Structure of the Subunit C Oligomer in the F1Fo ATP Synthase: Model Derived From Solution Structure of the Monomer and Cross-Linking in the Native Enzyme

Proceedings of the National Academy of Sciences of the United States of America - United States
doi 10.1073/pnas.96.14.7785
Full Text
Abstract

Available in full text

Date
Authors
Publisher

Proceedings of the National Academy of Sciences

Related search

Rotation of the C Subunit Oligomer in Fully Functional F1Fo ATP Synthase

Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
2001English

ATP Synthase – The Structure of the Stator Stalk

Trends in Biochemical Sciences
BiochemistryMolecular Biology
2007English

The C-Subunit of the ATP Synthase Forms the Pore of the PTP

Biophysical Journal
Biophysics
2014English

The C-Subunit Ring of the F1FO ATP Synthase Constitutes a Leak Channel That Regulates Cellular Metabolic Efficiency by Counteracting the H+ Translocator

Biophysical Journal
Biophysics
2012English

The Chemical Structure of Asphaltene Derived From Coal Hydrogenation. Oligomer Structure of Asphaltene Molecule.

NIPPON KAGAKU KAISHI
1990English

Recombinant Production and Purification of the Subunit C of Chloroplast ATP Synthase

Protein Expression and Purification
Biotechnology
2011English

Solution Structure of the Mature HIV-1 Protease Monomer

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2003English

Three Distinct Isoforms of ATP Synthase Subunit C Are Expressed in T. Brucei and Assembled Into the Mitochondrial ATP Synthase Complex

PLoS ONE
Multidisciplinary
2013English

Modulation of the Channel Activity of the C-Subunit of the ATP Synthase by Polyphosphate and Polyhydroxybutyrate

Biophysical Journal
Biophysics
2019English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy