Monoclonal antibodies to mitochondrial F1-ATPase and oligomycin sensitivity conferring protein (OSCP). Tools for recognition of well conserved and essential antigenic sites

scientific article published on August 30, 1984

Monoclonal antibodies to mitochondrial F1-ATPase and oligomycin sensitivity conferring protein (OSCP). Tools for recognition of well conserved and essential antigenic sites is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/0006-291X(84)90406-6
P953full work available at URLhttps://api.elsevier.com/content/article/PII:0006291X84904066?httpAccept=text/plain
https://api.elsevier.com/content/article/PII:0006291X84904066?httpAccept=text/xml
P698PubMed publication ID6206858

P2093author name stringC. Godinot
D. C. Gautheron
P. Archinard
M. Moradi-Améli
P2860cites workProtein measurement with the Folin phenol reagentQ20900776
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Q25938983
Continuous cultures of fused cells secreting antibody of predefined specificityQ26776979
Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-SepharoseQ39218339
49 Oligomycin-sensitivity-conferring proteinQ39888355
Optimization of the purification of mitochondrial F1-adenosine triphosphataseQ39895471
The Proton-Translocating Pumps of Oxidative PhosphorylationQ40098476
The proton-ATPase of bacteria and mitochondriaQ40107164
Purification of pig heart mitochondrial membranes. Enzymatic and morphological characterization as compared to microsomes.Q52473994
[Regulation of the respiratory activity of pig heart mitochondria and the transformation of the adenylic nucleotides and of phosphate].Q54404399
Studies on the mitochondrial adenosine triphosphatase system. IV. Purification and characterization of the oligomycin sensitivity conferring proteinQ68420770
"Hysteric" behavior and nucleotide binding sites of pig heart mitochondrial F1 adenosine 5'-triphosphataseQ70538860
Correlations between ATP hydrolysis, ATP synthesis, generation and utilization of ΔpH in mitochondrial ATPase-ATP synthaseQ72719754
Subunit equivalence in Escherichia coli and bovine heart mitochondrial F1F0 ATPasesQ72769420
Use of trypsin to monitor conformational changes of mitochondrial adenosine triphosphatase induced by nucleotides and phosphateQ72781587
Amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria and its homology with the δ-subunit of the F1-ATPase ofEscherichia coliQ72804775
Vesicular preparation of a highly coupled ATPase-ATP synthase complex from pig heart mitochondriaQ72922501
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
biophysicsQ7100
cell biologyQ7141
P304page(s)254-261
P577publication date1984-08-01
1984-08-30
P1433published inBiochemical and Biophysical Research CommunicationsQ864228
P1476titleMonoclonal antibodies to mitochondrial F1-ATPase and oligomycin sensitivity conferring protein (OSCP). Tools for recognition of well conserved and essential antigenic sites
P478volume123

Reverse relations

cites work (P2860)
Q36239807Antibody-based approaches to diagnosis and characterization of oxidative phosphorylation diseases
Q38197240Evidence from immunological studies of structure-mechanism relationship of F1 and F1F0.
Q69057196Exploration of delta-subunit interactions in beef heart mitochondrial F1-ATPase by monoclonal antibodies
Q42004437Localization on the mitochondrial F1 ATPase alpha subunit of an epitope masked in the membrane-bound enzyme using a monoclonal antibody and synthetic peptides
Q43713922Mitochondrial ATPase and high-energy phosphates in failing hearts
Q69131475Monoclonal antibodies to F1-ATPase subunits as probes of structure, conformation, and functions of isolated or membrane-bound F1
Q39459806Structure and function of the ATPase-ATP synthase complex of mitochondria as compared to chloroplasts and bacteria
Q69933138Use of monoclonal antibodies to purify oligomycin sensitivity-conferring protein and to study its interactions with F0 and F1

Search more.