The rotary mechanism of the ATP synthase. - Wikidata - wikimedia - TriplyDB

The rotary mechanism of the ATP synthase.

The rotary mechanism of the ATP synthase.

http://www.wikidata.org/entity/Q24642754

about

Artificial Molecular Machines The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1 Investigating mitochondrial redox state using NADH and NADPH autofluorescence Structures of membrane proteins.Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation.Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell.A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis The Concise Guide to PHARMACOLOGY 2013/14: transporters.Predicting Protein-protein Association Rates using Coarse-grained Simulation and Machine Learning.ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry.Trimeric form of intracellular ATP synthase subunit β of Aggregatibacter actinomycetemcomitans binds human interleukin-1β.Chemomechanical Coupling in Hexameric Protein-Protein Interfaces Harnesses Energy within V-Type ATPases.F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.The ATP synthase a-subunit of extreme alkaliphiles is a distinct variant: mutations in the critical alkaliphile-specific residue Lys-180 and other residues that support alkaliphile oxidative phosphorylation.Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane.Combination therapy targeting ectopic ATP synthase and 26S proteasome induces ER stress in breast cancer cells.Knockdown of DAPIT (diabetes-associated protein in insulin-sensitive tissue) results in loss of ATP synthase in mitochondria.PAB is an assembly chaperone that functions downstream of chaperonin 60 in the assembly of chloroplast ATP synthase coupling factor 1 The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length.Decomposing the space of protein quaternary structures with the interface fragment pair library.Nature of Pre-Earthquake Phenomena and their Effects on Living Organisms.Discerning the Chemistry in Individual Organelles with Small-Molecule Fluorescent Probes.How does transmembrane electrochemical potential drive the rotation of Fo motor in an ATP synthase?Biophysical comparison of ATP-driven proton pumping mechanisms suggests a kinetic advantage for the rotary process depending on coupling ratio.Recombinant production and purification of the subunit c of chloroplast ATP synthase.Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.The role of the betaDELSEED-loop of ATP synthase.Escherichia coli F1Fo-ATP synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits.A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.Mitochondrial-associated metabolic disorders: foundations, pathologies and recent progress.ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm.The Possible Role of Nonbilayer Structures in Regulating ATP Synthase Activity in Mitochondrial Membranes.Molecular Mechanisms of Increased Heart Rate in Shenxianshengmai-treated Bradycardia Rabbits.Global identification of genes affecting iron-sulfur cluster biogenesis and iron homeostasis.Cellular and molecular mechanisms of mitochondrial function.Smart nanomachines based on DNA self-assembly.How mitochondrial dynamism orchestrates mitophagy.Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking

P2860

Q26783064-36D3B895-8470-457F-87F3-BEF27D278A5C Q27676363-189341B1-9CF3-4285-8103-D5201E38FF81 Q28072889-946A4701-CD36-4C6C-86A1-F2AB8B770EE3 Q30391943-C2DD62F9-5D96-48F2-B92E-EE1254972800 Q30429196-8661DADB-E4BE-4187-B1EB-3F26A298E8B6 Q30435062-461B7E2F-9212-43A9-A7D2-7419DA85FD3F Q30438509-58D54CE4-4AC7-46C8-90EA-E72692FC1466 Q30486743-96D19B08-C36B-46B0-812E-C0B41B9CA147 Q33572785-24C4A2B6-F415-495A-A36C-D26FC64C9717 Q33685784-4156B2BF-E836-4001-B57C-69CC158CBF4C Q33886294-960845D3-9B57-46B7-94D5-900A80988F05 Q33919788-40071D72-66C3-4D3C-90BA-BEC4A3829280 Q33931346-87A13F38-840D-45B9-BBB1-9AC3C2097CA2 Q34186410-DC72DD92-98C5-493F-BC3C-547730566175 Q34400874-D4CD27A9-77B6-4D6C-8231-8DD5A3EECCCD Q34662342-F7CE0D30-0D39-443E-8140-AD1F5FD208D3 Q35063443-7AA178C4-6CFF-4BEC-9C73-76C05C48ABCF Q35279715-6E79E23E-F276-4448-8A24-484E038BCA31 Q35313850-2E0A5B25-F0E6-43E3-8A1D-F1F87284A83D Q35543556-3757D757-AA97-4D29-AF87-33E192730A7F Q35827122-5DBA4914-E7DA-48D2-AB0F-8DC474170049 Q36115905-DBC73B8E-662C-4D21-B967-A1D2775E328F Q36220484-E1DF541C-1BF8-4A6F-A8FF-804207A8B3A0 Q36314842-B0FC12D8-9B02-403A-B591-FA33AD156DCF Q36821850-5824EE9B-E72C-401F-91EA-1438FB324598 Q37132174-E780A508-7A2B-49F0-8DF3-A4B946A4F52A Q37160889-65D43B10-BB3A-440C-842E-FFF9C6EFD77B Q37168333-F7140FBA-5395-4DE2-B0E4-13FD76D41DE9 Q37312462-12FED3E4-5235-4EF6-885D-9E4DDBDDB00D Q37322964-AD239374-D7AC-4263-BE78-C4750CF8BB2E Q37369860-C20688A7-3FBA-43C7-A720-0C6402F4DAB9 Q37446710-2D47F0E0-2569-4619-BB70-079A59778C52 Q37511718-7FC049C8-3E03-4FB5-AD22-F11FA77606C9 Q37559852-F7EF0C87-1C3C-4DD0-90CE-883651A4CF5B Q37615566-C66D0EF2-A0DB-41D9-9CB1-9E3612E30153 Q37643419-2A03556A-3C0D-4C35-AF0A-683186AAEC9B Q38061270-C930C476-DFE7-486E-BCA3-7F734FDEE4B0 Q38115277-3C5F2BF6-FD4C-4DEE-BB04-FDAFE9A4B2EE Q38497008-458488D8-A13C-4FAB-A81F-F74D9FFA61E6 Q39323280-D9D10471-3522-44D3-91C3-6E0E3582C7A6

