D. Mueller

发表

Mitochondrial Genome Integrity Mutations Uncouple the Yeast Saccharomyces cerevisiae ATP Synthase*

U. Singh, Yamin Wang, D. Mueller, 2007, Journal of Biological Chemistry.

Partially Redundant Actin Genes in Chlamydomonas Control Transition Zone Organization and Flagellum-Directed Traffic

P. Avasthi, Ashley L. Tetlow, D. Mueller, 2019, Cell reports.

Partially redundant actin genes in Chlamydomonas control flagellum-directed traffic and transition zone organization

P. Avasthi, Ashley L. Tetlow, D. Mueller, 2018, bioRxiv.

The subcellular location of the yeast Saccharomyces cerevisiae homologue of the protein defective in the juvenile form of Batten disease.

H. C. Choi, D. Mueller, J. B. Croopnick, 1998, Biochemical and biophysical research communications.

A candidate multi-epitope vaccine against SARS-CoV-2

F. Castiglione, Debashrito Deb, D. Mueller, 2020, Scientific Reports.

Bedaquiline inhibits the yeast and human mitochondrial ATP synthases

J. Symerský, M. Liao, J. Faraldo-Gómez, 2020, Communications Biology.

Site directed mutagenesis of the β-subunit of the yeast mitochondrial ATPase

D. Mueller, 1989 .

A candidate multi-epitope vaccine against SARS-CoV-2

F. Castiglione, Debashrito Deb, D. Mueller, 2020, Scientific Reports.

Early onset severe ATP1A2 epileptic encephalopathy: Clinical characteristics and underlying mutations

V. Shashi, M. McDonald, J. Jasien, 2021, Epilepsy & Behavior.

Chlamydomonas reinhardtii formin FOR1 and profilin PRF1 are optimized for acute rapid actin filament assembly

L. Mets, Shengping Huang, P. Avasthi, 2016, bioRxiv.

The structure of F 1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF 1

A. Leslie, John V. Bason, M. G. Montgomery, 2013 .

Temperature sensitive pet mutants in yeast Saccharomyces cerevisiae that lose mitochondrial RNA

G. Getz, M. Rabinowitz, J. Edwards, 2004, Current Genetics.

Complementation of deletion mutants in the genes encoding the F1-ATPase by expression of the corresponding bovine subunits in yeast S. cerevisiae.

D. Mueller, J. Lai‐Zhang, 2000, European journal of biochemistry.

Epistatic interactions of deletion mutants in the genes encoding the F1‐ATPase in yeast Saccharomyces cerevisiae

Yan Xiao, D. Mueller, J. Lai‐Zhang, 1999, The EMBO journal.

The elusive actin cytoskeleton of a green alga expressing both conventional and divergent actins

B. Engel, P. Avasthi, M. Schaffer, 2019, bioRxiv.

High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane

J. Symerský, M. Liao, J. Faraldo-Gómez, 2018, Science.

Introduction of the Chloroplast Redox Regulatory Region in the Yeast ATP Synthase Impairs Cytochrome c Oxidase*

D. Walters, D. Mueller, Hong-Der Shen, 2008, Journal of Biological Chemistry.

Crystallization and preliminary crystallographic studies of the mitochondrial F1-ATPase from the yeast Saccharomyces cerevisiae.

A. Leslie, V. Kabaleeswaran, N. Puri, 2004, Acta crystallographica. Section D, Biological crystallography.

Bovine Coupling Factor 6, with Just 14.5% Shared Identity, Replaces Subunit h in the Yeast ATP Synthase*

P. Paumard, J. Velours, V. Soubannier, 2001, The Journal of Biological Chemistry.

Level of ATP synthase activity required for yeast Saccharomyces cerevisiae to grow on glycerol media

Arindam Mukhopadhyay, M. Uh, D. Mueller, 1994, FEBS letters.

Steady state analysis of mitochondrial RNA after growth of yeast Saccharomyces cerevisiae under catabolite repression and derepression.

