Zobrazeno 1 - 10
of 14
pro vyhledávání: '"John S"'
Autor:
Eugene Khandros, Joel P. Mackay, Claire F. Dickson, Todd L. Mollan, John S. Olson, Peter A. Lay, Anne M. Rich, Jason A. Lowry, W. d’Avigdor, Daniel A. T. Collins, Mitchell J. Weiss, David A. Gell
Publikováno v:
Journal of Biological Chemistry. 288:19986-20001
α-Hemoglobin (αHb)-stabilizing protein (AHSP) is a molecular chaperone that assists hemoglobin assembly. AHSP induces changes in αHb heme coordination, but how these changes are facilitated by interactions at the αHb·AHSP interface is not well u
Publikováno v:
Journal of Biological Chemistry. 286:10515-10529
His(E7) to Trp replacements in HbA lead to markedly biphasic bimolecular CO rebinding after laser photolysis. For isolated mutant subunits, the fraction of fast phase increases with increasing [CO], suggesting a competition between binding to an open
Autor:
David Dantsker, Camille J. Roche, John S. Olson, Joel M. Friedman, Uri Samuni, George C. Blouin
Publikováno v:
Journal of Biological Chemistry. 280:38740-38755
After photodissociation, ligand rebinding to myoglobin exhibits complex kinetic patterns associated with multiple first-order geminate recombination processes occurring within the protein and a simpler bimolecular phase representing second-order liga
Publikováno v:
Journal of Biological Chemistry. 278:23027-23035
To localize the regions of lipoprotein lipase (LPL) that are responsive to activation by apoC-II, an apoC-II peptide fragment was cross-linked to bovine LPL. Following chemical hydrolysis and peptide separation, a specific fragment of LPL (residues 6
Autor:
Allison E. Arch, Abu Z. M. Saleh, Vinh-Phúc Nguyen, John S. Kim, Hai Yan, Flavia Piazza, John J. Krolewski
Publikováno v:
Journal of Biological Chemistry. 277:9713-9721
The interferon-alpha (IFNalpha) receptor consists of two subunits, the IFNalpha receptor 1 (IFNaR1) and 2 (IFNaR2) chains. Following ligand binding, IFNaR1 is phosphorylated on tyrosine 466, and this site recruits Stat2 via its SH2 domain. In contras
Publikováno v:
Journal of Biological Chemistry. 276:5177-5188
The effects of mutagenesis on geminate and bimolecular O2 rebinding to 90 mutants at 27 different positions were used to map pathways for ligand movement into and out of sperm whale myoglobin. By analogy to a baseball glove, the protein "catches" and
Autor:
Jonathan B. Wittenberg, R. Ashley Lile, K. Vyas, John S. Olson, Xuefeng Zhao, Bao D. Nguyen, Gerd N. La Mar, Eric Allen Brucker, George N. Phillips
Publikováno v:
Journal of Biological Chemistry. 273:9517-9526
The bivalve mollusc Lucina pectinata harbors sulfide-oxidizing chemoautotrophic bacteria and expresses a monomeric hemoglobin I, HbI, with normal O2, but extraordinarily high sulfide affinity. The crystal structure of aquomet Lucina HbI has revealed
Autor:
Bernd Bukau, Alexander Buchberger, Holger Theyssen, John S. McCarty, Giuseppe Virgallita, Philipp Milkereit, Jochen Reinstein, Hartwig Schröder
Publikováno v:
The Journal of Biological Chemistry
Interactions of the DnaK (Hsp70) chaperone from Escherichia coli with substrates are controlled by ATP. Nucleotide-induced changes in DnaK conformation were investigated by monitoring changes in tryptic digestion pattern and tryptophan fluorescence.
Autor:
Bashiri, Ghader1, Grove, Tyler L.2, Hegde, Subray S.2, Lagautriere, Thomas1, Gerfen, Gary J.2, Almo, Steven C.2, Squire, Christopher J.1, Blanchard, John S.2, Baker, Edward N.1 ted.baker@auckland.ac.nz
Publikováno v:
Journal of Biological Chemistry. 8/30/2019, Vol. 294 Issue 35, p13158-13170. 13p.
Autor:
Zheng, Suilan1, Krump, Nathan A.2, McKenna, Mary M.2, Yen-Hsing Li1, Hannemann, Anke3, Garrett, Lisa J.4, Gibson, John S.3, Bodine, David M.2 tedyaz@mail.nih.gov, Low, Philip S.1 plow@purdue.edu
Publikováno v:
Journal of Biological Chemistry. 2/15/2019, Vol. 294 Issue 7, p2519-2528. 11p.