Evolution of organellar proton-ATPases
N Nelson - Biochimica et Biophysica Acta (BBA)-Bioenergetics, 1992 - Elsevier
Proton ATPases function in biological energy conversion in every known living cell. Their
ubiquity and antiquity make them a prime source for evolutionary studies. There are two …
ubiquity and antiquity make them a prime source for evolutionary studies. There are two …
P-glycoprotein function involves conformational transitions detectable by differential immunoreactivity
EB Mechetner, B Schott, BS Morse… - Proceedings of the …, 1997 - National Acad Sciences
The MDR1 P-glycoprotein (Pgp), a member of the ATP-binding cassette family of
transporters, is a transmembrane ATPase efflux pump for various lipophilic compounds …
transporters, is a transmembrane ATPase efflux pump for various lipophilic compounds …
Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities.
LT Haber, GC Walker - The EMBO journal, 1991 - embopress.org
The Salmonella typhimurium and Escherichia coli MutS protein is one of several methyl‐
directed mismatch repair proteins that act together to correct replication errors. MutS is …
directed mismatch repair proteins that act together to correct replication errors. MutS is …
Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution
D Dreusicke, PA Karplus, GE Schulz - Journal of molecular biology, 1988 - Elsevier
The crystal structure of porcine cytosolic adenylate kinase has been established at 2.1 Å
resolution using a restrained least-squares refinement method. Based on 11,251 …
resolution using a restrained least-squares refinement method. Based on 11,251 …
C-Terminal Tails of Sulfonylurea Receptors Control ADP-Induced Activation and Diazoxide Modulation of ATP-Sensitive K+ Channels
T Matsuoka, K Matsushita, Y Katayama… - Circulation …, 2000 - Am Heart Assoc
The ATP-sensitive K+ (KATP) channels are composed of the pore-forming K+ channel Kir6.
0 and different sulfonylurea receptors (SURs). SUR1, SUR2A, and SUR2B are sulfonylurea …
0 and different sulfonylurea receptors (SURs). SUR1, SUR2A, and SUR2B are sulfonylurea …
Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli
J Reinstein, M Brune, A Wittinghofer - Biochemistry, 1988 - ACS Publications
Revised Manuscript Received February 23, 1988 abstract: The adk gene of Escherichia coli
has been used to overexpressthe adenylate kinase protein in two ways:(1) by cloning the …
has been used to overexpressthe adenylate kinase protein in two ways:(1) by cloning the …
Characterization of yeast Vps33p, a protein required for vacuolar protein sorting and vacuole biogenesis
vps33 mutants missort and secrete multiple vacuolar hydrolases and exhibit extreme defects
in vacuolar morphology. Toward a molecular understanding of the role of the VPS33 gene in …
in vacuolar morphology. Toward a molecular understanding of the role of the VPS33 gene in …
[HTML][HTML] Characterization of the ATP binding site on Escherichia coli DNA gyrase. Affinity labeling of Lys-103 and Lys-110 of the B subunit by pyridoxal 5 '-diphospho-5 …
JK Tamura, M Gellert - Journal of Biological Chemistry, 1990 - Elsevier
We have labeled the adenosine triphosphate binding site of Escherichia coli DNA gyrase
with the ATP affinity analog,[3H] pyridoxal 5 '-diphospho-5 '-adenosine (PLP-AMP). PLP …
with the ATP affinity analog,[3H] pyridoxal 5 '-diphospho-5 '-adenosine (PLP-AMP). PLP …
[HTML][HTML] Identification of lysine 15 at the active site in Escherichia coli glycogen synthase. Conservation of Lys-X-Gly-Gly sequence in the bacterial and mammalian …
K Furukawa, M Tagaya, M Inouye, J Preiss… - Journal of Biological …, 1990 - Elsevier
Glycogen synthases from Escherichia coli and mammalian muscle differ in many respects
including regulation, sugar nucleotide specificity, and primary sequence. To compare the …
including regulation, sugar nucleotide specificity, and primary sequence. To compare the …
[HTML][HTML] Characterization of the regulatory thioredoxin site of phosphoribulokinase.
MA Porter, CD Stringer, FC Hartman - Journal of Biological Chemistry, 1988 - Elsevier
Phosphoribulokinase is light-regulated via thioredoxin by reversible oxidation/reduction of
sulfhydryl/disulfide groups. To identify the cysteinyl residues that are involved in regulation …
sulfhydryl/disulfide groups. To identify the cysteinyl residues that are involved in regulation …