G. Getz, D. Mueller, 1986, The Journal of biological chemistry.

TNK2/ACK1-mediated phosphorylation of ATP5F1A (ATP synthase F1 subunit alpha) selectively augments survival of prostate cancer while engendering mitochondrial vulnerability

N. Mahajan, H. Earp, M. Terrado, 2022, Autophagy.

Photoaffinity labelling of submitochondrial membranes with the 3-azido analogue of 9-amino-3-chloro-7-methoxyacridine.

C. Lee, D. Mueller, S. Kopacz, 1985, Biochimica et biophysica acta.

Partial Uncoupling of the Mitochondrial Membrane by a Heterozygous Null Mutation in the Gene Encoding the γ- or δ-Subunit of the Yeast Mitochondrial ATPase*

Yan Xiao, D. Mueller, M. Metzl, 2000, The Journal of Biological Chemistry.

The Role of the Amino-Terminal β-Barrel Domain of the α and β Subunits in the Yeast F1-ATPase

D. Mueller, B. Yao, 1999 .

Increased expression of F1ATP synthase subunits in yeast strains carrying point mutations which destabilise the β subunit

R. Wiesner, R. Zak, D. Mueller, 1993 .

Heterologous expression, purification, and biochemistry of the oligomycin sensitivity conferring protein (OSCP) from yeast.

M. Uh, D. Mueller, A. Mukhopadhyay, 1992, The Journal of biological chemistry.

The ATP synthase is involved in generating mitochondrial cristae morphology

J. di Rago, P. Paumard, J. Velours, 2002, The EMBO journal.

The pathogenic m.8993 T > G mutation in mitochondrial ATP6 gene prevents proton release from the subunit c-ring rotor of ATP synthase.

R. Kucharczyk, Nahia Ezkurdia, J. di Rago, 2021, Human molecular genetics.

Structure of the c10 Ring of the Yeast Mitochondrial ATP Synthase in the Open Conformation

J. Symerský, J. Faraldo-Gómez, A. Krah, 2012, Nature Structural &Molecular Biology.

A candidate multi-epitope vaccine against SARS-CoV-2

F. Castiglione, Debashrito Deb, D. Mueller, 2020, Scientific Reports.

Oligomycin frames a common drug-binding site in the ATP synthase

J. Symerský, D. Walters, D. Mueller, 2012, Proceedings of the National Academy of Sciences.

Partially redundant actin genes in Chlamydomonas control transition zone and flagellum-directed protein dynamics.

P. Avasthi, Ashley L. Tetlow, D. Mueller, 2018 .

Steps and bumps: precision extraction of discrete states of molecular machines.

Max A. Little, Fan Bai, Max A Little, 2010, Biophysical journal.

Targeted exome sequencing of suspected mitochondrial disorders

V. Mootha, J. Schmahmann, Shangtao Liu, 2013, Neurology.

Targeted exome sequencing of suspected mitochondrial disorders April

V. Mootha, D. Thorburn, K. Sims, 2013 .

Synonymous codon usage affects the expression of wild type and F508del CFTR.

N. Bradbury, R. Bridges, D. Mueller, 2015, Journal of molecular biology.

The Binding Mechanism of the Yeast F1-ATPase Inhibitory Peptide

F. Haraux, P. Falson, D. Mueller, 2005, Journal of Biological Chemistry.

Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides*

David M Mueller, A. Leslie, J. Symerský, 2009, Journal of Biological Chemistry.

Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase

A. Leslie, V. Kabaleeswaran, N. Puri, 2006, The EMBO journal.

Understanding structure, function, and mutations in the mitochondrial ATP synthase

Ting Xu, D. Mueller, V. Pagadala, 2015, Microbial cell.

