Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Yingzhang Lin"'
Autor:
Irma Isordia-Salas, Fengling Li, Satya P. Kunapuli, Robert W. Colman, Robin A. Pixley, R. Balfour Sartor, Hemant K. Parekh, Yingzhang Lin, Anthony Stadnicki
Publikováno v:
Blood. 102:2835-2842
Crohn disease is immunologically mediated and characterized by intestinal and systemic chronic inflammation. In a rat model, injection of peptidoglycan-polysaccharide complexes into the intestinal wall induced chronic inflammation in Lewis but neithe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b133c1867024854216ffee402003c7ed
https://doi.org/10.1182/blood-2003-02-0661
https://doi.org/10.1182/blood-2003-02-0661
Publikováno v:
Biochemistry. 39:5104-5110
Previous investigations have shown that HK and its light chain bind heparin, preventing the enhancement of antithrombin inhibition of thrombin and potentiating the inhibition of plasma kallikrein by antithrombin. We found that both HK and HKa bound h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b688717da88106730e2e4a6f6cda7b72
https://doi.org/10.1021/bi992048z
https://doi.org/10.1021/bi992048z
Publikováno v:
Blood. 95:543-550
We have demonstrated that high molecular weight kininogen (HK) binds specifically on endothelial cells to domain 2/3 of the urokinase receptor (uPAR). Inhibition by vitronectin suggests that kallikrein-cleaved HK (HKa) is antiadhesive. Plasma kallikr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b361124a46874e472c9e9052e43be98
https://doi.org/10.1182/blood.v95.2.543
https://doi.org/10.1182/blood.v95.2.543
Autor:
Robert W. Colman, Stuart L. Cooper, Abraham Majluf-Cruz, Mohammad M. Khan, Raul A. DeLa Cadena, Satya P. Kunapuli, Yingzhang Lin
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 275:H145-H150
The binding of high-molecular-weight kininogen (HK) to neutrophils (polymorphonuclear leukocytes, PMN) is required for the stimulation of aggregation and degranulation by human plasma kallikrein as well as the displacement of fibrinogen from this cel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0d209eb2ea9052d9a788ded12996935
https://doi.org/10.1152/ajpheart.1998.275.1.h145
https://doi.org/10.1152/ajpheart.1998.275.1.h145
Publikováno v:
Blood. 90:690-697
A sequence of 31 amino acids (S565-K595) in domain 6 of the light chain of high molecular weight kininogen (HK) has previously been shown to be responsible for the binding of plasma prekallikrein (PK) or kallikrein. To find effective peptides that mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d45e17c87f70db208a69d8c32ce9ee0e
https://doi.org/10.1182/blood.v90.2.690
https://doi.org/10.1182/blood.v90.2.690
Publikováno v:
Blood. 90:690-697
A sequence of 31 amino acids (S565-K595) in domain 6 of the light chain of high molecular weight kininogen (HK) has previously been shown to be responsible for the binding of plasma prekallikrein (PK) or kallikrein. To find effective peptides that mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e55c3774ef2e79534a7d6d86f4f44f5b
https://doi.org/10.1182/blood.v90.2.690.690_690_697
https://doi.org/10.1182/blood.v90.2.690.690_690_697
Autor:
Wuyi Yan, Keith R. McCrae, Yingzhang Lin, Robert B. Harris, Robert W. Colman, Shilpa S. Shenoy
Publikováno v:
Immunopharmacology. 36:193-200
HK31 (S565–K595) has previously been shown to encompass the binding domain for plasma prekallikrein (PK) within domain 6 of high molecular weight kininogen (HK). The complementary binding domain for HK within PK is mapped to PK56 (F56–G86), in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb96433e2cf08cd3784e2c0d237433b3
https://doi.org/10.1016/s0162-3109(97)00021-0
https://doi.org/10.1016/s0162-3109(97)00021-0
Publikováno v:
Biochemistry. 35:12945-12949
HK31 (S565-K595) has previously been shown to encompass the binding domain for plasma prekallikrein (PK) within domain 6 of high molecular weight kininogen (HK). The complementary binding domain for HK within PK is mapped to PK56 (F56-G86), in the ap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb622485b838cdf0ccdef314fac2dc68
https://doi.org/10.1021/bi960547j
https://doi.org/10.1021/bi960547j
Autor:
Yingzhang Lin, Ben M. Dunn, Raterman D, S. I. Foundling, Suvit Thaisrivongs, Lin Hong, Leelamanit W, Shah M, Lin X, Robert L. Heinrikson
Publikováno v:
Biochemistry. 34:1143-1152
Mutations of human immunodeficiency virus type 1 (HIV-1) protease at four positions, Val82, Asp30, Gly48, and Lys45 were analyzed for the resulting effects on kinetics and inhibition. In these mutants, Val82 was substituted separately by Asn, Glu, Al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4a7e7e6f487a630d588cc27279820cc
https://doi.org/10.1021/bi00004a007
https://doi.org/10.1021/bi00004a007
Publikováno v:
Journal of thrombosis and haemostasis : JTH. 1(8)
Summary. We previously localized the heparin binding region on high molecular weight kininogen to domain 5 (D5) by quantifying the binding using surface plasmon resonance of D5 fused at its N-terminal to glutathione-S-transferase. We further examined
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9d2c9ffd694ab42ee6b3c2db6d99e46
https://pubmed.ncbi.nlm.nih.gov/12911595
https://pubmed.ncbi.nlm.nih.gov/12911595