Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Ronald T. Aimes"'
Publikováno v:
Thrombosis and Haemostasis. 89:382-392
SummaryMammalian urokinase-type plasminogen activator (uPA) is produced as a stable single polypeptide chain zymogen and requires a distinct proteolytic cleavage to become an active, two-chain enzyme. In contrast, chicken uPA, both native and recombi
Autor:
Boris Ionin, Ronald T. Aimes, Edward Bernton, Gabriel T. Meister, George Atiee, Robert J. Hopkins, Mario H. Skiadopoulos, Eric M. Vela, Nina V. Malkevich, Gary S. Nabors, Virginia Johnson
Publikováno v:
Antimicrobial agents and chemotherapy. 58(7)
Anthrax is an acute infectious disease caused by the spore-forming bacterium Bacillus anthracis . Timely administration of antibiotics approved for the treatment of anthrax disease may prevent associated morbidity and mortality. However, any delay in
Publikováno v:
Journal of Biological Chemistry. 275:40827-40838
We have isolated a novel 75-kDa gelatinase from a chicken macrophage cell line, HD11. Biochemical and immunological characterization of the purified enzyme demonstrated that it is distinct from the chicken 72-kDa gelatinase A (MMP-2). The enzyme is c
Autor:
James P. Quigley, Elizabeth Hahn-Dantona, Brian K. Weaver, Ling-Hui Li, Susan P. Hawkes, Ronald T. Aimes
Publikováno v:
Journal of Cellular Physiology. 174:342-352
Rous sarcoma virus-transformed chicken embryo fibroblasts (RSVCEF), when compared to normal CEF, produce elevated levels of matrix metalloproteinase-2 (MMP-2) that exists in a form free of complexed tissue inhibitor of metalloproteinase-2 (TIMP-2). I
Autor:
Nina V. Malkevich, Mario H. Skiadopoulos, Gary S. Nabors, Boris Ionin, Kristin H. Clement, Ronald T. Aimes, Ajoy C. Chakrabarti, Subhendu Basu, Thomas L. Rudge
Development of anthrax countermeasures that may be used concomitantly in a postexposure setting requires an understanding of the interaction between these products. Anthrax immune globulin intravenous (AIGIV) is a candidate immunotherapeutic that con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e930ed6d734f18426fe6306aa3d9fe4c
https://europepmc.org/articles/PMC3811249/
https://europepmc.org/articles/PMC3811249/
Autor:
Snehasikta Swarnakar, Sandra Misquith, Elizabeth A. Hahn, James P. Quigley, Peter B. Armstrong, S. Srimal, Ronald T. Aimes
Publikováno v:
Journal of Biological Chemistry. 271:14717-14721
A variety of invertebrates possess plasma lectins with sialic acid recognition capabilities. One of the best studied of these lectins is limulin, which is a member of the pentraxin family of proteins and is found in the plasma of the American horsesh
Autor:
Tami von Schalscha, James P. Quigley, Luraynne C. Sanders, David A. Cheresh, Peter C. Brooks, Staffan Strömblad, William G. Stetler-Stevenson, Ronald T. Aimes
Publikováno v:
Cell. 85:683-693
Cellular invasion depends on cooperation between adhesive and proteolytic mechanisms. Evidence is provided that the matrix metalloproteinase MMP-2 can be localized in a proteolytically active form on the surface of invasive cells, based on its abilit
Autor:
Ronald T. Aimes, Nancy B. Seward, James P. Quigley, Steingrimur Stefansson, Daniela S. Alexander
Publikováno v:
Journal of Cellular Physiology. 161:419-428
Rous sarcoma virus-transformed cultures of chicken embryo fibroblasts (RSVCEF) secrete elevated levels of a 70 kDa progelatinase, an avian form of the 72 kDa matrix metalloproteinase-2 (MMP-2). Affinity-purified preparations of secreted 70 kDa progel
Publikováno v:
Biochemical Journal. 300:729-736
Chicken embryo fibroblasts secrete a 72 kDa progelatinase that displays all of the characteristics of a matrix metalloproteinase. Employing reverse-transcription PCR and degenerate oligonucleotide primers that are specific for two highly conserved se
Publikováno v:
Cell Differentiation and Development. 32:263-275
Cultures of transformed fibroblasts actively involved in extracellular matrix degradation have been examined for initial activation of serine and metallo protease cascade systems. Rous sarcoma virus transformed chick embryo fibroblasts (RSVCEF), in c