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Volumn 111, Issue 31, 2014, Pages 11305-11310

Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F1-ATPase

Author keywords

Binding site; Folding; Inhibitory path; Rotary catalysis

Indexed keywords

ADENOSINE TRIPHOSPHATE; INHIBITOR PROTEIN; MITOCHONDRIAL INHIBITOR PROTEIN IF 1; MITOCHONDRIAL PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84905662028     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1411560111     Document Type: Article
Times cited : (76)

References (34)
  • 1
    • 0000228422 scopus 로고
    • A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity
    • Pullman ME, Monroy GC (1963) A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity. J Biol Chem 238:3762-3769.
    • (1963) J Biol Chem , vol.238 , pp. 3762-3769
    • Pullman, M.E.1    Monroy, G.C.2
  • 2
    • 84877759621 scopus 로고    scopus 로고
    • The affinity purification and characterization of ATP synthase complexes from mitochondria
    • Runswick MJ, et al. (2013) The affinity purification and characterization of ATP synthase complexes from mitochondria. Open Biol 3(2):120160.
    • (2013) Open Biol , vol.3 , Issue.2 , pp. 120160
    • Runswick, M.J.1
  • 3
    • 0023621390 scopus 로고
    • ATP synthase from bovine mitochondria: Sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6, and adenosinetriphosphatase inhibitor protein
    • Walker JE, Gay NJ, Powell SJ, Kostina M, Dyer MR (1987) ATP synthase from bovine mitochondria: Sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6, and adenosinetriphosphatase inhibitor protein. Biochemistry 26(26):8613-8619. (Pubitemid 18040787)
    • (1987) Biochemistry , vol.26 , Issue.26 , pp. 8613-8619
    • Walker, J.E.1    Gay, N.J.2    Powell, S.J.3    Kostina, M.4    Dyer, M.R.5
  • 10
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6(3):197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: Implications for structural proteomics
    • DOI 10.1016/j.str.2003.10.002
    • Linding R, et al. (2003) Protein disorder prediction: Implications for structural proteomics. Structure 11(11):1453-1459. (Pubitemid 37412427)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3    Bork, P.4    Gibson, T.J.5    Russell, R.B.6
  • 15
    • 34547135425 scopus 로고    scopus 로고
    • Insight into the bind-lock mechanism of the yeast mitochondrial ATP synthase inhibitory peptide
    • DOI 10.1021/bi700522v
    • Corvest V, Sigalat C, Haraux F (2007) Insight into the bind-lock mechanism of the yeast mitochondrial ATP synthase inhibitory peptide. Biochemistry 46(29):8680-8688. (Pubitemid 47106118)
    • (2007) Biochemistry , vol.46 , Issue.29 , pp. 8680-8688
    • Corvest, V.1    Sigalat, C.2    Haraux, F.3
  • 16
    • 47749083052 scopus 로고    scopus 로고
    • From the first protein structures to our current knowledge of protein folding: Delights and scepticisms
    • Fersht AR (2008) From the first protein structures to our current knowledge of protein folding: Delights and scepticisms. Nat Rev Mol Cell Biol 9(8):650-654.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.8 , pp. 650-654
    • Fersht, A.R.1
  • 17
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • DOI 10.1038/nrm1126
    • Daggett V, Fersht A (2003) The present view of the mechanism of protein folding. Nat Rev Mol Cell Biol 4(6):497-502. (Pubitemid 36648595)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.6 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 18
    • 27144532135 scopus 로고    scopus 로고
    • Solution structure of a protein denatured state and folding intermediate
    • DOI 10.1038/nature04054, PII N04054
    • Religa TL, Markson JS, Mayor U, Freund SM, Fersht AR (2005) Solution structure of a protein denatured state and folding intermediate. Nature 437(7061):1053-1056. (Pubitemid 41486989)
    • (2005) Nature , vol.437 , Issue.7061 , pp. 1053-1056
    • Religa, T.L.1    Markson, J.S.2    Mayor, U.3    Freund, S.M.V.4    Fersht, A.R.5
  • 19
    • 84861562196 scopus 로고    scopus 로고
    • 1, to ATP homeostasis, cell growth, mitochondrial morphology, and cell viability
    • 1, to ATP homeostasis, cell growth, mitochondrial morphology, and cell viability. J Biol Chem 287(22):18781-18787.
    • (2012) J Biol Chem , vol.287 , Issue.22 , pp. 18781-18787
    • Fujikawa, M.1    Imamura, H.2    Nakamura, J.3    Yoshida, M.4
  • 20
    • 84884849570 scopus 로고    scopus 로고
    • 1, a natural inhibitor of mitochondrial ATP synthase, is not essential for the normal growth and breeding of mice
    • 1, a natural inhibitor of mitochondrial ATP synthase, is not essential for the normal growth and breeding of mice. Biosci Rep 33(5):33.
    • (2013) Biosci Rep , vol.33 , Issue.5 , pp. 33
    • Nakamura, J.1    Fujikawa, M.2    Yoshida, M.3
  • 22
    • 77955483825 scopus 로고    scopus 로고
    • +-ATP synthase in human tumors mediates the metabolic shift of cancer cells to a Warburg phenotype
    • +-ATP synthase in human tumors mediates the metabolic shift of cancer cells to a Warburg phenotype. J Biol Chem 285(33):25308-25313.
    • (2010) J Biol Chem , vol.285 , Issue.33 , pp. 25308-25313
    • Sánchez-Cenizo, L.1
  • 23
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • DOI 10.1002/jmr.747
    • Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18(5):343-384. (Pubitemid 41341287)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.5 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 24
    • 84866463338 scopus 로고    scopus 로고
    • Structural biology. Versatility from protein disorder
    • Babu MM, Kriwacki RW, Pappu RV (2012) Structural biology. Versatility from protein disorder. Science 337(6101):1460-1461.
    • (2012) Science , vol.337 , Issue.6101 , pp. 1460-1461
    • Babu, M.M.1    Kriwacki, R.W.2    Pappu, R.V.3
  • 31
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov GN, et al. (2011) REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67(Pt 4):355-367.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , Issue.PART 4 , pp. 355-367
    • Murshudov, G.N.1
  • 32
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 1 , pp. 12-21
    • Chen, V.B.1
  • 34
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372(3):774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


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