Zobrazeno 1 - 10
of 22
pro vyhledávání: '"James E, Knapp"'
Autor:
Jaimie Adams, Jill Sharma, Taylor Boyd, Edwin Gunn, Robert Dunwoody, R E Garner, Claudia Alvarado, James E. Knapp, John Lamb, Brittany L. House, Traci Ness
Publikováno v:
Biomedicines, Vol 7, Iss 2, p 41 (2019)
Biomedicines
Volume 7
Issue 2
Biomedicines
Volume 7
Issue 2
Hemoglobin (Hb) released during red blood cell lysis can initiate TLR4-dependent signaling and trigger NF-&kappa
B activation in surrounding cells. Observations of chronic bleeding in various cancers leads us to hypothesize that Hb and Hb degrad
B activation in surrounding cells. Observations of chronic bleeding in various cancers leads us to hypothesize that Hb and Hb degrad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f385306e12bbd8278a09aae91fd2e9c6
https://www.mdpi.com/2227-9059/7/2/41
https://www.mdpi.com/2227-9059/7/2/41
Autor:
James E. Knapp, Jordi Cohen, Quentin H. Gibson, Vukica Šrajer, Klaus Schulten, R. Pahl, Jeffry C. Nichols, William E. Royer
Publikováno v:
Structure. 17:1494-1504
SummaryAs in many other hemoglobins, no direct route for migration of ligands between solvent and active site is evident from crystal structures of Scapharca inaequivalvis dimeric HbI. Xenon (Xe) and organic halide binding experiments, along with com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a8e2e24bc2cbe0c0abd35d8ad156a72
https://doi.org/10.1016/j.str.2009.09.004
https://doi.org/10.1016/j.str.2009.09.004
Autor:
D. W. Carroll, Janet E. Lawson, Lester J. Reed, Marvin L. Hackert, Stephen R. Ernst, James E. Knapp
Publikováno v:
Protein Science. 9:37-48
The dihydrolipoamide succinyltransferase (E2o) component of the alpha-ketoglutarate dehydrogenase complex catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A. E2o is normally a 24-mer, but is found as a tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac5cb5ff062bb3652cdde7d6361bd99c
https://doi.org/10.1110/ps.9.1.37
https://doi.org/10.1110/ps.9.1.37
Publikováno v:
Biochemistry. 44:14419-14430
Residue F4 (Phe 97) undergoes the most dramatic ligand-linked transition in Scapharca dimeric hemoglobin, with its packing in the heme pocket in the unliganded (T) state suggested to be a primary determinant of its low affinity. Mutation of Phe 97 to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96831bc92fdad815b4d699613a1b2070
https://doi.org/10.1021/bi051052+
https://doi.org/10.1021/bi051052+
Publikováno v:
Journal of Biological Chemistry. 280:27477-27480
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cafe108f9c09ca89c9991ddd0474da1
https://doi.org/10.1074/jbc.r500006200
https://doi.org/10.1074/jbc.r500006200
Autor:
Alan M. Friedman, David A. Chavous, Jens Bjerregaard, James E. Knapp, Eric J. Bennett, William E. Royer, Clare M. O'Connor
Publikováno v:
Biochemistry. 42:12844-12853
Protein L-isoaspartyl methyltransferases (PIMT; EC 2.1.1.77) catalyze the S-adenosylmethionine-dependent methylation of L-isoaspartyl residues that arise spontaneously in proteins with age, thereby initiating a repair process that restores the normal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd5da8b01ad689661f1bb86525a34c16
https://doi.org/10.1021/bi034891+
https://doi.org/10.1021/bi034891+
Autor:
William E. Royer, James E. Knapp
Publikováno v:
Biochemistry. 42:4640-4647
Cooperative ligand binding in the dimeric hemoglobin (HbI) from the blood clam Scapharca inaequivalvis is mediated primarily by tertiary structural changes, but with a small quaternary rearrangement (approximately 3 degrees), based on analysis of dis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab09945cbddadd21eb856f2c8a7023bc
https://doi.org/10.1021/bi027136p
https://doi.org/10.1021/bi027136p
Publikováno v:
Trends in Biochemical Sciences. 26:297-304
Assembly of hemoglobin subunits into cooperative complexes produces a remarkable variety of architectures, ranging in oligomeric state from dimers to complexes containing 144 hemoglobin subunits. Diverse stereochemical mechanisms for modulating ligan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6203119788da3eb763cf4495fa234cb
https://doi.org/10.1016/s0968-0004(01)01811-4
https://doi.org/10.1016/s0968-0004(01)01811-4
Publikováno v:
Journal of Biological Chemistry. 275:13517-13528
Lampreys, among the most primitive living vertebrates, have hemoglobins (Hbs) with self-association and ligand-binding properties very different from those that characterize the α2β2 tetrameric Hbs of higher vertebrates. Monomeric, ligated lamprey
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::512c7aa30eb77533049c01cf3c75c198
https://doi.org/10.1074/jbc.275.18.13517
https://doi.org/10.1074/jbc.275.18.13517
Autor:
Lester J. Reed, James E. Knapp, Mohammad A. Yazdi, David T. Mitchell, Stephen R. Ernst, Marvin L. Hackert
Publikováno v:
Journal of Molecular Biology. 280:655-668
The dihydrolipoamide succinyltransferase (E2o) component of the 2-oxoglutarate dehydrogenase multienzyme complex is composed of 24 subunits arranged with 432 point group symmetry. The catalytic domain (CD) of the E2o component catalyzes the transfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06b9e5f646d9cc75e4f296663d3b6ea0
https://doi.org/10.1006/jmbi.1998.1924
https://doi.org/10.1006/jmbi.1998.1924