Výsledky vyhledávání - "S P, Weinheimer"

Atazanavir Signature I50L Resistance Substitution Accounts for Unique Phenotype of Increased Susceptibility to Other Protease Inhibitors in a Variety of Human Immunodeficiency Virus Type 1 Genetic Backbones

Autor: Richard J. Colonno, Jacques Friborg, Hyekyung Yang, S P Weinheimer, Linda Discotto

Publikováno v: Antimicrobial Agents and Chemotherapy. 49:3816-3824

Substitution of leucine for isoleucine at residue 50 (I50L) of human immunodeficiency virus (HIV) protease is the signature substitution for atazanavir (ATV) resistance. A unique phenotypic profile has been associated with viruses containing the I50L

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52bff98dad94f133d0d2ffc145a65828
https://doi.org/10.1128/aac.49.9.3816-3824.2005

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Clinical Emergence of Entecavir-Resistant Hepatitis B Virus Requires Additional Substitutions in Virus Already Resistant to Lamivudine

Autor: Peter W Angus, Ann W. Walsh, Daniel J. Tenney, Steven Levine, Geoff Thompson, Ronald E. Rose, William Sievert, Angeline Bartholomeusz, Nadia Warner, Linda Discotto, S P Weinheimer, Cheng-Fang Yu, Kevin A. Pokornowski, Mary Jane Plym, Richard J. Colonno, Stephen Locarnini, A Ayres

Publikováno v: Antimicrobial Agents and Chemotherapy. 48:3498-3507

Entecavir (ETV) exhibits potent antiviral activity in patients chronically infected with wild-type or lamivudine (3TC)-resistant (3TC r ) hepatitis B virus (HBV). Among the patients treated in phase II ETV clinical trials, two patients for whom previ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5ac69abdcb808cb5500003789cc76ca
https://doi.org/10.1128/aac.48.9.3498-3507.2004

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Efficacies of Entecavir against Lamivudine-Resistant Hepatitis B Virus Replication and Recombinant Polymerases In Vitro

Autor: Ronald E. Rose, Steven Levine, Gregory Yamanaka, Sharon Zhang, Dennis Hernandez, S P Weinheimer, Richard J. Colonno

Publikováno v: Antimicrobial Agents and Chemotherapy. 46:2525-2532

Entecavir (ETV) is a potent and selective inhibitor of hepatitis B virus (HBV) replication in vitro and in vivo that is currently in clinical trials for the treatment of chronic HBV infections. A major limitation of the current HBV antiviral therapy,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d19db7f4448c8f9b88b9025981dacdc
https://doi.org/10.1128/aac.46.8.2525-2532.2002

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The C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsids

Autor: W. Hurlburt, P J McCann, Min Gao, L. Matusick-Kumar, S P Weinheimer, W. W. Newcomb, Jay C. Brown

Publikováno v: Journal of Virology. 69:4347-4356

The herpes simplex virus type 1 protease and its substrate, ICP35, are involved in the assembly of viral capsids. Both proteins are encoded by a single open reading frame from overlapping mRNAs. The protease is autoproteolytically processed at two si

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c6972fac2b109e246ef48ae9f929249
https://doi.org/10.1128/jvi.69.7.4347-4356.1995

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The Effect of Internal Autocleavage on Kinetic Properties of the Human Cytomegalovirus Protease Catalytic Domain

Autor: Karen Wager-Smith, S P Weinheimer, J T Stevens, Donald R. O'Boyle

Publikováno v: Journal of Biological Chemistry. 270:4753-4758

The 28-kilodalton (kDa) catalytic domain of the human cytomegalovirus (HCMV) protease undergoes autoproteolytic cleavage at an internal site (I site), yielding amino-terminal 15-kDa (N15) and carboxyl-terminal 13-kDa (C13) fragments. I site autocleav

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feb07a003c571c6400b89c0cea9cd831
https://doi.org/10.1074/jbc.270.9.4753

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

Autor: Mark S. Bolgar, Richard J. Colonno, S P Weinheimer, D.R. O'Boyle nd, J T Stevens, C.L. DiIanni

Publikováno v: Journal of Biological Chemistry. 269:12672-12676

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=doi_________::a06492f6461d34d28c36944627904530
https://doi.org/10.1016/s0021-9258(18)99928-x

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In vitro activity of the herpes simplex virus type 1 protease with peptide substrates

Autor: Stephen M. Festin, Sesha Natarajan, Claudio Mapelli, S P Weinheimer, C.L. DiIanni, Jonglin Tsao, Douglas James Riexinger, Gregory Yamanaka, D A Drier, Mark S. Bolgar

Publikováno v: Journal of Biological Chemistry. 268:25449-25454

Herpes simplex virus type-1 (HSV-1) protease is responsible for proteolytic processing of itself and the virus assembly protein ICP35 (infected cell protein 35). Two proteolytic processing sites within the protease have recently been identified betwe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3885d69a725a660d62ba930758fbd297
https://doi.org/10.1016/s0021-9258(19)74412-3

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Autoproteolysis of herpes simplex virus type 1 protease releases an active catalytic domain found in intermediate capsid particles

Autor: P J McCann, Gregory Yamanaka, S P Weinheimer, Donald R. O'Boyle, M G Cordingley, C.L. DiIanni, Ingrid C. Deckman, B A Boyd, J T Stevens, D A Drier

Publikováno v: Journal of Virology. 67:5813-5822

The UL26 gene of herpes simplex virus type 1 (HSV-1) encodes a 635-amino-acid protease that cleaves itself and the HSV-1 assembly protein ICP35cd (F. Liu and B. Roizman, J. Virol. 65:5149-5156, 1991). We previously examined the HSV protease by using

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6ac2eed8b46b79f827f324b2b5743a4
https://doi.org/10.1128/jvi.67.10.5813-5822.1993

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Deletion of the VP16 open reading frame of herpes simplex virus type 1

Autor: S K Durham, J L Resnick, S P Weinheimer, Donald R. O'Boyle, B A Boyd

Publikováno v: Journal of Virology. 66:258-269

VP16 (also called Vmw65 and alpha TIF) is a structural protein of herpes simplex virus type 1 (HSV-1) that trans-induces HSV-1 immediate-early gene transcription. This report describes an HSV-1 VP16 deletion mutant that was constructed and propagated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9626af5f0fbcffb6d82f975cd3606bed
https://doi.org/10.1128/jvi.66.1.258-269.1992

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Identification of a novel peptide substrate of HSV-1 protease using substrate phage display

Autor: S P Weinheimer, P J McCann, Donald R. O'Boyle, Kevin A. Pokornowski

Publikováno v: Virology. 236(2)

The method of substrate phage display was used to select a preferred substrate from three monovalent display libraries using the HSV-1 protease. The display libraries consisted of four random amino acids, six random amino acids, and a biased library

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::351521d268f689743442788a75125867
https://pubmed.ncbi.nlm.nih.gov/9325241

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