Zobrazeno 1 - 7
of 7
pro vyhledávání: '"L A, Ouellette"'
Autor:
R A Henriksen, W R Church, Lilley Leong, K L Hayes, L A Ouellette, Beth A. Bouchard, Paula B. Tracy
Publikováno v:
Journal of Biological Chemistry. 269:28606-28612
Prior studies using the mutant thrombin, thrombin Quick I, indicate that this protease induces maximum platelet aggregation and intraplatelet [Ca2+] fluxes at agonist concentrations where dissociable, equilibrium platelet binding is undetectable and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1e69c6d186cc3e8dd5200c941465a47
https://doi.org/10.1016/s0021-9258(19)61948-4
https://doi.org/10.1016/s0021-9258(19)61948-4
Publikováno v:
Molecular and Cellular Biology. 11:3537-3544
The Saccharomyces cerevisiae CDC42 gene product, a member of the ras superfamily of low-molecular-weight GTP-binding proteins, is involved in the control of cell polarity. We have analyzed the effects of three CDC42 mutations (Gly to Val-12, Gln to L
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cf47a8020e2f7ae8a9e52e503958f44
https://doi.org/10.1128/mcb.11.7.3537-3544.1991
https://doi.org/10.1128/mcb.11.7.3537-3544.1991
Publikováno v:
Journal of Biological Chemistry. 266:8384-8391
Prothrombin contains two kringle domains that are removed during activation to the blood clotting enzyme alpha-thrombin. By analogy with other kringle-containing proteins the prothrombin kringles may play a role in the protein-protein interactions ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d91d194ac187731dc2d4d1cb101bcf5f
https://doi.org/10.1016/s0021-9258(18)92987-x
https://doi.org/10.1016/s0021-9258(18)92987-x
Publikováno v:
Spinal cord. 46(9)
Clonal typing of neurogenic clones. To determine whether neurogenic clones carried over weeks in the urine of asymptomatic children with neurogenic bladder were similar to known uropathogenic clones associated with disease. Michigan State University;
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d94d5d02843d1a62e2e7fcd76f0a23ec
https://pubmed.ncbi.nlm.nih.gov/18560376
https://pubmed.ncbi.nlm.nih.gov/18560376
Publikováno v:
Methods in enzymology. 222
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::17b90117050b37f0e7b91618d016347f
https://pubmed.ncbi.nlm.nih.gov/8412807
https://pubmed.ncbi.nlm.nih.gov/8412807
Publikováno v:
Blood coagulationfibrinolysis : an international journal in haemostasis and thrombosis. 3(5)
Factor X, a vitamin K-dependent protein, is the plasma zymogen for the active serine protease factor Xa. Factor Xa is the proteolytic enzyme for prothrombinase, the multi-protein membrane complex that catalyses the cleavage of prothrombin to thrombin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::649cad2a8dc97dab678546f119a9a9d9
https://pubmed.ncbi.nlm.nih.gov/1450323
https://pubmed.ncbi.nlm.nih.gov/1450323
Publikováno v:
The Journal of biological chemistry. 266(13)
Prothrombin contains two kringle domains that are removed during activation to the blood clotting enzyme alpha-thrombin. By analogy with other kringle-containing proteins the prothrombin kringles may play a role in the protein-protein interactions ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d7fedece6a3482b54c0749f83a6de067
https://pubmed.ncbi.nlm.nih.gov/2022654
https://pubmed.ncbi.nlm.nih.gov/2022654