(Q72389876)

English

A phenylalanine for serine substitution in the beta subunit of Escherichia coli F1-ATPase affects dependence of its activity on divalent cations

scientific article published on August 25, 1984

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scholarly article

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Europe PubMed Central

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26 October 2019

A phenylalanine for serine substitution in the beta subunit of Escherichia coli F1-ATPase affects dependence of its activity on divalent cations (English)

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26 October 2019

Escherichia coli

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bacterial genes

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2 August 2023

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10.1016/S0021-9258(18)90929-4

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2 August 2023

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2 August 2023

author name string

T. Noumi

1

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2 August 2023

M. E. Mosher

2

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2 August 2023

S. Natori

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2 August 2023

M. Futai

4

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2 August 2023

H. Kanazawa

5

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2 August 2023

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1 August 1984

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26 October 2019

25 August 1984

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National Center for Biotechnology Information

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2 August 2023

full work available at URL

http://intl.jbc.org/cgi/content/abstract/259/16/10071

online access status

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2 August 2023

https://api.elsevier.com/content/article/PII:S0021925818909294?httpAccept=text/xml

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10.1016/S0021-9258(18)90929-4

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2 August 2023

https://api.elsevier.com/content/article/PII:S0021925818909294?httpAccept=text/plain

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2 August 2023

Journal of Biological Chemistry

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26 October 2019

259

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26 October 2019

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26 October 2019

10071-10075

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6088479%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

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2

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Affinity labeling of purified Ca2+,Mg2+-activated ATPase of Escherichia coli by the 2',3'-dialdehydes of adenosine 5'-di- and triphosphates

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Identification of Amino-Acid Substitutions in the Proteolipid Subunit of the ATP Synthase from Dicyclohexylcarbodiimide-Resistant Mutants of Escherichia coli

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An Asp—Asn substitution in the proteolipid subnit of the ATP‐synthase from Escherichia coli leads to a non‐functional proton channel

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Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-binding protein and the α subunit of proton-translocating ATPase of Escherichia coli

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Nucleotide sequence of the gene coding for the delta subunit of proton translocating ATPase of Escherichia coli.

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Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli.

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Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from : Prediction of the primary structure of F0 subunits

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Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coli

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The atp operon: nucleotide sequence of the region encoding the α-subunit of Escherichia coli ATP-synthase

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The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase

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The atp operon: nucleotide sequence of the genes for the γ, β, and ε subunits of Escherichia coli ATP synthase

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The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit δ of the membrane bound ATP synthase of Escherichia coli

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Escherichia coli mutants defective in the γ subunit of proton-translocating ATPase: Intracistronic mapping of the defective site and the biochemical properties of the mutants

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Intracistronic mapping of the defective site and the biochemical properties of β subunit mutants of Escherichia coli H+-ATPase: Correlation of structural domains with functions of the β subunit

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PubMed publication ID

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6088479%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

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