Zobrazeno 1 - 10 of 14 pro vyhledávání: '"Carol A, Bannow"'
1
Employing a superior BACE1 cleavage sequence to probe cellular APP processing
Autor: June M. Lull, Carol A. Bannow, Riqiang Yan, Alfredo G. Tomasselli, Thomas L. Emmons, Isam Qahwash, Michael Jerome Bienkowski, Kam F. Fok, Clark W. Smith, Joseph W. Leone, Yifeng Lu, Robert L. Heinrikson
Publikováno v: Journal of Neurochemistry. 84:1006-1017
The involvement of β-secretase (BACE1; β-site APP-cleaving enzyme) in producing the β-amyloid component of plaques found in the brains of Alzheimer's patients, has fueled a major research effort to characterize this protease. Here, we describe wor
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::918f105b854f505ed1ea7223d2f1ff7c
https://doi.org/10.1046/j.1471-4159.2003.01597.x
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2
The Differential Processing of Homodimers of Reverse Transcriptases from Human Immunodeficiency Viruses Type 1 and 2 Is a Consequence of the Distinct Specificities of the Viral Proteases
Autor: Satish K. Sharma, Kenneth B. Rank, Carol A. Bannow, Joseph W. Leone, Alfredo G. Tomasselli, Donna J. Rothrock, Robert L. Heinrikson, Clark W. Smith, Susan M. Poppe, David B. Evans, Naisheng Fan, W. Gary Tarpley
Publikováno v: Journal of Biological Chemistry. 270:13573-13579
Active, recombinant p68 reverse transcriptase (RT) from human immunodeficiency virus type 2 (HIV-2), with an NH2-terminal extension containing a hexahisti-dine sequence was isolated from extracts of Escherichia coli by immobilized metal affinity chro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3f0385378507adbac5194e72c348fbaa
https://doi.org/10.1016/s0021-9258(18)92316-1
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3
The HIV-1 Protease as Enzyme and Substrate: Mutagenesis of Autolysis Sites and Generation of a Stable Mutant with Retained Kinetic Properties
Autor: D J Rothrock, Carol A. Bannow, C S Tomich, J M Lull, A. M. Mildner, I M Reardon, J L Sarcich, Clark W. Smith, W J Howe, Joseph W. Leone
Publikováno v: Biochemistry. 33:9405-9413
Site-directed mutagenesis of autolysis sites in the human immunodeficiency virus type 1 (HIV-1) protease was applied in an analysis of enzyme specificity; the protease served, therefore, as both enzyme and substrate in this study. Inspection of natur
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1c53661bef00e283b8c61084e47454c
https://doi.org/10.1021/bi00198a005
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4
Specificity and inhibition of proteases from human immunodeficiency viruses 1 and 2
Autor: W. J. Howe, Robert L. Heinrikson, Carol A. Bannow, J. O. Hui, A G Tomasselli, D L DeCamp, I M Reardon, C S Craik, D J Staples, Tomi K. Sawyer
Publikováno v: Journal of Biological Chemistry. 265:14675-14683
Highly purified, recombinant preparations of the virally encoded proteases from human immunodeficiency viruses (HIV) 1 and 2 have been compared relative to 1) their specificities toward non-viral protein and synthetic peptide substrates, and 2) their
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cfa638659f7a59d753b524a0b8f2aa9a
https://doi.org/10.1016/s0021-9258(18)77355-9
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5
Proteases from human immunodeficiency virus and avian myeloblastosis virus show distinct specificities in hydrolysis of multidomain protein substrates
Autor: Carol A. Bannow, Tomi K. Sawyer, V K Chaudhary, J. O. Hui, A G Tomasselli, I Pastan, C M Fryling, I M Reardon, D J Staples, Desmond J. Fitzgerald
Publikováno v: Journal of Virology. 64:3157-3161
The virally encoded proteases from human immunodeficiency virus (HIV) and avian myeloblastosis virus (AMV) have been compared relative to their ability to hydrolyze a variant of the three-domain Pseudomonas exotoxin, PE66. This exotoxin derivative, m
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76d895471b489fcf099ab1128900925e
https://doi.org/10.1128/jvi.64.7.3157-3161.1990
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6
Identification of a novel mitochondrial protein ('mitoNEET') cross-linked specifically by a thiazolidinedione photoprobe
Autor: June M. Lull, Daniel J. Waldon, W. Rodney Mathews, Joseph W. Leone, William G. McDonald, Carol A. Bannow, Eric T. Lund, Jerry R. Colca
Publikováno v: American journal of physiology. Endocrinology and metabolism. 286(2)
Thiazolidinediones address underlying causes of type 2 diabetes, although their mechanism of action is not clearly understood. The compounds are thought to function as direct activators of the nuclear receptor PPARγ (peroxisome proliferator-activate
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f9c2250527805b800351aa8f695aa05
https://pubmed.ncbi.nlm.nih.gov/14570702
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7
Employing a superior BACE1 cleavage sequence to probe cellular APP processing
Autor: Alfredo G, Tomasselli, Isam, Qahwash, Thomas L, Emmons, Yifeng, Lu, Joseph W, Leone, June M, Lull, Kam F, Fok, Carol A, Bannow, Clark W, Smith, Michael J, Bienkowski, Robert L, Heinrikson, Riqiang, Yan
Publikováno v: Journal of neurochemistry. 84(5)
The involvement of beta-secretase (BACE1; beta-site APP-cleaving enzyme) in producing the beta-amyloid component of plaques found in the brains of Alzheimer's patients, has fueled a major research effort to characterize this protease. Here, we descri
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2b13dcf7e0acf3ba2cce4cd0921b08f7
https://pubmed.ncbi.nlm.nih.gov/12603825
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8
Cloning and functional expression of the first Drosophila melanogaster sulfakinin receptor DSK-R1
Autor: Roger A. Martin, Carol A Bannow, Marjorie R. Zantello, Katherine J. Burton, Martha J. Larsen, David E. Lowery, Teresa Kubiak
Publikováno v: Biochemical and biophysical research communications. 291(2)
Described in this report is a successful cloning and characterization of a functionally active Drosophila sulfakinin receptor designated DSK-R1. When expressed in mammalian cells, DSK-R1 was activated by a sulfated, Met(7--Leu(7)-substituted analog o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b92715df127db06ced92acb468b43d0
https://pubmed.ncbi.nlm.nih.gov/11846406
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10
A peptide inhibitor of cholesteryl ester transfer protein identified by screening a bacteriophage display library
Autor: H. David Fischer, Laurence A. Erickson, Paul D. Bonin, Carol A. Bannow, Clark W. Smith
Publikováno v: The journal of peptide research : official journal of the American Peptide Society. 51(3)
We screened a bacteriophage display library of random decapeptides to identify peptide inhibitors of cholesteryl ester transfer protein (CETP). After affinity selection against CETP, bacteriophage-infected Escherichia coli were plated at clonal densi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::283467b35496b5bae5fc2c2861433f3f
https://pubmed.ncbi.nlm.nih.gov/9531425
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