Zobrazeno 1 - 10 of 16 pro vyhledávání: '"Anne R. Kaplan"'
1
Akademický článek
NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
Autor: Anne R. Kaplan, Katherine Kaus, Swastik De, Rich Olson, Andrei T. Alexandrescu
Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Abstract In addition to multiple virulence factors, Bacillus cereus a pathogen that causes food poisoning and life-threatening wound infections, secretes the pore-forming toxin hemolysin II (HlyII). The HlyII toxin has a unique 94 amino acid C-termin
Externí odkaz: https://doaj.org/article/0ba821a0456742d090fc2ca6e2423836
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2
Protein yoga: Conformational versatility of the Hemolysin II C-terminal domain detailed by NMR structures for multiple states
Autor: Andrei T. Alexandrescu, Anne R. Kaplan, Rich Olson
Publikováno v: Protein Sci
The C-terminal domain of Bacillus cereus hemolysin II (HlyIIC), stabilizes the trans-membrane-pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by cis/trans i
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::096e69f4dd722b3570da607fc3290e52
https://pubmed.ncbi.nlm.nih.gov/33733504
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3
Akademický článek
p53 Dimers associate with a head-to-tail response element to repress cyclin B transcription.
Autor: Robert Lipski, Daniel J Lippincott, Brittany C Durden, Anne R Kaplan, Hilary E Keiser, Jung-Ho Park, Aime A Levesque
Publikováno v: PLoS ONE, Vol 7, Iss 8, p e42615 (2012)
DNA damage induced by the topoisomerase I inhibitor SN38 activates cell cycle checkpoints which promote cell cycle arrest. This arrest can be abrogated in p53-defective cells by the Chk1 inhibitor 7-hydroxystaurosporine (UCN-01). Previously, we compa
Externí odkaz: https://doaj.org/article/9bb815b69d5f4ab8b85027c93c2a69c0
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4
NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
Autor: Rich Olson, Anne R. Kaplan, Swastik De, Katherine Kaus, Andrei T. Alexandrescu
Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Scientific Reports
In addition to multiple virulence factors, Bacillus cereus a pathogen that causes food poisoning and life-threatening wound infections, secretes the pore-forming toxin hemolysin II (HlyII). The HlyII toxin has a unique 94 amino acid C-terminal domain
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9632460f82ae8926227eeadaf70e47c5
https://doaj.org/article/0ba821a0456742d090fc2ca6e2423836
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5
Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages
Autor: Anne R. Kaplan, Carolyn M. Teschke, Andrei T. Alexandrescu, Therese N Tripler
Publikováno v: Journal of Virology. 93
Despite very low sequence homology, the major capsid proteins of double-stranded DNA (dsDNA) bacteriophages, some archaeal viruses, and the herpesviruses share a structural motif, the HK97 fold. Bacteriophage P22, a paradigm for this class of viruses
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ede100c131f45a5e6115b2b28c011a3e
https://doi.org/10.1128/jvi.00007-19
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7
Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix
Autor: Mark W. Maciejewski, Andrei T. Alexandrescu, Richard A. Kammerer, Megan R Brady, Anne R. Kaplan
Publikováno v: Biochemistry. 56(11)
To understand the roles ion pairs play in stabilizing coiled coils, we determined nuclear magnetic resonance structures of GCN4p at three pH values. At pH 6.6, all acidic residues are fully charged; at pH 4.4, they are half-charged, and at pH 1.5, th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e2ba63ddfc80d7991ca90997dd3d392
https://pubmed.ncbi.nlm.nih.gov/28230348
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10
NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain
Autor: Rich Olson, Andrei T. Alexandrescu, Anne R. Kaplan, Mark W. Maciejewski
Publikováno v: Biomolecular NMR assignments. 8(2)
Pathogenic bacteria secrete pore-forming toxins (PFTs) to selectively defend against immune cells and to break through cellular barriers in the host. Understanding how PFTs attack cell membranes is not only essential for therapeutic intervention but
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4900492f48d9f67270776dfc8494c219
https://pubmed.ncbi.nlm.nih.gov/24234348
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