Zobrazeno 1 - 6 of 6 pro vyhledávání: '"C S Devine"'
1
Involvement of cysteine residues in catalysis and inhibition of human aldose reductase. Site-directed mutagenesis of Cys-80, -298, and -303
Autor: Satish K. Srivastava, C S Devine, Theresa M. Harter, P O Olins, A. Bhatnagar, Shaopeng Liu, J M Petrash
Publikováno v: Journal of Biological Chemistry. 267:24833-24840
In order to study the potential role of cysteinyl residues in catalysis and inhibition of human aldose reductase, mutants containing cysteine to serine substitution at positions 80 (ALR2:C80S), 298 (ALR2:C298S), and 303 (ALR2:C303S) were constructed.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::716105727c228c2f13d8a8ce17e8c5f6
https://doi.org/10.1016/s0021-9258(18)35839-3
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2
A peptide isolated by phage display binds to ICAM-1 and inhibits binding to LFA-1
Autor: J K, Welply, C N, Steininger, M, Caparon, M L, Michener, S C, Howard, L E, Pegg, D M, Meyer, P A, De Ciechi, C S, Devine, G F, Casperson
Publikováno v: Proteins. 26(3)
A mixed phage library containing random peptides from four to eight residues in length flanked by cysteine residues was screened using a recombinant soluble, form of human ICAM-1, which included residues 1-453, (ICAM-1(1-453)). Phage bound to immobil
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6665a60dbb632861636c1fca0852ddff
https://pubmed.ncbi.nlm.nih.gov/8953648
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3
Utilization of multiple phage display libraries for the identification of dissimilar peptide motifs that bind to a B7-1 monoclonal antibody
Autor: C. S. Devine, P. A. De Ciechi, M. H. Caparon, P. O. Olins, S. C. Howard, Stephen C. Lee
Publikováno v: Molecular diversity. 1(2)
Seven random peptide libraries (two displaying linear peptides and five displaying cysteine-constrained peptides) were constructed as gene III fusion proteins of the bacteriophage fd-tet. These libraries were used to screen a blocking monoclonal anti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f04be4796312a547235af8c7d193f95
https://pubmed.ncbi.nlm.nih.gov/9237196
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4
Involvement of cysteine residues in catalysis and inhibition of human aldose reductase. Site-directed mutagenesis of Cys-80, -298, and -303
Autor: J M, Petrash, T M, Harter, C S, Devine, P O, Olins, A, Bhatnagar, S, Liu, S K, Srivastava
Publikováno v: The Journal of biological chemistry. 267(34)
In order to study the potential role of cysteinyl residues in catalysis and inhibition of human aldose reductase, mutants containing cysteine to serine substitution at positions 80 (ALR2:C80S), 298 (ALR2:C298S), and 303 (ALR2:C303S) were constructed.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b7995c3605ddca0e84dccfce971bc47e
https://pubmed.ncbi.nlm.nih.gov/1332968
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5
Heparin interferes with the biological effectiveness of atriopeptin
Autor: S W Holmberg, C S Devine, Y F Wei, Philip Needleman, K M Leahy, P O Olins
Publikováno v: Hypertension. 9:607-610
The chromatographic mobility of atriopeptin-28 or of the prohormone is markedly altered by preincubation of the peptides with heparin before separation on reverse-phase high performance liquid chromatography. Protamine prevented the heparin effect an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e50966e19b28d8bed0254e1f28e87530
https://doi.org/10.1161/01.hyp.9.6.607
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