Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kenneth H. Minor"'
Autor:
Daniel A. Lawrence, Peter Schuck, Kenneth H. Minor, Christine R. Schar, Joseph D. Shore, Cynthia B. Peterson, Grant E. Blouse
Publikováno v:
Journal of Biological Chemistry. 280:28711-28720
Plasminogen activator inhibitor-1 (PAI-1) and vitronectin are cofactors involved in pathological conditions such as injury, inflammation, and cancer, during which local levels of PAI-1 are increased and the active serpin forms complexes with vitronec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c95c2360aca0e5656977286f355b451
https://doi.org/10.1074/jbc.m500478200
https://doi.org/10.1074/jbc.m500478200
Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation
Autor:
Andrea Balbo, Roy A. Mariuzza, Peter Schuck, Kenneth H. Minor, Carlos A. Velikovsky, Cynthia B. Peterson
Publikováno v:
Proceedings of the National Academy of Sciences. 102:81-86
Protein interactions can promote the reversible assembly of multiprotein complexes, which have been identified as critical elements in many regulatory processes in cells. The biophysical characterization of assembly products, their number and stoichi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae559748b6a05b091d87c61eda9eda72
https://doi.org/10.1073/pnas.0408399102
https://doi.org/10.1073/pnas.0408399102
Publikováno v:
Biochemistry. 44:565-574
Small-angle X-ray scattering (SAXS) measurements were used to characterize vitronectin, a circulatory protein found in human plasma that functions in regulating cell adhesion and migration, as well as proteolytic cascades that affect blood coagulatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a8152d0c798efc7ef0fe2aa44286ed0
https://doi.org/10.1021/bi048347s
https://doi.org/10.1021/bi048347s
Autor:
Kenneth H. Minor, Rudolfs K. Zalups
Publikováno v:
Journal of Toxicology and Environmental Health. 46:73-100
The principle aim of the present study was to provide evidence for the existence of both a luminal and a basolateral mechanism involved in the renal tubular uptake of inorganic mercury. To accomplish this aim, we examined individually and collectivel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea9632b71fd3f1b87d55e008eee651e4
https://doi.org/10.1080/15287399509532019
https://doi.org/10.1080/15287399509532019
Autor:
Kenneth H. Minor, Grant E. Blouse, Cynthia B. Peterson, Jan K. Jensen, Henrik Gårdsvoll, Michael Ploug, Christine R. Schar, Peter A. Andreasen, Daniel M. Dupont, John Y Anagli
Publikováno v:
Blouse, G E, Dupont, D M, Schar, C R, Jensen, J K, Minor, K H, Anagli, J Y, Gårdsvoll, H, Ploug, M, Peterson, C B & Andreasen, P A 2009, ' Interactions of plasminogen activator inhibitor-1 with vitronectin involve an extensive binding surface and induce mutual conformational rearrangements ', Biochemistry, vol. 48, no. 8, pp. 1723-35 . https://doi.org/10.1021/bi8017015
In order to explore early events during the association of plasminogen activator inhibitor-1 (PAI-1) with its cofactor vitronectin, we have applied a robust strategy that combines protein engineering, fluorescence spectroscopy, and rapid reaction kin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f36726a9959233bc1a17aa987da6ab3
https://pubmed.ncbi.nlm.nih.gov/19193026
https://pubmed.ncbi.nlm.nih.gov/19193026
Publikováno v:
The Journal of biological chemistry. 283(16)
Vitronectin and plasminogen activator inhibitor-1 (PAI-1) are important physiological binding partners that work in concert to regulate cellular adhesion, migration, and fibrinolysis. The high affinity binding site for PAI-1 is located within the N-t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f4cf272498727682605f0a212ebc875
https://pubmed.ncbi.nlm.nih.gov/18174166
https://pubmed.ncbi.nlm.nih.gov/18174166
Autor:
Lori G. Stinnett, R. Derike Smiley, Kenneth H. Minor, Stephanie N. Hicks, Elizabeth E. Howell
Publikováno v:
The Journal of biological chemistry. 279(45)
R67 dihydrofolate reductase (R67 DHFR) is a novel protein encoded by an R-plasmid that confers resistance to the antibiotic, trimethoprim. This homotetrameric enzyme possesses 222 symmetry, which imposes numerous constraints on the single active site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::100bf9c43d3d1f351c3cf98973f6d9b9
https://pubmed.ncbi.nlm.nih.gov/15333636
https://pubmed.ncbi.nlm.nih.gov/15333636
Autor:
Kenneth H. Minor, Cynthia B. Peterson
Publikováno v:
The Journal of biological chemistry. 277(12)
Serine proteinase inhibitors, including plasminogen activator inhibitor type 1 (PAI-1) and antithrombin, are key regulators of hemostatic processes such as thrombosis and wound healing. Much evidence suggests that PAI-1 can influence such processes,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::340cb695f3b393a0a61d2334d99c7403
https://pubmed.ncbi.nlm.nih.gov/11796716
https://pubmed.ncbi.nlm.nih.gov/11796716