Výsledky vyhledávání - "R. J. Colonno"

Characterization of a Mutant HIV-1 Reverse Transcriptase Resistant to (+)-(5S)-4,5,6,7-tetrahydro-5-methyl-6-(3-methyl-2-butenyl)-imidazo[4,5,1-jk][1,4]benzodiazepin-2(1H)-thione (TIBO R82150)

Autor: C. M. Bechtold, Himadri Samanta, Pin-Fang Lin, H. Li, A. Lee, Ronald E. Rose, John J. Trimble, A K Patick, R. J. Colonno

Publikováno v: Antiviral Chemistry and Chemotherapy. 5:278-281

A virus strain resistant to R82150, a non-nucleoside reverse transcriptase (NNRT) inhibitor (tetrahydro-imidazo [4,5, 1- jk] [1,4] benzodiazepine-2(1 H)-thione), was isolated following serial passage of HIV-1 RF in CEM-SS cells. The virus is cross-re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::912693319509c7ae464d89ce9e6b6f23
https://doi.org/10.1177/095632029400500410

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Identification of the human immunodeficiency virus reverse transcriptase residues that contribute to the activity of diverse nonnucleoside inhibitors

Autor: J A Wolfgang, R J Colonno, V V Sardana, A J Schlabach, Jon H. Condra, L Gotlib, Emilio A. Emini, Donald J. Graham

Publikováno v: Antimicrobial Agents and Chemotherapy. 36:1441-1446

The reverse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1) is potently inhibited by a structurally diverse group of nonnucleoside compounds. These include pyridinone derivatives, tetrahydroimadazo[4,5,1-j,k][1,4]-benzodiazepin-2(1H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::933fb6c2943385a57af6bca69e11548b
https://doi.org/10.1128/aac.36.7.1441

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Genotypic and phenotypic analysis of human immunodeficiency virus type 1 isolates from patients on prolonged stavudine therapy

Autor: P.-F. Lin, H. Samanta, R. E. Rose, A. K. Patick, J. Trimble, C. M. Bechtold, D. R. Revie, N. C. Khan, M. E. Federici, H. Li, A. Lee, R. E. Anderson, R. J. Colonno

Publikováno v: The Journal of infectious diseases. 170(5)

Development of stavudine resistance was studied using human immunodeficiency virus type 1 isolates from 13 patients treated with stavudine for 18-22 months. Drug sensitivity testing on 11 of these pre- and posttherapy isolates identified only 2 postt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4916112d636fc8c408959d05e5fc38f8
https://pubmed.ncbi.nlm.nih.gov/7963708

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Identification of the serine residue at the active site of the herpes simplex virus type 1 protease

Autor: C L, DiIanni, J T, Stevens, M, Bolgar, D R, O'Boyle, S P, Weinheimer, R J, Colonno

Publikováno v: The Journal of biological chemistry. 269(17)

Herpes simplex virus type 1 (HSV-1) encodes a protease that is essential for proteolytic processing of itself and of the nucleocapsid-associated protein, ICP35 (infected cell protein 35) (Liu, F., and Roizman, B. (1991) J. Virol. 65, 5149-5156). Inhi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bed39a8aabbdab23edf321252050f825
https://pubmed.ncbi.nlm.nih.gov/8175677

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Identification of the herpes simplex virus-1 protease cleavage sites by direct sequence analysis of autoproteolytic cleavage products

Autor: C L, DiIanni, D A, Drier, I C, Deckman, P J, McCann, F, Liu, B, Roizman, R J, Colonno, M G, Cordingley

Publikováno v: The Journal of biological chemistry. 268(3)

Herpes simplex virus type-1 (HSV-1) encodes a protease responsible for proteolytic processing of the virus assembly protein, ICP35 (infected cell protein 35). The coding region of ICP35 is contained within the gene that encodes the protease, and ICP3

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ac177b0f2d67367da983d3a41f912d5d
https://pubmed.ncbi.nlm.nih.gov/8380586

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Substrate requirements of human rhinovirus 3C protease for peptide cleavage in vitro

Autor: M G, Cordingley, P L, Callahan, V V, Sardana, V M, Garsky, R J, Colonno

Publikováno v: The Journal of biological chemistry. 265(16)

A series of synthetic peptides representing authentic proteolytic cleavage sites of human rhinovirus type 14 were assayed as substrates for purified 3C protease. Competition cleavage assays were employed to determine the relative specificity constant

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ee6d2987a8abc30744e8d5eb56bdf600
https://pubmed.ncbi.nlm.nih.gov/2160953

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Bacterial expression of antibody fragments that block human rhinovirus infection of cultured cells

Autor: J H, Condra, V V, Sardana, J E, Tomassini, A J, Schlabach, M E, Davies, D W, Lineberger, D J, Graham, L, Gotlib, R J, Colonno

Publikováno v: The Journal of biological chemistry. 265(4)

Human rhinoviruses are the major causative agents of the common cold in humans and have been divided into major and minor groups based on receptor specificity. cDNAs encoding the light and heavy chains of a murine monoclonal antibody that recognizes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ac9e4e589c400176207116cdffa4822e
https://pubmed.ncbi.nlm.nih.gov/2153680

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