Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Enriqueta R. Guinto"'
Publikováno v:
Proceedings of the National Academy of Sciences. 96:1852-1857
Residue 225 in serine proteases of the chymotrypsin family is Pro or Tyr in more than 95% of nearly 300 available sequences. Proteases with Y225 (like some blood coagulation and complement factors) are almost exclusively found in vertebrates, whereas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f425aeedb103766f5e67560f392f605
https://doi.org/10.1073/pnas.96.5.1852
https://doi.org/10.1073/pnas.96.5.1852
Publikováno v:
Nature Biotechnology. 15:146-149
The discovery of the Na(+)-dependent allosteric regulation in serine proteases makes it possible to control catalytic activity and specificity in this class of enzymes in a way never considered before. We demonstrate that rational site-directed mutag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::228eaa906226ad44e78210912c57f03e
https://doi.org/10.1038/nbt0297-146
https://doi.org/10.1038/nbt0297-146
Autor:
Enriqueta R. Guinto, Enrico Di Cera
Publikováno v:
Biophysical Chemistry. 64:103-109
Mutation of residue W60d of thrombin, located 17 A away from the Na + binding site, suppresses Na + binding and the functional differences between the slow and fast forms. The molecular basis for the long-range effect of this mutation is provided by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09ec3e26cae98ebb7de60523eaa8417a
https://doi.org/10.1016/s0301-4622(96)02211-9
https://doi.org/10.1016/s0301-4622(96)02211-9
Autor:
E. Di Cera, Enriqueta R. Guinto
Publikováno v:
Biochemistry. 35:8800-8804
Current views about protein-ligand interactions state that electrostatic forces drive the binding of charged species and that burial of hydrophobic and polar surfaces controls the heat capacity change associated with the reaction. For the interaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcc8a844aa5579e8447f23d40ea63d48
https://doi.org/10.1021/bi9608828
https://doi.org/10.1021/bi9608828
Autor:
Alexander Tulinsky, Enriqueta R. Guinto, Meng Wuyi, Alessandro Vindigni, Quoc D. Dang, Enrico Di Cera, Youhna M. Ayala
Publikováno v:
Journal of Biological Chemistry. 270:22089-22092
Thrombin is an allosteric serine protease existing in two forms, slow and fast, targeted toward anticoagulant and procoagulant activities. The slow --fast transition is induced by Na+ binding to a site contained within a cylindrical cavity formed by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b50848d478ac9fbaade76cd4c088b397
https://doi.org/10.1074/jbc.270.38.22089
https://doi.org/10.1074/jbc.270.38.22089
Autor:
Savvas N. Savvides, Enriqueta R. Guinto, Erli Zhang, Enrico Di Cera, Alexander Tulinsky, Agustin O. Pineda
Publikováno v:
Biophysical chemistry. 112(2-3)
The thrombin mutant D221A/D222K (ARK) does not bind Na+ and has interesting functional properties intermediate between those of the slow and fast forms of wild type. We solved the X-ray crystal structure of ARK bound at exosite I with a fragment of h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4345ec3d62795a3d95829521e3732c2d
https://pubmed.ncbi.nlm.nih.gov/15572256
https://pubmed.ncbi.nlm.nih.gov/15572256
Publikováno v:
Annals of the New York Academy of Sciences. 485:73-79
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6ebc5ce21130e7fc5c01b5fb326a209
https://doi.org/10.1111/j.1749-6632.1986.tb34569.x
https://doi.org/10.1111/j.1749-6632.1986.tb34569.x
Autor:
Deborah E. Cool, Bernard A. Van Oost, Marion R. Fung, Enriqueta R. Guinto, Marlys L. Koschinsky, Ross T. A. MacGillivray
Publikováno v:
Genetic Engineering ISBN: 9781461570837
During the past 25 years, studies in many different laboratories throughout the world have led to our present understanding of the mechanisms of blood clotting. This process involves the complex interaction of platelets, endothelial cells lining the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bcf898a6d71300ada181741f574b4cea
https://doi.org/10.1007/978-1-4615-7081-3_14
https://doi.org/10.1007/978-1-4615-7081-3_14
