Výsledky vyhledávání - "Robert F. Weaver"

The p26 gene of the Autographa californica nucleopolyhedrovirus: Timing of transcription, and cellular localization and dimerization of product

Autor: Robert F. Weaver, Shreevrat Goenka

Publikováno v: Virus Research. 131:136-144

p26, an early AcMNPV gene, codes for a 240-amino acid polypeptide of unknown function. Primer extension analysis showed that the p26 transcripts, initiating at three clustered start sites, accumulated between 2 and 12 h post-infection, after which th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b0044fa8e38596ef6242b29a51b7d44
https://doi.org/10.1016/j.virusres.2007.08.017

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Molecular Mode of Action of a Covalently Inhibiting Peptidomimetic on the Human Calpain Protease Core

Autor: Qing-Shan Li, Robert F. Weaver, Robert P. Hanzlik, Ernst Schönbrunn

Publikováno v: Biochemistry. 45:701-708

Calpain is a nearly ubiquitous Ca2+-activated proteolytic enzyme whose precise physiological function is unknown. However, aberrant Ca2+ homeostasis in the course of cellular injuries and certain diseases of the CNS appears to activate calpain, in tu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5cfea7c81435096fc6b8e85865ee6fd
https://doi.org/10.1021/bi052077b

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Overexpression of the 77-kD echinoderm microtubule-associated protein (EMAP), a WD-40 repeat protein, in baculovirus-infected Sf9 cells

Autor: Robert F. Weaver, Melissa A. F. Daggett, Kathy A. Suprenant, Qingwen Li

Publikováno v: Cell Motility and the Cytoskeleton. 41:57-67

The purpose of this study was to test whether any assembly-promoting microtubule-associated protein (MAP) would bundle microtubules and induce process formation in recombinant baculovirus-infected Sf9 cells, in particular, whether a non-neural MAP fr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::239985b02588182d3640487a7b81a74f
https://doi.org/10.1002/(sici)1097-0169(1998)41:1<57::aid-cm5>3.0.co

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Purification of Porcine Phospholamban Expressed inEscherichia coli

Autor: Qing Yao, Judy L. Bevan, Diana J. Bigelow, Robert F. Weaver

Publikováno v: Protein Expression and Purification. 8:463-468

Phospholamban (PLB) is a small hydrophobic protein that regulates contractility in the heart. This membrane protein expressed in bacterial cells is resistant to purification by conventional strategies that have been used to isolate expressed soluble

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::774f9a575439ca795d96fbd8af743a59
https://doi.org/10.1006/prep.1996.0125

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Temperature-Sensitive Mutations in the Protein Kinase-1 (pk-1) Gene of theAutographa californicaNuclear Polyhedrosis Virus That Block Very Late Gene Expression

Autor: Robert F. Weaver, Kannan Thirunavukkarasu, Xiaomin Fan

Publikováno v: Virology. 224(1):1-9

We have developed a genetic screen for temperature-sensitive mutations in the very late transcription apparatus of the Autographa californica nuclear polyhedrosis virus. This method starts with the BacPAK6 virus, which has the Escherichia coli lacZ g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::651acfb8c04a52a0ac8956d2c58fcda9

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Physical and Biological Characteristics of the Antitumor Drug Actinomycin D Analogues Derivatized at N-Methyl-l-valine Residues

Autor: Li Wen, Robert G. Carlson, Ken T. Takusagawa, Wenhua Chu, Qifang Li, Fusao Takusagawa, Robert F. Weaver

Publikováno v: Biochemistry. 35:13240-13249

The crystal structure of the DNA-actinomycin D (AMD) complex and a simple molecular modeling study indicated that AMD analogues derivatized at N-methyl-L-valine residues (fifth amino acid residue in the cyclic depsipeptide of AMD) could bind to DNA a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9919eab64398968cce1748047f6178f4
https://doi.org/10.1021/bi960828r

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Structural, Physical, and Biological Characteristics of RNA.cntdot.DNA Binding Agent N8-Actinomycin D

Autor: Miho Shinomiya, Robert F. Weaver, Robert G. Carlson, Wenhua Chu, Fusao Takusagawa

Publikováno v: Biochemistry. 34:8481-8491

The crystal structure of the self-complementary DNA octamer d(GAAGCTTC)2 complexed with N8-actinomycin D (N8AMD) has been determined at 3.0 A resolution (space group: P3(1)21; unit cell: a = 62.30, b = 62.30, c = 42.97 A; R = 0.173 for 1845 reflectio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::be13298006f741b9ff5aab7ea7ccfcd6
https://doi.org/10.1021/bi00026a032

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