Molecular Biology. 425:1961-1981
Crystal structures of factor (F) VIIa/soluble tissue factor (TF), obtained under high Mg(2+) (50mM Mg(2+)/5mM Ca(2+)), have three of seven Ca(2+) sites in the γ-carboxyglutamic acid (Gla) domain replaced by Mg(2+) at positions 1, 4, and 7. We now re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09b2104a1306c029bd9399574f99dbb7
https://doi.org/10.1016/j.jmb.2013.02.017
https://doi.org/10.1016/j.jmb.2013.02.017
Autor:
Stephen B. Smith, David Gailani, Mao-fu Sun, Yipeng Geng, S. Paul Bajaj, Ingrid M. Verhamme, Amanda S. Messer
Publikováno v:
Journal of Biological Chemistry. 287:38200-38209
During blood coagulation, the protease factor XIa (fXIa) activates factor IX (fIX). We describe a new mechanism for this process. FIX is cleaved initially after Arg(145) to form fIXα, and then after Arg(180) to form the protease fIXaβ. FIXα is rel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ce1f9c41ca00070fd1184de6d18dc3e
https://doi.org/10.1074/jbc.m112.376343
https://doi.org/10.1074/jbc.m112.376343