P2860

The rotary mechanism of the ATP synthase.

http://www.wikidata.org/entity/Q24642754

description

2008 nî lūn-bûn

@nan

2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

The rotary mechanism of the ATP synthase

@nl

The rotary mechanism of the ATP synthase.

@ast

The rotary mechanism of the ATP synthase.

@en

type

label

The rotary mechanism of the ATP synthase

@nl

The rotary mechanism of the ATP synthase.

@ast

The rotary mechanism of the ATP synthase.

@en

prefLabel

The rotary mechanism of the ATP synthase

@nl

The rotary mechanism of the ATP synthase.

@ast

The rotary mechanism of the ATP synthase.

@en

P1433

Q24642754-4DEF7A1D-553D-486E-A927-39BA37ADE56B

P1476

Q24642754-1B59A6BC-D396-442D-9B32-6CE402C9B2F6

P2093

Q24642754-750F1FF1-690D-473B-96BD-C3D940774974

Q24642754-75BB929D-C728-4E84-8517-B76DCCBC0FA2

Q24642754-A08D82D4-8D0A-4528-95C6-F362099395B7

P2860

Q24642754-01E9513C-C8E6-48BB-8464-C6744568F8AE

Q24642754-02607B6B-21F4-4D05-B0EC-242B00D2DF09

Q24642754-0672E4DF-384C-4550-A6D7-FD951A2197D3

Q24642754-08D95607-FF3F-48BE-99C9-88374CE24349

Q24642754-0A0A18C6-2B01-4EE4-A46F-2E714D74F2A0

Q24642754-0B6E60D6-D156-4BC8-A00F-4EAE3716883C

Q24642754-0C3C2F69-D3A6-4820-A464-216AD6409D3C

Q24642754-1205E527-BDCF-4D81-893E-DCBF7AEF343B

Q24642754-127A44EF-C4D5-4F40-8844-610B2BBA9FED

Q24642754-12D7A724-CEC8-4B39-8764-BCB980BA3340

P304

Q24642754-CEA7235D-3D69-4602-9FC3-0E2E2AF0EAF9

P31

Q24642754-2F396948-7A8E-41D6-A856-9125F44ECBDB

P3181

Q24642754-1CA68A3E-35A5-4AD2-9BDD-933747FEE399

P356

Q24642754-51D35FA1-49D7-417A-93E5-775EA5AFD45F

P407

Q24642754-3EF09520-ECD0-42AC-9C3A-B6A7F5FB84B4

P433

Q24642754-5583E3AA-86D2-4181-AAAB-87EBA86614C2

P478

Q24642754-A4B299D3-5B2C-4B32-93A6-1B80C1F0EA5D

P577

Q24642754-DF9AEB82-B5E4-4D8C-B3D9-0968FA2F5F56

P5875

Q24642754-740A78A0-63F5-4D9E-A891-D5F828245E16

P698

Q24642754-E6F56FC8-B1F0-4289-A97B-08BD72E4C47D

P921

Q24642754-C5A1FAAC-EC8F-4642-A85A-92CE9A9850FE

P932

Q24642754-6CCA0C7D-B55A-45D0-945F-A256590C88EB

P3181

P356

J.ABB.2008.05.004

P1433

Archives of Biochemistry and Biophysics

P1476

The rotary mechanism of the ATP synthase.

@en

P2093

Joanne A Baylis Scanlon

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

Marwan K Al-Shawi

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

Robert K Nakamoto

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

P2860

Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue

A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions

Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase

Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography

Molecular architecture of the rotary motor in ATP synthase

Structural changes linked to proton translocation by subunit c of the ATP synthase

Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain

P304

43-50

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

P31

scholarly article

P3181

4180910

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

P356

10.1016/J.ABB.2008.05.004

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

P407

P433

1

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

P478

476

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

P577

2008-05-20T00:00:00Z

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

P5875

5336067

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

P698

18515057

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

P921

P932

2581510

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