Search Results - (Author, Cooperation:B. T. Chait)
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1Latest Papers from Table of Contents or Articles in PressM. Di Virgilio ; E. Callen ; A. Yamane ; W. Zhang ; M. Jankovic ; A. D. Gitlin ; N. Feldhahn ; W. Resch ; T. Y. Oliveira ; B. T. Chait ; A. Nussenzweig ; R. Casellas ; D. F. Robbiani ; M. C. Nussenzweig
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-01-12Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; B-Lymphocytes/immunology/metabolism ; Cell Cycle Proteins/antagonists & inhibitors/metabolism ; Cells, Cultured ; Chromosomal Proteins, Non-Histone/*metabolism ; DNA/*metabolism ; *DNA Breaks, Double-Stranded ; DNA Repair ; DNA-Binding Proteins/antagonists & inhibitors/*metabolism ; G1 Phase ; G2 Phase ; Genomic Instability ; *Immunoglobulin Class Switching ; Mice ; Phosphorylation ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; S Phase ; Telomere-Binding Proteins/*metabolism ; Tumor Suppressor Proteins/antagonists & inhibitors/metabolismPublished by: -
2Latest Papers from Table of Contents or Articles in PressJ. F. Scheid ; H. Mouquet ; B. Ueberheide ; R. Diskin ; F. Klein ; T. Y. Oliveira ; J. Pietzsch ; D. Fenyo ; A. Abadir ; K. Velinzon ; A. Hurley ; S. Myung ; F. Boulad ; P. Poignard ; D. R. Burton ; F. Pereyra ; D. D. Ho ; B. D. Walker ; M. S. Seaman ; P. J. Bjorkman ; B. T. Chait ; M. C. Nussenzweig
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-07-19Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Amino Acid Sequence ; Antibodies, Neutralizing/*chemistry/*immunology/metabolism ; Antibody Affinity ; Antibody Specificity ; Antigens, CD4/immunology/*metabolism ; Binding Sites ; Binding Sites, Antibody ; Cloning, Molecular ; Consensus Sequence ; Crystallography, X-Ray ; Genes, Immunoglobulin Heavy Chain ; HIV Antibodies/*chemistry/*immunology/metabolism ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV Infections/immunology ; Humans ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Heavy Chains/chemistry ; Immunoglobulin Light Chains/chemistry ; Molecular Mimicry ; Molecular Sequence Data ; Mutation ; Protein ConformationPublished by: -
3Articles: DFG German National LicensesStaff View
ISSN: 0030-493XKeywords: Chemistry ; Analytical Chemistry and SpectroscopySource: Wiley InterScience Backfile Collection 1832-2000Topics: Chemistry and PharmacologyAdditional Material: 2 Ill.Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesBaptista, G. B. ; Brunelle, A. ; Chaurand, P. ; Della-negra, S. ; Depauw, J. ; Le Bayec, Y. ; Chait, B. T.
New York, NY : Wiley-Blackwell
Published 1991Staff ViewISSN: 0951-4198Keywords: Chemistry ; Analytical Chemistry and SpectroscopySource: Wiley InterScience Backfile Collection 1832-2000Topics: PhysicsNotes: A time-to-digital converter coupled to a charge-to-digitalconverter has been used to record mass spectra in matrix-assisted laser desorption(MALD) time-of-flight mass spectrometry. Masses above 100 000 Da have been detected by ion counting. Utilizing an electrostatic mirror, good mass resolution has been achieved in MALD. When the number of detedted secondary ions is small the sensitivity of mass measurements is improved by using a charge-to-digital converter rather than a transient recorder.Additional Material: 11 Ill.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesKnierman, Michael D. ; Coligan, John E. ; Parker, Kenneth C. ; Chait, B. T.
New York, NY : Wiley-Blackwell
Published 1994Staff ViewISSN: 0951-4198Keywords: Chemistry ; Analytical Chemistry and SpectroscopySource: Wiley InterScience Backfile Collection 1832-2000Topics: PhysicsNotes: A method is described by which a sequence-dependent peptide fingerprint can be rapidly obtained upon partial hydrolysis of peptides with hydrochloric acid and subsequent analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). When synthetic peptides are treated with 3M HCI for 5 min at 110°C, amino acids are released in turn from the C-terminus or, depending on the peptide, from the N-terminus. Sequence information can be deduced by identifying the amino acid whose mass corresponds to the difference in MW between the major hydrolysis products, beginning from the MW of the starting peptide. A similar pattern exclusively from the C-terminus has been obtained using pentafluoropropionic acid as a hydrolyzing agent (Tsugita et al. Eur. J. Biochem. 206, 691 (1992)), but required longer hydrolysis time and more handling prior to analysis. The technique we have developed could be used to obtain a sequence-dependent ‘fingerprint’ for a peptide cheaply and rapidly, starting with picomole amounts of peptide, because the hydrolysate can be directly analyzed by MALDI. This methodology might be especially useful for confirming the identity of peptides during peptide mapping.Additional Material: 1 Ill.Type of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesLafortune, F. ; Beavis, R. ; Tang, X. ; Standing, K. G. ; Chait, B. T. ; Sundqvist, Bo
New York, NY : Wiley-Blackwell
Published 1987Staff ViewISSN: 0951-4198Keywords: Chemistry ; Analytical Chemistry and SpectroscopySource: Wiley InterScience Backfile Collection 1832-2000Topics: PhysicsAdditional Material: 4 Ill.Type of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesStaff View
ISSN: 0951-4198Keywords: Chemistry ; Analytical Chemistry and SpectroscopySource: Wiley InterScience Backfile Collection 1832-2000Topics: PhysicsNotes: The plasma desorption (PD) mass spectra of several enzymes and proenzymes are reported. Chymotrypsin and chymotrypsinogen both yield usable PD mass spectra; however, the single-chain chymotrypsinogen exhibits better sensitivity and less fragmentation than the multi-chain chymotrypsin. Porcine pepsinogen contains 11 more basic residues (lysine and arginine) than porcine pepsin, but this does not lead to an increase in positive ion response. In fact, the additional basic residues may hinder response by increasing the strength of the interaction between the protein and the nitrocellulose surface. A series of subtilisins showed comparable PD mass spectrometric, response despite the fact that they differ considerably in primary sequence. Finally, PD mass spectrometry was used to correct the previously reported mass of a heat-stable protease, a value that we found to be in error by almost 5000 Da.Additional Material: 4 Ill.Type of Medium: Electronic ResourceURL: