Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Agustin O. Pineda"'
Autor:
Agustin O. Pineda, Leslie A. Bush-Pelc, Francesca Marino, Zhi-wei Chen, F. Scott Mathews, Enrico Di Cera
Publikováno v:
Journal of Biological Chemistry. 282:27165-27170
Little is known on the role of disulfide bonds in the catalytic domain of serine proteases. The Cys-191-Cys-220 disulfide bond is located between the 190 strand leading to the oxyanion hole and the 220-loop that contributes to the architecture of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e810ddc4744044d20e6de7ceb695f5e
https://doi.org/10.1074/jbc.m703202200
https://doi.org/10.1074/jbc.m703202200
Autor:
Agustin O. Pineda, Christodoulos S. Flordellis, F. Scott Mathews, Michael E. Maragoudakis, Nikos E. Tsopanoglou, M. E. Papaconstantinou, Christopher J. Carrell, Kevin M. Bobofchak, Enrico Di Cera
Publikováno v:
Journal of Biological Chemistry. 280:29393-29396
Previous studies have suggested that thrombin interacts with integrins in endothelial cells through its RGD (Arg-187, Gly-188, Asp-189) sequence. All existing crystal structures of thrombin show that most of this sequence is buried under the 220-loop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::904fa8d56bee74cfc0fa3ca567e01529
https://doi.org/10.1074/jbc.c500248200
https://doi.org/10.1074/jbc.c500248200
Publikováno v:
Journal of Biological Chemistry. 280:25644-25650
The oxyanion hole of serine proteases is formed by the backbone N atoms of the catalytic Ser-195 and Gly-193 and engages the backbone O atom of the P1 residue of substrate in an important H-bonding interaction. The energetic contribution of this inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63f93220bbc131a0681c8427d4c85b89
https://doi.org/10.1074/jbc.m503499200
https://doi.org/10.1074/jbc.m503499200
Autor:
Annette J. Eckardt, Enrico Di Cera, Jack A. Kauffman, Edward C. Giardino, Thomas W. Corcoran, Michael N. Greco, Bruce E. Maryanoff, Lawrence de Garavilla, Claudia K. Derian, Narayanasami Sukumar, Barbara J. Haertlein, Zhi-wei Chen, Bruce P. Damiano, Grace I. Wells, Patricia Andrade-Gordon, F. Scott Mathews, Agustin O. Pineda
Publikováno v:
Journal of Biological Chemistry. 280:18001-18007
Certain leukocytes release serine proteases that sustain inflammatory processes and cause disease conditions, such as asthma and chronic obstructive pulmonary disease. We identified beta-ketophosphonate 1 (JNJ-10311795; RWJ-355871) as a novel, potent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2bb41a9acbf419e02cb964ca95c9e201
https://doi.org/10.1074/jbc.m501302200
https://doi.org/10.1074/jbc.m501302200
Publikováno v:
Journal of Biological Chemistry. 280:7956-7961
The interaction of thrombin with protein C triggers a key down-regulatory process of the coagulation cascade. Using a panel of 77 Ala mutants, we have mapped the epitope of thrombin recognizing protein C in the absence or presence of the cofactor thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a83deac83aa07bac4e50d7d351811d80
https://doi.org/10.1074/jbc.m412869200
https://doi.org/10.1074/jbc.m412869200
Autor:
Leslie A. Bush, Agustin O. Pineda, F. Scott Mathews, Sonia Caccia, Enrico Di Cera, Zhi-wei Chen, Christopher J. Carrell, Swati Prasad
Publikováno v:
Journal of Biological Chemistry. 279:31842-31853
Na(+) binding near the primary specificity pocket of thrombin promotes the procoagulant, prothrombotic, and signaling functions of the enzyme. The effect is mediated allosterically by a communication between the Na(+) site and regions involved in sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a90b08be0b3cdd98c63b17d0d2ec7ea
https://doi.org/10.1074/jbc.m401756200
https://doi.org/10.1074/jbc.m401756200
Publikováno v:
Journal of Biological Chemistry. 277:40177-40180
Using the thrombin mutant R77aA devoid of the site of autoproteolytic degradation at exosite I, we have solved for the first time the structure of thrombin free of any inhibitors and effector molecules and stabilized in the Na(+)-free slow form. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d80dfa7ec832058eb4306c43454a645
https://doi.org/10.1074/jbc.c200465200
https://doi.org/10.1074/jbc.c200465200
Autor:
W. Ross Ellington, Agustin O Pineda
Publikováno v:
Gene. 265:115-121
Two major gene duplication events are thought to have taken place in the evolution of creatine kinases (CK) in the vertebrates - (1) the formation of distinct mitochondrial (MiCK) and cytoplasmic forms from the primordial gene and (2) subsequent form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fad1ca6360b8689f0615f56babb5b64d
https://doi.org/10.1016/s0378-1119(01)00352-3
https://doi.org/10.1016/s0378-1119(01)00352-3
Autor:
W. Ross Ellington, Agustin O Pineda
Publikováno v:
European Journal of Biochemistry. 264:67-73
The cDNA and deduced amino-acid sequences for dimeric and octameric isoforms of creatine kinase (CK) from a protostome, the polychaete Chaetopterus variopedatus, were elucidated and then analysed in the context of available vertebrate CK sequences an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7adcb11eda72ad8c2919287d2bbc5795
https://doi.org/10.1046/j.1432-1327.1999.00577.x
https://doi.org/10.1046/j.1432-1327.1999.00577.x
Publikováno v:
FEBS Letters. 425:75-78
Mitochondrial creatine kinase (MiCK) occurs primarily as an octameric form localized in the mitochondrial intermembrane compartment in vertebrate tissues and echinoderm spermatozoa (both deuterostome groups). The octameric quaternary structure is tho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6088052c0a825f8b95bdf0d0a5189e9b
https://doi.org/10.1016/s0014-5793(98)00204-x
https://doi.org/10.1016/s0014-5793(98)00204-x