Intragenic Suppressors of P-loop Mutations in the -Subunit of the Mitochondrial ATPase in the Yeast Saccharomyces cerevisiae(*)

A. Sosa-Peinado, D. Mueller, Honggang Shen, 1996, The Journal of Biological Chemistry.

ATPase kinetics for wild-type Saccharomyces cerevisiae F1-ATPase and F1-ATPase with the beta-subunit Thr197-->Ser mutation.

D. Mueller, L. McGill, V. Indyk, 1994, European journal of biochemistry.

Comparison between single-molecule and X-ray crystallography data on yeast F1-ATPase

Ashley L. Nord, R. Berry, B. Steel, 2015, Scientific Reports.

2015A Xu Microbial Cell

Ting Xu, D. Mueller, V. Pagadala, 2015 .

The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1

A. Leslie, John V. Bason, M. G. Montgomery, 2013, Open Biology.

Characterization of the mitochondrial ATP synthase from yeast Saccharomyces cerevisae

J. Symerský, Luke F Vistain, D. Mueller, 2011, Journal of bioenergetics and biomembranes.

Crystal Structures of Mutant Forms of the Yeast F1 ATPase Reveal Two Modes of Uncoupling*

J. Symerský, D. Arsenieva, Yamin Wang, 2010, The Journal of Biological Chemistry.

Expression of Bovine F1-ATPase with Functional Complementation in Yeast Saccharomyces cerevisiae*

N. Puri, D. Mueller, S. Meier, 2005, Journal of Biological Chemistry.

Ni-chelate-affinity purification and crystallization of the yeast mitochondrial F1-ATPase.

A. Leslie, V. Kabaleeswaran, N. Puri, 2004, Protein expression and purification.

Structure/Function of the β-Barrel Domain of F1-ATPase in the Yeast Saccharomyces cerevisiae *

D. Mueller, J. Lai‐Zhang, B. Yao, 1999, The Journal of Biological Chemistry.

Primary structural constraints of P-loop of mitochondrial F1-ATPase from yeast.

D. Mueller, H. Shen, B. Yao, 1994, The Journal of biological chemistry.

The sequence of the yeast ATP5 gene.

D. Jones, D. Mueller, M. Lee, 1988, Nucleic acids research.

Pigment epithelium‐derived factor binds to cell‐surface F1‐ATP synthase

L. Notari, N. Arakaki, S. Becerra, 2010, The FEBS journal.

The gene coding for the yeast oligomycin sensitivity-conferring protein.

D. Jones, M. Uh, D. Mueller, 1990, The Journal of biological chemistry.

D-DEMØ, a distinct phenotype caused by ATP1A3 mutations

R. Schiffmann, E. Heinzen, V. Shashi, 2020, Neurology: Genetics.

Transcriptional regulation of the mitochondrial genome of yeast Saccharomyces cerevisiae.

G. Getz, D. Mueller, 1986, The Journal of biological chemistry.

Identification of a single transcriptional initiation site for the glutamic tRNA and COB genes in yeast mitochondria.

M. Rabinowitz, T. Christianson, J. Edwards, 1983, Proceedings of the National Academy of Sciences of the United States of America.

An azido analogue of quinacrine: its synthesis and utilization as a photoaffinity probe with submitochondrial particles.

D. Mueller, C. Lee, R. A. Hudson, 1982, Biochemistry.

AZIDE PHOTOAFFINITY ANALOGS FOR ACRIDINE DYE BINDING SITES

D. Mueller, Chuan-pu Lee, R. A. Hudson, 1981 .

Arginine 328 of the beta-subunit of the mitochondrial ATPase in yeast is essential for protein stability.

D. Mueller, 1988, The Journal of biological chemistry.

Chlamydomonas reinhardtii formin FOR1 and profilin PRF1 are optimized for acute rapid actin filament assembly

L. Mets, Shengping Huang, P. Avasthi, 2019, Molecular biology of the cell.

Steps and bumps: precision extraction of discrete states of molecular machines.

Max A. Little, R. Berry, F. Bai, 2010, Biophysical journal.