Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Kerry F. Franklin"'
Publikováno v:
Cytogenetic and Genome Research. 83:104-108
Proteinase-3 (PR-3) and neutrophil elastase (NE) are polymorphonuclear leukocyte serine proteinases that degrade extracellular matrix proteins including elastin and appear to be involved in the pathogenesis of several diseases characterized by tissue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::16f18ed922665b72addea0d42538bd4a
https://doi.org/10.1159/000015144
https://doi.org/10.1159/000015144
Publikováno v:
Journal of Biological Chemistry. 271:32392-32402
Human proteinase-3 is one of three serine proteinases present in the azurophil granules of polymorphonuclear leukocytes along with elastase and cathepsin G. Proteinase-3 gene expression is confined to the promyelocytic stage of polymorphonuclear leuk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3a843635a74fdd73336366231e9cf4e
https://doi.org/10.1074/jbc.271.50.32392
https://doi.org/10.1074/jbc.271.50.32392
Autor:
John R. Hoidal, Gopna V. Rao, Anne Sturrock, Richard S. Lemons, M B Rebentisch, Kerry F. Franklin, Bruce C. Marshall
Publikováno v:
Journal of Biological Chemistry. 267:21193-21199
Proteinase-3 (PR-3) is a neutral serine proteinase present in the azurophil granules of human polymorphonuclear leukocytes. It degrades a variety of extracellular matrix proteins including elastin in vitro and causes emphysema when administered by tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18b3bf3c98dfaefe53636448403c0ccb
https://doi.org/10.1016/s0021-9258(19)36816-4
https://doi.org/10.1016/s0021-9258(19)36816-4
Publikováno v:
Biochimica et biophysica acta. 1676(1)
Leukocyte elastase (LE) degrades connective tissue, is involved in the inflammatory process and implicated in cyclic and congenital neutropenia. The human LE gene is within a serine proteinase locus on chromosome 19 pter13.3. Our observations demonst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ade4c6223f5742e8e96d077b32e49a7a
https://pubmed.ncbi.nlm.nih.gov/14732495
https://pubmed.ncbi.nlm.nih.gov/14732495
Autor:
Kathy M. Metcalf, David A. Brown, James P. Kushner, Kerry F. Franklin, James R. Garey, Lyle M. Harrison
Publikováno v:
Gastroenterology. 105(1)
Background: Sporadic porphyria cutanea tarda (S-PCT) has been considered an acquired disease because of the generation of liver-specific inhibitors of uroporphyrinogen decarboxylase (URO-D) activity. Several families have been described with S-PCT in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee34d3d5c41a4d9a4a49c197d71ab423
https://pubmed.ncbi.nlm.nih.gov/8099886
https://pubmed.ncbi.nlm.nih.gov/8099886
Autor:
Lyle M. Harrison, Kerry F. Franklin, James P. Kushner, James R. Garey, Evette S. Radisky, K M Metcalf
Publikováno v:
The Journal of clinical investigation. 86(5)
Uroporphyrinogen decarboxylase (URO-D) is a cytosolic heme-biosynthetic enzyme that converts uroporphyrinogen to coproporphyrinogen. Defects at the uroporphyrinogen decarboxylase locus cause the human genetic disease familial porphyria cutanea tarda.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfedae19cdf8326f440fb853e549d1f7
https://pubmed.ncbi.nlm.nih.gov/2243121
https://pubmed.ncbi.nlm.nih.gov/2243121