(Q42247779)

English

Kinetics of interaction of adenosine diphosphate and adenosine triphosphate with adenosine triphosphatase of bovine heart submitochondrial particles

scientific article published on June 1980

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

Kinetics of interaction of adenosine diphosphate and adenosine triphosphate with adenosine triphosphatase of bovine heart submitochondrial particles (English)

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

adenosine triphosphate

0 references

author name string

Vasilyeva EA

1

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

Fitin AF

2

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

Minkov IB

3

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

Vinogradov AD

4

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

language of work or name

0 references

publication date

1 June 1980

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

Biochemical Journal

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

188

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

3

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

807-815

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble dinitrophenol-stimulated adenosine triphosphatase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Formation constants for the complexes of adenosine di- or tri-phosphate with magnesium or calcium ions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Preparation and general properties of a soluble adenosine triphosphatase from mitochondria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

The protonmotive force in bovine heart submitochondrial particles. Magnitude, sites of generation and comparison with the phosphorylation potential

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Mg2+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

A thermodynamic analysis of the interaction between the mitochondrial coupling adenosine triphosphatase and its naturally occurring inhibitor protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Specificity of nucleotide binding and coupled reactions utilising the mitochondrial ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Tightly-bound ATP and ADP in reconstituted submitochondrial particles

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

The interactions of coupling ATPases with nucleotides

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Tightly bound nucleotides of the energy-transducing ATPase, and their role in oxidative phosphorylation. II. The beef heart mitochondrial system

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Removal of "tightly bound" nucleotides from phosphorylating submitochondrial particles

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Kinetic studies on rat liver and beef heart mitochondrial ATPase. Evidence for nucleotide binding at separate regulatory and catalytic sites

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Interaction of adenine nucleotides with multiple binding sites on beef heart mitochondrial adenosine triphosphatase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Active/inactive state transitions of mitochondrial ATPase molecules influenced by Mg2+ , anions and aurovertin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Nucleotide-binding properties of native and cold-treated mitochondrial ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

26 October 2017

Steady state kinetics of soluble and membrane-bound mitochondrial ATPase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

29 May 2018

Respiration-driven proton transport in submitochondrial particles.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1161965

29 May 2018

Partial resolution of the enzymes catalyzing oxidative phosphorylation. IV. Formation of a complex between coupling factor 1 and adenosine diphosphate and its relation to the 14C-adenosine diphosphate-adenosine triphosphate exchange reaction

1 reference

https://pubmed.ncbi.nlm.nih.gov/6451217

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Partial resolution of the enzymes catalyzing oxidative phosphorylation. 13. Structure and function of submitochondrial particles completely resolved with respect to coupling factor

1 reference

https://pubmed.ncbi.nlm.nih.gov/6451217

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Adenosine triphosphatase from rat liver mitochondria. II. Interaction with adenosine diphosphate

1 reference

https://pubmed.ncbi.nlm.nih.gov/6451217

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Equilibrium binding of nucleotides to beef heart mitochondrial adenosine triphosphatase

1 reference

https://pubmed.ncbi.nlm.nih.gov/6451217

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Tight binding of adenine nucleotides to beef-heart mitochondrial ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/6451217

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Partial resolution of the enzymes catalyzing oxidative phosphorylation. II. Participation of a soluble adenosine tolphosphatase in oxidative phosphorylation

1 reference

https://pubmed.ncbi.nlm.nih.gov/6451217

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

RESTORATION OF OXIDATIVE PHOSPHORYLATION IN NON-PHOSPHORYLATING SUBMITOCHONDRIAL PARTICLES BY OLIGOMYCIN

1 reference

https://pubmed.ncbi.nlm.nih.gov/6451217

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/BJ1880807

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

19 October 2017

ResearchGate publication ID

0 references

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