Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Jo Louise Seltzer"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1293:259-266
The gelatinases (type IV collagenases) are members of the matrix metalloproteinase family that not only have a high degree of structural homology but are known to be nearly identical in their digestion profile against macromolecular substrates. We ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58e6d07d3681f548d99efe6cb8cda0a9
https://doi.org/10.1016/0167-4838(95)00259-6
https://doi.org/10.1016/0167-4838(95)00259-6
Autor:
D. W. Mccourt, H Weingarten, Kathryn Akers, Jo Louise Seltzer, Arthur Z. Eisen, Gregory A. Grant
Publikováno v:
Journal of Biological Chemistry. 265:20409-20413
Type IV collagenase (gelatinase) readily cleaves denatured collagen into very small peptides. Large cyanogen bromide fragments (25 kDa) of type I collagen are degraded at the same rate as the complete alpha-chain. A number of the gelatinolytic cleava
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b97e07fc2c7e397249b49014750e00f9
https://doi.org/10.1016/s0021-9258(17)30519-7
https://doi.org/10.1016/s0021-9258(17)30519-7
Publikováno v:
Journal of Biological Chemistry. 265:13521-13527
We have studied the degradation of type X collagen by human skin fibroblast and rat uterus interstitial collagenases and human 72-kDa type IV collagenase. The interstitial collagenases attacked the native type X helix at two loci, cleaving residues G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e719b2b6c7f0b1578a5ef2e2cc12eea
https://doi.org/10.1016/s0021-9258(18)77378-x
https://doi.org/10.1016/s0021-9258(18)77378-x
Autor:
Jo Louise Seltzer, Charles T. Lauhon, Yingsheng Zhang, Paul J. Bertics, Donald T. Witiak, Dongmei Li, Jon C. D. Houtman
Publikováno v:
Bioorganicmedicinal chemistry letters. 9(19)
A novel series of hydroxamate/urea-based inhibitors of gelatinases has been discovered via solid-phase combinatorial chemistry. SAR of P1′, P2′, and P3′ has been exploited and structures different from traditional succinate-based MMP inhibitors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04b8e6e68a17ba45b1ddb1ef665767b6
https://pubmed.ncbi.nlm.nih.gov/10522699
https://pubmed.ncbi.nlm.nih.gov/10522699
Publikováno v:
Experimental cell research. 232(2)
In monolayer culture, fibroblasts secrete all matrix metalloproteinases, including gelatinase A (72-kDa type IV collagenase), as inactive zymogens. Whereas limited proteolysis by plasmin or other matrix metalloproteinases (MMPs) can accomplish the ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a9d009ec8d12366b2ebe9f3e9277ad9
https://pubmed.ncbi.nlm.nih.gov/9168808
https://pubmed.ncbi.nlm.nih.gov/9168808
Normal fibroblasts cultured as monolayers secrete matrix metalloproteinases (MMP), including gelatinase A (72-kDa type IV collagenase) as inactive zymogens. Previously we found that normal fibroblasts cultured in a type I collagen lattice (dermal equ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec84df44e4e0c56d1b589cfc5ccdc6cc
https://europepmc.org/articles/PMC20738/
https://europepmc.org/articles/PMC20738/
Autor:
E A Southon, Kathryn Akers, B Sudbeck, Elizabeth A. Wayner, Arthur Z. Eisen, Jo Louise Seltzer, A Y Lee
Publikováno v:
Experimental cell research. 213(2)
The matrix metalloproteinase 72-kDa type IV collagenase (also known as gelatinase A) is thought to be involved in both normal connective tissue remodeling and invasive pathological processes. Like other matrix metalloproteinases, 72-kDa type IV colla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f70a258028093f8aa6604a8a8845c6cd
https://pubmed.ncbi.nlm.nih.gov/7519563
https://pubmed.ncbi.nlm.nih.gov/7519563
Autor:
Jo Louise Seltzer, Arthur Z. Eisen
Publikováno v:
Journal of Investigative Dermatology. 112:993
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0667556d343f9b1b9db687d8f24e9177
https://doi.org/10.1046/j.1523-1747.1999.00616.x
https://doi.org/10.1046/j.1523-1747.1999.00616.x
Publikováno v:
Journal of Chromatography A. 326:147-155
Human skin, maintained in serum-free organ culture, secretes a neutral metalloendopeptidase which is remarkably specific for gelatin. Because the product peptides from the action of collagenase on collagen become denatured into random coil polypeptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9b27db6f05bf9b2999b0b2e46ad621a
https://doi.org/10.1016/s0021-9673(01)87440-9
https://doi.org/10.1016/s0021-9673(01)87440-9
Publikováno v:
Archives of Biochemistry and Biophysics. 173:355-361
The removal of extrinsic Ca2+ from human skin, rat skin, and postpartum rat uterus collagenases results in a reversible loss of enzymatic activity, which becomes irreversible with increasing length of Ca2+-free incubation at physiological temperature
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::926460b17e11bbd2f6b8283ab324298b
https://doi.org/10.1016/0003-9861(76)90270-8
https://doi.org/10.1016/0003-9861(76)90270-8