相关参考文献
注意：仅列出部分参考文献，下载原文获取全部文献信息。Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology
Alexander Hahn et al.
MOLECULAR CELL (2016)
Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance
Daniel G. Schep et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2016)
Rotary ATPases: A New Twist to an Ancient Machine
Werner Kuehlbrandt et al.
TRENDS IN BIOCHEMICAL SCIENCES (2016)
A modular platform for one-step assembly of multi-component membrane systems by fusion of charged proteoliposomes
Robert R. Ishmukhametov et al.
NATURE COMMUNICATIONS (2016)
Structure of a thermophilic F-1-ATPase inhibited by an epsilon-subunit: deeper insight into the epsilon-inhibition mechanism
Yasuo Shirakihara et al.
FEBS JOURNAL (2015)
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Alexis Rohou et al.
JOURNAL OF STRUCTURAL BIOLOGY (2015)
Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
Jianhua Zhao et al.
NATURE (2015)
Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase
Matteo Allegretti et al.
NATURE (2015)
Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution
Edgar Morales-Rios et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2015)
Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
Anna Zhou et al.
ELIFE (2015)
Sampling the conformational space of the catalytic subunit of human γ-secretase
Xiao-chen Bai et al.
ELIFE (2015)
Rotary ATPases - dynamic molecular machines
Alastair G. Stewart et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2014)
Quantifying the local resolution of cryo-EMEM density maps
Alp Kucukelbir et al.
NATURE METHODS (2014)
ATP Synthase: A Molecular Therapeutic Drug Target for Antimicrobial and Antitumor Peptides
Zulfiqar Ahmad et al.
CURRENT MEDICINAL CHEMISTRY (2013)
Operation mechanism of FoF1-adenosine triphosphate synthase revealed by its structure and dynamics
Ryota Iino et al.
IUBMB LIFE (2013)
Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
Xueming Li et al.
NATURE METHODS (2013)
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Sjors H. W. Scheres
JOURNAL OF STRUCTURAL BIOLOGY (2012)
Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation
Jindrich Symersky et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2012)
Priming a Molecular Motor for Disassembly
Alastair G. Stewart et al.
STRUCTURE (2012)
The dynamic stator stalk of rotary ATPases
Alastair G. Stewart et al.
NATURE COMMUNICATIONS (2012)
REFMAC5 for the refinement of macromolecular crystal structures
Garib N. Murshudov et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2011)
Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an autoinhibited conformation
Gino Cingolani et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2011)
Features and development of Coot
P. Emsley et al.
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (2010)
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Paul D. Adams et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2010)
Essential arginine residue of the F0-a subunit in F0F1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the F0 proton channel
Noriyo Mitome et al.
BIOCHEMICAL JOURNAL (2010)
Direct observation of stepped proteolipid ring rotation in E. coli FoF1-ATP synthase
Robert Ishmukhametov et al.
EMBO JOURNAL (2010)
Microscopic rotary mechanism of ion translocation in the F0 complex of ATP synthases
Denys Pogoryelov et al.
NATURE CHEMICAL BIOLOGY (2010)
The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase
Lawrence K. Lee et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2010)
Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
Ian N. Watt et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
36° step size of proton-driven c-ring rotation in FoF1-ATP synthase
Monika G. Dueser et al.
EMBO JOURNAL (2009)
Solution Structure, Determined by Nuclear Magnetic Resonance, of the b30-82 Domain of Subunit b of Escherichia coli F1Fo ATP Synthase
Ragunathan Priya et al.
JOURNAL OF BACTERIOLOGY (2009)
Constant c10 Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking
Britta Ballhausen et al.
JOURNAL OF BACTERIOLOGY (2009)
Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators
Hiromi Imamura et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Unique rotary ATP synthase and its biological diversity
Christoph von Ballmoos et al.
ANNUAL REVIEW OF BIOPHYSICS (2008)
ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase
Robert R. Ishmukhametov et al.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2008)
The barg36 contributes to efficient coupling in F1FO ATP synthase in Escherichia coli
Amanda K. Welch et al.
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES (2008)
Subunit a facilitates aqueous access to a membrane-embedded region of subunit C in Escherichia coli F1F0 ATP synthase
P. Ryan Steed et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Structural Interactions between Transmembrane Helices 4 and 5 of Subunit a and the Subunit c Ring of Escherichia coli ATP Synthase
Kyle J. Moore et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15
Denys Pogoryelov et al.
JOURNAL OF BACTERIOLOGY (2007)
Structures of the thermophilic F1-ATPase ε subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1
Hiromasa Yagi et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2007)
Phospholipids occupy the internal lumen of the c ring of the ATP synthase of Escherichia coli
B Oberfeld et al.
BIOCHEMISTRY (2006)
Structural characterization of the interaction of the δ and α subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy
S Wilkens et al.
BIOCHEMISTRY (2005)
Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an α-subunit
RJ Carbajo et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1F0 ATP synthase
RR Ishmukhametov et al.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2005)
Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase
A Aksimentiev et al.
BIOPHYSICAL JOURNAL (2004)
Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane
CM Angevine et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2003)
Purification and biochemical characterization of the F1FO-ATP synthase from thermoalkaliphilic Bacillus sp strain TA2.A1
GM Cook et al.
JOURNAL OF BACTERIOLOGY (2003)
Aqueous access channels in subunit a of rotary ATP synthase
CM Angevine et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
The second stalk of Escherichia coli ATP synthase:: structure of the isolated dimerization domain
PA Del Rizzo et al.
BIOCHEMISTRY (2002)
ATP synthase - A marvellous rotary engine of the cell
M Yoshida et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2001)
The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
WP Jiang et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2001)
Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase:: Influence of the Fo sector and ε subunit on the catalytic transition state
YB Peskova et al.
BIOCHEMISTRY (2000)
A rotary molecular motor that can work at near 100% efficiency
K Kinosita et al.
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES (2000)
Observations of rotation within the FOFl-ATP synthase:: deciding between rotation of the FOc subunit ring and artifact
SP Tsunoda et al.
FEBS LETTERS (2000)
分享论文
