Zobrazeno 1 - 10 of 23 pro vyhledávání: '"I. S. SIGAL"'
2
Design and synthesis of HIV protease inhibitors. Variations of the carboxy terminus of the HIV protease inhibitor L-682,679
Autor: I S Sigal, S J deSolms, Zugay Ja, J. M. Wiggins, J. P. Vacca, Samuel L. Graham, J. P. Guare, E A Giuliani, William M. Sanders, Paul L. Darke
Publikováno v: Journal of medicinal chemistry. 34(9)
A series of tetrapeptide analogues of 1 (L-682,679), in which the carboxy terminus has been shortened and modified, was prepared and their inhibitory activity measured against the HIV protease in a peptide cleavage assay. Selected examples were teste
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc8da6dbba186808bacd8b16f0dfec43
https://pubmed.ncbi.nlm.nih.gov/1910089
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3
Separation of the structural requirements for agonist-promoted activation and sequestration of the beta-adrenergic receptor
Autor: A H, Cheung, R A, Dixon, W S, Hill, I S, Sigal, C D, Strader
Publikováno v: Molecular pharmacology. 37(6)
The deletion of residues 222-229 from the hamster beta 2-adrenergic receptor (beta AR) resulted in an inability of the mutant receptor to couple to the guanine nucleotide-binding protein (G protein) Gs and to undergo the agonist-mediated sequestratio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::03f1bdb72b81a894dbbfb3e1d8c93b24
https://pubmed.ncbi.nlm.nih.gov/2163011
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4
Purification and properties of thiol beta-lactamase. A mutant of pBR322 beta-lactamase in which the active site serine has been replaced with cysteine
Autor: S R Petteway, B J Thomas, William F. DeGrado, I S Sigal
Publikováno v: Journal of Biological Chemistry. 259:5327-5332
The specifically mutated enzyme thiol beta-lactamase has been expressed in Escherichia coli by means of the trp promoter and purified to homogeneity. The gene for this enzyme results from a single base change N410 A----T in the gene of pBR322 RTEM be
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f8c4763daca07592365fe33dc121aee4
https://doi.org/10.1016/s0021-9258(17)42994-2
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5
Solar energy storage reactions. Thermal and photochemical redox reactions of polynuclear rhodium isocyanide complexes
Autor: Harry B. Gray, I. S. Sigal, Kent R. Mann
Publikováno v: Journal of the American Chemical Society. 102:7252-7256
The binuclear Rh/sup 1/ complex Rh/sub 2/(bridge)/sub 4//sup 2 +/ (or Rh/sub 2//sup 2 +/) (bridge = 1,3-diisocyanopropane) reacts with 12 M HCl to form H/sub 2/ and (Rh/sub 2/(bridge)/sub 4/)/sub 2/Cl/sub 2//sup 4 +/ (or Rh/sub 4/Cl/sub 2//sup 4 +/).
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::543907b784327d3ba778945b2d369f6d
https://doi.org/10.1021/ja00544a014
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7
Solar energy storage reactions involving polynuclear rhodium isocyanide complexes. Flash photolysis studies in aqueous sulfuric acid solutions
Autor: Steven J. Milder, P. Ray Ryason, Harry B. Gray, George S. Hammond, I. S. Sigal, Kent R. Mann, Vincent M. Miskowski
Publikováno v: Journal of the American Chemical Society. 101:4383-4385
Results of flash photolysis studies of the complexes Rh/sub 2/(bridge)/sub 4//sup 2 +/ where bridge = 1,3 diisocyanopropane are reported. The decay of the complex was found to obey second-order kinetics, and the product of the charges of the reactant
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d9b2aab8ef134e7ac7490088166e3ec3
https://doi.org/10.1021/ja00509a061
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8
Mutations that uncouple the beta-adrenergic receptor from Gs and increase agonist affinity
Autor: C D, Strader, R A, Dixon, A H, Cheung, M R, Candelore, A D, Blake, I S, Sigal
Publikováno v: The Journal of biological chemistry. 262(34)
The deletion of residues 239-272 from the hamster beta-adrenergic receptor resulted in a loss of the ability of the receptor, expressed in mouse L cells, to stimulate adenylate cyclase (Dixon, R. A. F., Sigal, I. S., Rands, E., Register, R. B., Cande
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b0ad2c3acd1611b153b5c3617e21cf4e
https://pubmed.ncbi.nlm.nih.gov/2890637
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10
Human immunodeficiency virus protease. Bacterial expression and characterization of the purified aspartic protease
Autor: P L, Darke, C T, Leu, L J, Davis, J C, Heimbach, R E, Diehl, W S, Hill, R A, Dixon, I S, Sigal
Publikováno v: The Journal of biological chemistry. 264(4)
The protease of human immunodeficiency virus has been expressed in Escherichia coli and purified to apparent homogeneity. Immunoreactivity toward anti-protease peptide sera copurified with an activity that cleaved the structural polyprotein gag p55 a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a89329ec2e943d2b29fbcc0abbb4ee5b
https://pubmed.ncbi.nlm.nih.gov/2644259
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