Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Carol D. Farr"'
1
Ischemic Preconditioning Regulates Expression of microRNAs and a Predicted Target, MeCP2, in Mouse Cortex
Autor: Theresa A. Lusardi, Carol D. Farr, Giuseppe Pignataro, Craig L Faulkner, Jing-Quan Lan, Julie A. Saugstad, Roger P. Simon, Tao Yang
Publikováno v: Journal of Cerebral Blood Flow & Metabolism. 30:744-756
Preconditioning describes the ischemic stimulus that triggers an endogenous, neuroprotective response that protects the brain during a subsequent severe ischemic injury, a phenomenon known as ‘tolerance’. Ischemic tolerance requires new protein s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6fff87ecfeb62ee66a1eae96270d69e
https://doi.org/10.1038/jcbfm.2009.253
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2
Three-Dimensional Quantitative Structure−Activity Relationship Analysis of Ligand Binding to Human Sequence Antidigoxin Monoclonal Antibodies Using Comparative Molecular Field Analysis
Autor: Michael R. Tabet, Xia Wang, Anil Nair, Carol D. Farr, Dianne M. Fishwild, William J. Welsh, William J. Ball
Publikováno v: Journal of Medicinal Chemistry. 45:3257-3270
The present study indicates that the newly generated human sequence antidigoxin monoclonal antibody (mAb), 1B3, binds digoxin with a different fine specificity binding than our previously obtained human sequence monoclonal antibodies (mAbs) (Ball, W.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::749b57060cdebae15e5c8f3f2dca4092
https://doi.org/10.1021/jm0102811
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3
Three-dimensional quantitative structure-activity relationship modeling of cocaine binding by a novel human monoclonal antibody
Autor: Carol D. Farr, Michael R. Tabet, Andrew B. Norman,‡,‖ and, W. James Ball, Stefan Paula
Publikováno v: Journal of medicinal chemistry. 47(1)
Human monoclonal antibodies (mAbs) designed for immunotherapy have a high potential for avoiding the complications that may result from human immune system responses to the introduction of nonhuman mAbs into patients. This study presents a characteri
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76f6457df6236dcb1fee2664b29f8fed
https://pubmed.ncbi.nlm.nih.gov/14695827
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4
Three-dimensional quantitative structure-activity relationship study of the inhibition of Na(+),K(+)-ATPase by cardiotonic steroids using comparative molecular field analysis
Autor: Xia Wang, William J. Welsh, Michael R. Tabet, Carol D. Farr, William J. Ball, Craig J. Burd
Publikováno v: Biochemistry. 41(4)
Na(+),K(+)-ATPase is a transmembrane protein that transports sodium and potassium ions across cell membranes during an activity cycle that uses the energy released by ATP hydrolysis. Cardiotonic steroids (digitalis) inhibit this activity and conseque
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb6733a7584008f63927f1359a8b2f78
https://pubmed.ncbi.nlm.nih.gov/11802712
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5
Visualization of a slow, ATP-induced structural transition in the bacterial molecular chaperone DnaK
Autor: Carol D. Farr, Sergey V. Slepenkov, Stephan N. Witt
Publikováno v: The Journal of biological chemistry. 273(16)
Recent reports have shown that the binding of ATP to a 70-kDa molecular chaperone induces a rapid global conformational transition from a "high affinity" state to a "low affinity" state, where these states are defined by tight and weak binding to (po
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adac2181b6447a75b71137a9d539406f
https://pubmed.ncbi.nlm.nih.gov/9545310
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6
Kinetic evidence for peptide-induced oligomerization of the molecular chaperone DnaK at heat shock temperatures
Autor: Carol D. Farr, Stephan N. Witt
Publikováno v: Biochemistry. 36(35)
The pre-steady-state kinetics of the binding of a fluorescent peptide (dansyl-KLIGVLSSLFRPK, fVSV13) to the Escherichia coli molecular chaperone DnaK were investigated over a range of temperatures (25-42 degrees C). At 42 degrees C, over a wide range
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b91c418af12e03b4a6100168664529a0
https://pubmed.ncbi.nlm.nih.gov/9271511
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7
Large activation energy barriers to chaperone-peptide complex formation and dissociation
Autor: Floyd Galiano, Carol D. Farr, Stephan N. Witt
Publikováno v: Biochemistry. 34(47)
To probe the mechanism of chaperone substrate selection, we have investigated the kinetics of complex formation and dissociation between the molecular chaperone DnaK and a short peptide (Cro, representing amino acids 1-12 of the cro repressor protein
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c588c39295459d6ed8c61ad1b6cbd8d
https://pubmed.ncbi.nlm.nih.gov/7492560
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9
ATP lowers the activation enthalpy barriers to Dnak-peptide complex formation and dissociation
Autor: Stephan N. Witt, Carol D. Farr
Publikováno v: Cell Stress & Chaperones. 4:77
The role of nucleotide in controlling the pre-steady-state kinetics of peptide binding to the Escherichia coli 70-kDa molecular chaperone DnaK was investigated using stopped-flow fluorescence. The peptide used in this study, fVSV13 (representing amin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::469819831e73cd257d6f662284d2bb13
https://doi.org/10.1379/1466-1268(1999)004<0077:altaeb>2.3.co
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