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Inhibition of Human Stromelysin by Peptides Based on the N-Terminal Domain of Tissue Inhibitor of Metalloproteinases-1

Autor: A. Lugo, Robert L. Walsky, M. Visnick, N. Fotouhi, A. C. Hanglow, John W. Coffey

Publikováno v: Biochemical and Biophysical Research Communications. 205:1156-1163

The tissue inhibitors of metalloproteinases (TIMPs) represent a family of naturally occurring protein inhibitors of stromelysin and other members of the family of matrix metalloproteinases. A series of peptides based on the N-terminal sequence of nat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74fddf090ace952990c472e737903cd4
https://doi.org/10.1006/bbrc.1994.2787

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Potent peptide inhibitors of stromelysin based on the prodomain region of matrix metalloproteinases

Autor: John W. Coffey, L. Lusch, M. Visnick, A. C. Hanglow, N. Fotouhi, A. Lugo, Robert L. Walsky

Publikováno v: Journal of Biological Chemistry. 269:30227-30231

Stromelysin is secreted as an inactive zymogen that is activated in the extracellular space by cleavage of the His81-Phe82 bond with the release of the 81-amino acid propeptide domain. This segment contains a 12-amino acid sequence (MRKPRC75GVPDVG) t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::76e2b6548aecb2b607c41606e2d28305
https://doi.org/10.1016/s0021-9258(18)43801-x

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Interaction of phosphorylated FcepsilonRIgamma immunoglobulin receptor tyrosine activation motif-based peptides with dual and single SH2 domains of p72syk. Assessment of binding parameters and real time binding kinetics

Autor: T, Chen, B, Repetto, R, Chizzonite, C, Pullar, C, Burghardt, E, Dharm, Z, Zhao, R, Carroll, P, Nunes, M, Basu, W, Danho, M, Visnick, J, Kochan, D, Waugh, A M, Gilfillan

Publikováno v: The Journal of biological chemistry. 271(41)

To examine the characteristics of the interaction of the FcepsilonRIgamma ITAM with the SH2 domains of p72(syk), the binding of an 125I-labeled dual phosphorylated FcepsilonRIgamma ITAM-based peptide to the p72(syk) SH2 domains was monitored utilizin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4d4354b7ebfa0869789a0e5d4270afe2
https://pubmed.ncbi.nlm.nih.gov/8810294

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Potent peptide inhibitors of stromelysin based on the prodomain region of matrix metalloproteinases

Autor: N, Fotouhi, A, Lugo, M, Visnick, L, Lusch, R, Walsky, J W, Coffey, A C, Hanglow

Publikováno v: The Journal of biological chemistry. 269(48)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0b9a0d009cad15b5a9064f43a1756118
https://pubmed.ncbi.nlm.nih.gov/7982931

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Peptides based on the conserved predomain sequence of matrix metalloproteinases inhibit human stromelysin and collagenase

Autor: N. Fotouhi, Robert L. Walsky, A. Lugo, A. C. Hanglow, M. B. Finch-Arietta, L. Lusch, M. Visnick

Publikováno v: Agents and actions.

Prostromelysin, a member of the family of matrix metalloproteinases, is secreted as a zymogen which is activated after cleavage of the His81-Phe82 bond. The 82 amino acid propeptide that is removed during activation contains 12 amino acids, MRKPRC75G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::393c5a84654aef3175cd8a6b2204ef9e
https://pubmed.ncbi.nlm.nih.gov/8273554

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