Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
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Title
Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
Authors
Keywords
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Journal
Nature Communications
Volume 12, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2021-09-06
DOI
10.1038/s41467-021-25570-y
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Note: Only part of the references are listed.- Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex
- (2020) B. O. Forsberg et al. Nature Communications
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- (2019) Sabin Prajapati et al. STRUCTURE
- The EMBL-EBI search and sequence analysis tools APIs in 2019
- (2019) Fábio Madeira et al. NUCLEIC ACIDS RESEARCH
- Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
- (2019) Dorothee Liebschner et al. Acta Crystallographica Section D-Structural Biology
- Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant
- (2019) Babak Andi et al. Acta Crystallographica Section F-Structural Biology Communications
- DALI and the persistence of protein shape
- (2019) Liisa Holm PROTEIN SCIENCE
- Atomic Structure of the E2 Inner Core of Human Pyruvate Dehydrogenase Complex
- (2018) Jiansen Jiang et al. BIOCHEMISTRY
- Instant Clue: A Software Suite for Interactive Data Visualization and Analysis
- (2018) Hendrik Nolte et al. Scientific Reports
- Role of the Pyruvate Dehydrogenase Complex in Metabolic Remodeling: Differential Pyruvate Dehydrogenase Complex Functions in Metabolism
- (2018) Sungmi Park et al. Diabetes & Metabolism Journal
- UniProt: a worldwide hub of protein knowledge
- (2018) NUCLEIC ACIDS RESEARCH
- cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
- (2017) Ali Punjani et al. NATURE METHODS
- Alignment of cryo-EM movies of individual particles by optimization of image translations
- (2015) John L. Rubinstein et al. JOURNAL OF STRUCTURAL BIOLOGY
- Collaborative Computational Project for Electron cryo-Microscopy
- (2015) Chris Wood et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Why are the 2-oxoacid dehydrogenase complexes so large? Generation of an active trimeric complex
- (2014) Nia L. Marrott et al. BIOCHEMICAL JOURNAL
- Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from theEscherichia coliPyruvate Dehydrogenase Multienzyme Complex
- (2014) Palaniappa Arjunan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The Pyruvate Dehydrogenase Complexes: Structure-based Function and Regulation
- (2014) Mulchand S. Patel et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component inEscherichia coliPyruvate Dehydrogenase Complex
- (2014) Junjie Wang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The novel component Kgd4 recruits the E3 subunit to the mitochondrial α-ketoglutarate dehydrogenase
- (2014) Manfred Heublein et al. MOLECULAR BIOLOGY OF THE CELL
- Ultrasensitive proteome analysis using paramagnetic bead technology
- (2014) C. S. Hughes et al. Molecular Systems Biology
- Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in theEscherichia coliPyruvate Dehydrogenase Complex via Multifaceted Structural Approaches
- (2013) Krishnamoorthy Chandrasekhar et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Interchain Acetyl Transfer in the E2 Component of Bacterial Pyruvate Dehydrogenase Suggests a Model with Different Roles for Each Chain in a Trimer of the Homooligomeric Component
- (2012) Jaeyoung Song et al. BIOCHEMISTRY
- Prevention of overfitting in cryo-EM structure determination
- (2012) Sjors H W Scheres et al. NATURE METHODS
- The catalytic core of an archaeal 2-oxoacid dehydrogenase multienzyme complex is a 42-mer protein assembly
- (2011) Nia L. Marrott et al. FEBS Journal
- Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
- (2011) Jürgen Cox et al. JOURNAL OF PROTEOME RESEARCH
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Communication between Thiamin Cofactors in theEscherichia coliPyruvate Dehydrogenase Complex E1 Component Active Centers
- (2010) Natalia S. Nemeria et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Solution Structure and Characterisation of the Human Pyruvate Dehydrogenase Complex Core Assembly
- (2010) S. Vijayakrishnan et al. JOURNAL OF MOLECULAR BIOLOGY
- Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase
- (2010) James E. Knapp et al. PROTEIN SCIENCE
- MolProbity: all-atom structure validation for macromolecular crystallography
- (2009) Vincent B. Chen et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Structural and Functional Insights into the Molecular Mechanisms Responsible for the Regulation of Pyruvate Dehydrogenase Kinase 2
- (2008) Todd Green et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
- (2008) Jürgen Cox et al. NATURE BIOTECHNOLOGY
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- (2008) Xuekui Yu et al. STRUCTURE
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