The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin - Test2 - elhamkhani - TriplyDB

The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

http://www.wikidata.org/entity/Q27733342

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Bioenergetics of the Archaea.Antimalarial activities of peptide antibiotics isolated from fungi The structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride Structural model of F1-ATPase and the implications for rotary catalysis Structure of the bacteriophage T4 DNA adenine methyltransferase Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria The three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio cholerae Structure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP Synthase The dimer formed by the periplasmic domain of EpsL from the Type 2 Secretion System of Vibrio parahaemolyticus Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis Intergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling.Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.ATP synthesis driven by proton transport in F1F0-ATP synthase.How azide inhibits ATP hydrolysis by the F-ATPases.Inhibition of mitochondrial proton F0F1-ATPase/ATP synthase by polyphenolic phytochemicals.Understanding structure, function, and mutations in the mitochondrial ATP synthase.The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology.Transport bicycles.ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides Medicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.Four Classes of Structurally Unusual Peptides from Two Marine-Derived Fungi: Structures and Bioactivities.ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas.Inhibition of ATP synthase by chlorinated adenosine analogue.Traditional and novel tools to probe the mitochondrial metabolism in health and disease.Catalytic robustness and torque generation of the F1-ATPase A therapeutic connection between dietary phytochemicals and ATP synthase.Chromatophore vesicles of Rhodobacter capsulatus contain on average one F(O)F(1)-ATP synthase each.Conformational dynamics of the F1-ATPase beta-subunit: a molecular dynamics study.Nitroarginine and tetrahydrobiopterin binding to the haem domain of neuronal nitric oxide synthase using a scintillation proximity assay.Functional halt positions of rotary FOF1-ATPase correlated with crystal structures.Inhibition sites in F1-ATPase from bovine heart mitochondria.Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology Binding affinities and protein ligand complex geometries of nucleotides at the F(1) part of the mitochondrial ATP synthase obtained by ligand docking calculations.Rebuilt 3D structure of the chloroplast f1 ATPase-tentoxin complex.The subunit b dimer of the FOF1-ATP synthase: interaction with F1-ATPase as deduced by site-specific spin-labeling.

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P2860

The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

http://www.wikidata.org/entity/Q27733342

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1996 nî lūn-bûn

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1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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type

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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PNAS.93.18.9420

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Proceedings of the National Academy of Sciences of the United States of America

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

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A G Leslie

http://www.w3.org/2001/XMLSchema#string

I M Fearnley

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J E Walker

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S K Buchanan

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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

Improved methods for building protein models in electron density maps and the location of errors in these models

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B

The binding change mechanism for ATP synthase--some probabilities and possibilities

The regulation of catalysis in ATP synthase.

Antibiotic inhibitors of mitochondrial ATP synthesis.

Inhibitors of the ATP synthethase system.

The defective proton-ATPase of uncA mutants of Escherichia coli. Identification by DNA sequencing of residues in the alpha-subunit which are essential for catalysis or normal assembly.

Inhibition of spinach chloroplasts photophosphorylation by the antibiotics leucinostatin and efrapeptin.

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4721421

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10.1073/PNAS.93.18.9420

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18

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93

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Mark J van Raaij

Jan Pieter Abrahams

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1996-09-01T00:00:00Z

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14413369

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8790345

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38443

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