Zobrazeno 1 - 10
of 10
pro vyhledávání: '"J S, Munger"'
Publikováno v:
Procoagulant Activity in Health and Disease ISBN: 9780429279850
Procoagulant Activity in Health and Disease
Procoagulant Activity in Health and Disease
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::45999386251b61dfecb9afd48b1eee9b
https://doi.org/10.1201/9780429279850-10
https://doi.org/10.1201/9780429279850-10
Autor:
K. E. Foster, A. C. Webb, Joan H.M. Knoll, Cynthia A. Lemere, J. S. Munger, Guo-Ping Shi, Harold A. Chapman
Publikováno v:
Journal of Biological Chemistry. 269:11530-11536
The human lysosomal cysteine proteinases, cathepsins H, L, and B, have been mapped to chromosomes 15, 9, and 8, respectively, and the genomic structures of cathepsins L and B have been determined. We report here the chromosomal localization and parti
Publikováno v:
Journal of Biological Chemistry. 267:7258-7262
Human alveolar macrophages (HAM) express an elastase activity of acidic pH optimum inhibitable by cysteine protease inhibitors. Recent studies indicate that the only known eukaryotic elastinolytic cysteine protease, cathepsin L, cannot completely acc
Publikováno v:
Journal of Biological Chemistry. 266:18832-18838
We identified a 60-kDa diisopropylfluorophosphate-(DFP) reactive protein in human bronchoalveolar lavage fluid, at a yield of 50-100 pmol/lavage. The protein is associated with the cell-free lavage fluid sediment, which consists mainly of surfactant.
Autor:
J S, Munger, X, Huang, H, Kawakatsu, M J, Griffiths, S L, Dalton, J, Wu, J F, Pittet, N, Kaminski, C, Garat, M A, Matthay, D B, Rifkin, D, Sheppard
Publikováno v:
Cell. 96(3)
Transforming growth factor beta (TGF beta) family members are secreted in inactive complexes with a latency-associated peptide (LAP), a protein derived from the N-terminal region of the TGF beta gene product. Extracellular activation of these complex
Autor:
Dennis J. Selkoe, J. S. Munger, Cynthia A. Lemere, W. S. F. Wong, David B. Teplow, Christian Haass, Guo-Ping Shi, Harold A. Chapman
To investigate the potential contribution of the lysosomal compartment in the processing of amyloid precursor protein (APP) to amyloid beta-peptides (A beta s), we stably overexpressed a series of lysosomal proteases (the cysteine proteases, cathepsi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d552453f13954e4ebd6e3b30eb6e975
https://europepmc.org/articles/PMC1136152/
https://europepmc.org/articles/PMC1136152/
Publikováno v:
American journal of respiratory and critical care medicine. 150(6 Pt 2)
Human lung macrophages express all four of the known lysosomal thiol proteases: cathepsins B, H, L, and S. These enzymes share a similar size and targeting mechanism for lysosomal accumulation and all have relatively indiscriminate substrate specific
Publikováno v:
The Journal of biological chemistry. 269(15)
The human lysosomal cysteine proteinases, cathepsins H, L, and B, have been mapped to chromosomes 15, 9, and 8, respectively, and the genomic structures of cathepsins L and B have been determined. We report here the chromosomal localization and parti
Publikováno v:
The Journal of biological chemistry. 267(11)
Human alveolar macrophages (HAM) express an elastase activity of acidic pH optimum inhibitable by cysteine protease inhibitors. Recent studies indicate that the only known eukaryotic elastinolytic cysteine protease, cathepsin L, cannot completely acc
Publikováno v:
The Journal of biological chemistry. 266(28)
We identified a 60-kDa diisopropylfluorophosphate-(DFP) reactive protein in human bronchoalveolar lavage fluid, at a yield of 50-100 pmol/lavage. The protein is associated with the cell-free lavage fluid sediment, which consists mainly of surfactant.