Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Tattanahalli L. Nagabhushan"'
Autor:
Raymond Cure, Yan-Hui Liu, David Wylie, Jia Zhao, Susan Cannon-Carlson, Collette M. Cutler, Birendra N. Pramanik, Tattanahalli L. Nagabhushan, Xiaoyu Yang
Publikováno v:
Analytical Biochemistry. 408:105-117
The isoforms Iso-2, Iso-3, and Iso-4 of Escherichia coli-derived recombinant human interferon alpha-2b (rhIFN α-2b), generated by posttranslational modifications of the protein during fermentation, present a major problem in terms of purification an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b2e4ddcb81fcace84ca36b81fd7336c
https://doi.org/10.1016/j.ab.2010.08.033
https://doi.org/10.1016/j.ab.2010.08.033
Publikováno v:
Canadian Journal of Chemistry. 80:1166-1173
The structures of several type I interferons (IFNs) are known. We review the structural information known for IFN alphas and compare them to other interferons and cytokines. We also review the structural information known or proposed for IFNcell re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6557977d78fb33ca230662df1eae90b2
https://doi.org/10.1139/v02-158
https://doi.org/10.1139/v02-158
Autor:
Tattanahalli L. Nagabhushan, Brassard Diana L, Jessie M. English, Michael Malkowski, Paul Kirschmeier, W. Robert Bishop
Publikováno v:
Experimental Cell Research. 273:138-146
Farnesyl protein transferase inhibitors (FTIs) reverse the transformed phenotype of fibroblasts expressing activated H-Ras and block anchorage-independent growth and tumorigenesis of tumor cell lines independent of their Ras mutational status. FTIs i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90ecb209862a2908d76faedf47d6ae9e
https://doi.org/10.1006/excr.2001.5440
https://doi.org/10.1006/excr.2001.5440
Autor:
Tattanahalli L. Nagabhushan, Mark R. Walter, Matthew H. Parker, Giovanni Rizzi, Ruth DiGiacomo, Brandi Curry, Stephen R. Indelicato, Aimee Landar
Publikováno v:
Journal of Molecular Biology. 299:169-179
A mutant form of human interferon-gamma (IFN-gamma SC1) that binds one IFN-gamma receptor alpha chain (IFN-gamma R alpha) has been designed and characterized. IFN-gamma SC1 was derived by linking the two peptide chains of the IFN-gamma dimer by a sev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e2e8e816d10819826cf86323f68296b
https://doi.org/10.1006/jmbi.2000.3734
https://doi.org/10.1006/jmbi.2000.3734
Autor:
Tattanahalli L. Nagabhushan, John Bradford Bishop, Lawrence J. DeLucas, Paul Reichert, G. David Smith, Marianna M. Long
Publikováno v:
Journal of Crystal Growth. 168:233-243
The protein crystal growth facility (PCF) is space-flight hardware that accommodates large scale protein crystal growth experiments using temperature change as the inductive step. Recent modifications include specialized instrumentation for monitorin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a31b53be35caf2f0e9b538d63c86cd5f
https://doi.org/10.1016/0022-0248(96)00325-9
https://doi.org/10.1016/0022-0248(96)00325-9
Autor:
Tattanahalli L. Nagabhushan, Rosalinda Syto, Mark R. Walter, William J. Cook, William T. Windsor, James Fossetta, Leigh J Walter
Publikováno v:
Proteins: Structure, Function, and Genetics. 26:108-114
X-ray diffraction quality crystals have been obtained from a complex between interferon gamma and the extracellular domain of its high-affinity cell surface receptor. The crystals were obtained from interferon gamma/interferon gamma receptor complexe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7460176cf3c00a8ce4c906d7b5270965
https://doi.org/10.1002/(sici)1097-0134(199609)26:1<108::aid-prot10>3.0.co
https://doi.org/10.1002/(sici)1097-0134(199609)26:1<108::aid-prot10>3.0.co
Publikováno v:
Journal of Mass Spectrometry. 30:1752-1763
Electrospray (ES) ionization mass spectrometric analysis of CHO-derived recombinant interleukin-4 (IL-4) before and after deglycosylation with peptide: N-glycosidase F is described. That proved useful not only in deriving the size of the attached car
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ffe8367df274fc98a90ab574d87f54e9
https://doi.org/10.1002/jms.1190301217
https://doi.org/10.1002/jms.1190301217
Publikováno v:
Biochemistry. 34:12118-12125
The crystal structure of recombinant human interleukin 10 (rhIL-10) has been determined by X-ray crystallography at 2.0 A resolution. Interleukin 10 is a dimer composed of identical polypeptide chains related by a 2-fold axis. The molecule is predomi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::157e5d1c36f17933b822370c2df42da9
https://doi.org/10.1021/bi00038a004
https://doi.org/10.1021/bi00038a004
Autor:
Dina M. Martin, Markus Maeurer, Tattanahalli L. Nagabhushan, Eric C. Huang, Michael T. Lotze, Chiara Castelli, Walter J. Storkus, Birendra N. Pramanik, Giorgio Parmiani
Publikováno v:
The Journal of Experimental Medicine
We and others have previously reported that melanoma-specific, cytotoxic T lymphocytes (CTL) define a minimum of six class I-presented peptide epitopes common to most HLA-A2+ melanomas. Here we show that three of these peptide epitopes are coordinate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69a857c6c5e6ce0363b681f7b0823cb8
https://doi.org/10.1084/jem.181.1.363
https://doi.org/10.1084/jem.181.1.363
Autor:
Michael Karas, Anthony Tsarbopoulos, Birendra N. Pramanik, Tattanahalli L. Nagabhushan, Kerstin Strupat, Franz Hillenkamp
Publikováno v:
Analytical Chemistry. 66:2062-2070
The mass spectrometric (MS) techniques of 252Cf-plasma desorption (PD) and matrix-assisted laser desorption/ionization (MALDI) are compared in the molecular weight determination and the mapping analysis of several recombinant proteins and glycoprotei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8037cebcd44f86d05d3532499a8e5921
https://doi.org/10.1021/ac00085a022
https://doi.org/10.1021/ac00085a022