ATP20/YPR020W Literature Guide Help

Other names published for ATP20: YPR020W

ATP20 - Function/Process (24)

ReferenceOther Genes Addressed
Davies KM, et al.  (2012) Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae. Proc Natl Acad Sci U S A 109(34):13602-7
Forster K, et al.  (2010) Proton transport coupled ATP synthesis by the purified yeast H(+)-ATP synthase in proteoliposomes. Biochim Biophys Acta 1797(11):1828-37
Ozalp VC, et al.  (2010) Time-resolved Measurements of Intracellular ATP in the Yeast Saccharomyces cerevisiae using a New Type of Nanobiosensor. J Biol Chem 285(48):37579-88
Wagner K, et al.  (2010) Stepwise assembly of dimeric F(1)F(o)-ATP synthase in mitochondria involves the small F(o)-subunits k and i. Mol Biol Cell 21(9):1494-504
Olsen LF, et al.  (2009) Regulation of glycolytic oscillations by mitochondrial and plasma membrane H+-ATPases. Biophys J 96(9):3850-61
Rabl R, et al.  (2009) Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g. J Cell Biol 185(6):1047-63
Wagner K, et al.  (2009) Mitochondrial F1Fo-ATP synthase: the small subunits e and g associate with monomeric complexes to trigger dimerization. J Mol Biol 392(4):855-61
Saddar S, et al.  (2008) The F1F0-ATP synthase complex influences the assembly state of the cytochrome bc1-cytochrome oxidase supercomplex and its association with the TIM23 machinery. J Biol Chem 283(11):6677-86
Wittig I, et al.  (2008) Characterization of domain interfaces in monomeric and dimeric ATP synthase. Mol Cell Proteomics 7(5):995-1004
Corvest V, et al.  (2007) Insight into the bind-lock mechanism of the yeast mitochondrial ATP synthase inhibitory Peptide. Biochemistry 46(29):8680-8
Reinders J, et al.  (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
Zeng X, et al.  (2007) The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase. Mol Biol Cell 18(2):617-26
Bornhovd C, et al.  (2006) Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes. J Biol Chem 281(20):13990-8
Fronzes R, et al.  (2006) The peripheral stalk participates in the yeast ATP synthase dimerization independently of e and g subunits. Biochemistry 45(21):6715-23
Everard-Gigot V, et al.  (2005) Functional analysis of subunit e of the F1Fo-ATP synthase of the yeast Saccharomyces cerevisiae: importance of the N-terminal membrane anchor region. Eukaryot Cell 4(2):346-55
Arselin G, et al.  (2004) The modulation in subunits e and g amounts of yeast ATP synthase modifies mitochondrial cristae morphology. J Biol Chem 279(39):40392-9
Gavin PD, et al.  (2004) Cross-linking ATP synthase complexes in vivo eliminates mitochondrial cristae. J Cell Sci 117(Pt 11):2333-43
Giraud MF, et al.  (2002) Is there a relationship between the supramolecular organization of the mitochondrial ATP synthase and the formation of cristae? Biochim Biophys Acta 1555(1-3):174-80
Soubannier V, et al.  (2002) In the absence of the first membrane-spanning segment of subunit 4(b), the yeast ATP synthase is functional but does not dimerize or oligomerize. J Biol Chem 277(12):10739-45
Paumard P, et al.  (2000) Environmental study of subunit i, a F(o) component of the yeast ATP synthase. Biochemistry 39(14):4199-205
Velours J, et al.  (2000) Organisation of the yeast ATP synthase F(0):a study based on cysteine mutants, thiol modification and cross-linking reagents. Biochim Biophys Acta 1458(2-3):443-56
Boyle GM, et al.  (1999) Identification of subunit g of yeast mitochondrial F1F0-ATP synthase, a protein required for maximal activity of cytochrome c oxidase. Eur J Biochem 262(2):315-23
Arnold I, et al.  (1998) Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J 17(24):7170-8
Schatz G, et al.  (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation. XIV. J Biol Chem 242(10):2552-60