(Q24676255)

English

Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes

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scholarly article

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Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes (English)

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Euclidean geometry

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based on heuristic

inferred from title

author name string

T Izard

1

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A Aevarsson

2

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M D Allen

3

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A H Westphal

4

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R N Perham

5

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A de Kok

6

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W G Hol

7

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language of work or name

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publication date

16 February 1999

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Proceedings of the National Academy of Sciences of the United States of America

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96

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1240-5

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4

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Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)

1 reference

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7 April 2017

The CCP4 suite: programs for protein crystallography

1 reference

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7 April 2017

Raster3D Version 2.0. A program for photorealistic molecular graphics

1 reference

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Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

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7 April 2017

On the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complex

1 reference

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Physical Principles in the Construction of Regular Viruses

1 reference

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Structure-function relationships in dihydrolipoamide acyltransferases

1 reference

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7 April 2017

Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein

1 reference

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7 April 2017

Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex

1 reference

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7 April 2017

Purification of the pyruvate dehydrogenase multienzyme complex of Zymomonas mobilis and identification and sequence analysis of the corresponding genes.

1 reference

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28 September 2017

Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 A resolution

1 reference

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Three-dimensional structure of the truncated core of the Saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images

1 reference

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2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain.

1 reference

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Improvement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals

1 reference

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Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus

1 reference

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Isolation and characterisation of the pyruvate dehydrogenase complex of anaerobically grown Enterococcus faecalis NCTC 775

1 reference

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30 May 2018

Conformational studies of the interdomain linker peptides in the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

1 reference

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Structure and symmetry of B. stearothermophilus pyruvate dehydrogenase multienzyme complex and implications for eucaryote evolution

1 reference

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30 May 2018

The catalytic domain of dihydrolipoyl acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Expression, purification and reversible denaturation.

1 reference

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21 January 2018

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1 reference

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The pyruvate dehydrogenase multienzyme complex

1 reference

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Two lipoyl domains in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase multienzyme complex of Streptococcus faecalis

1 reference

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21 January 2018

The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis

1 reference

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21 January 2018

Heavy riboflavin synthase from Bacillus subtilis. Crystal structure analysis of the icosahedral beta 60 capsid at 3.3 A resolution

1 reference

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21 January 2018

Identifiers

10.1073/PNAS.96.4.1240

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1999PNAS...96.1240I

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OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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