메뉴 건너뛰기




Volumn 8, Issue 10, 2016, Pages 1032-1046

Mammalian Fe-S proteins: Definition of a consensus motif recognized by the co-chaperone HSC20

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALS; PROTEINS; SCAFFOLDS (BIOLOGY);

EID: 84991492609     PISSN: 17565901     EISSN: 1756591X     Source Type: Journal    
DOI: 10.1039/c6mt00167j     Document Type: Review
Times cited : (29)

References (163)
  • 1
    • 84978047747 scopus 로고    scopus 로고
    • Nitrogenases - A Tale of Carbon Atom(s)
    • Y. Hu M. W. Ribbe Nitrogenases - A Tale of Carbon Atom(s) Angew. Chem., Int. Ed. 2016 55 8216 8226
    • (2016) Angew. Chem., Int. Ed. , vol.55 , pp. 8216-8226
    • Hu, Y.1    Ribbe, M.W.2
  • 3
    • 0035834117 scopus 로고    scopus 로고
    • Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
    • C. L. Drennan J. Heo M. D. Sintchak E. Schreiter P. W. Ludden Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase Proc. Natl. Acad. Sci. U. S. A. 2001 98 11973 11978
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11973-11978
    • Drennan, C.L.1    Heo, J.2    Sintchak, M.D.3    Schreiter, E.4    Ludden, P.W.5
  • 4
    • 84930041923 scopus 로고    scopus 로고
    • A giant molecular proton pump: Structure and mechanism of respiratory complex i
    • L. A. Sazanov A giant molecular proton pump: structure and mechanism of respiratory complex I Nat. Rev. Mol. Cell Biol. 2015 16 375 388
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 375-388
    • Sazanov, L.A.1
  • 5
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • H. Beinert R. H. Holm E. Munck Iron-sulfur clusters: nature's modular, multipurpose structures Science 1997 277 653 659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 6
    • 3042779462 scopus 로고
    • A natural factor catalyzing reduction of methaemoglobin by isolated chloroplasts
    • H. E. Davenport R. Hill F. R. Whatley A natural factor catalyzing reduction of methaemoglobin by isolated chloroplasts Proc. R. Soc. London, Ser. B 1952 139 346 358
    • (1952) Proc. R. Soc. London, Ser. B , vol.139 , pp. 346-358
    • Davenport, H.E.1    Hill, R.2    Whatley, F.R.3
  • 7
    • 0001977469 scopus 로고
    • Studies on Succinic and Dpnh Dehydrogenase Preparations by Paramagnetic Resonance (Epr) Spectroscopy
    • H. Beinert R. H. Sands Studies on Succinic and Dpnh Dehydrogenase Preparations by Paramagnetic Resonance (Epr) Spectroscopy Biochem. Biophys. Res. Commun. 1960 3 41 46
    • (1960) Biochem. Biophys. Res. Commun. , vol.3 , pp. 41-46
    • Beinert, H.1    Sands, R.H.2
  • 8
    • 0002345887 scopus 로고
    • Studies on Mitochondria and Submitochondrial Particles by Paramagnetic Resonance (Epr) Spectroscopy
    • R. H. Sands H. Beinert Studies on Mitochondria and Submitochondrial Particles by Paramagnetic Resonance (Epr) Spectroscopy Biochem. Biophys. Res. Commun. 1960 3 47 52
    • (1960) Biochem. Biophys. Res. Commun. , vol.3 , pp. 47-52
    • Sands, R.H.1    Beinert, H.2
  • 10
    • 0027141376 scopus 로고
    • Aconitase, a two-faced protein: Enzyme and iron regulatory factor
    • H. Beinert M. C. Kennedy Aconitase, a two-faced protein: enzyme and iron regulatory factor FASEB J. 1993 7 1442 1449
    • (1993) FASEB J. , vol.7 , pp. 1442-1449
    • Beinert, H.1    Kennedy, M.C.2
  • 11
    • 0001531847 scopus 로고    scopus 로고
    • Iron-Sulfur Proteins with Non redox Functions
    • D. H. Flint R. M. Allen Iron-Sulfur Proteins with Non redox Functions Chem. Rev. 1996 96 2315 2334
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 12
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as Iron-Sulfur Protein, Enzyme, and Iron-Regulatory Protein
    • H. Beinert M. C. Kennedy C. D. Stout Aconitase as Iron-Sulfur Protein, Enzyme, and Iron-Regulatory Protein Chem. Rev. 1996 96 2335 2374
    • (1996) Chem. Rev. , vol.96 , pp. 2335-2374
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 13
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • T. A. Rouault The role of iron regulatory proteins in mammalian iron homeostasis and disease Nat. Chem. Biol. 2006 2 406 414
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 14
    • 39149112760 scopus 로고    scopus 로고
    • The functional duality of iron regulatory protein 1
    • K. Volz The functional duality of iron regulatory protein 1 Curr. Opin. Struct. Biol. 2008 18 106 111
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 106-111
    • Volz, K.1
  • 15
  • 16
    • 84974736098 scopus 로고    scopus 로고
    • Radical S -Adenosylmethionine Enzymes in Human Health and Disease
    • B. J. Landgraf E. L. McCarthy S. J. Booker Radical S -Adenosylmethionine Enzymes in Human Health and Disease Annu. Rev. Biochem. 2016 85 485 514
    • (2016) Annu. Rev. Biochem. , vol.85 , pp. 485-514
    • Landgraf, B.J.1    McCarthy, E.L.2    Booker, S.J.3
  • 17
    • 84857029886 scopus 로고    scopus 로고
    • Iron-sulphur clusters in nucleic acid processing enzymes
    • M. F. White M. S. Dillingham Iron-sulphur clusters in nucleic acid processing enzymes Curr. Opin. Struct. Biol. 2012 22 94 100
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 94-100
    • White, M.F.1    Dillingham, M.S.2
  • 19
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • J. Rudolf V. Makrantoni W. J. Ingledew M. J. Stark M. F. White The DNA repair helicases XPD and FancJ have essential iron-sulfur domains Mol. Cell 2006 23 801 808
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 20
    • 84945283339 scopus 로고    scopus 로고
    • How Is Fe-S Cluster Formation Regulated?
    • E. L. Mettert P. J. Kiley How Is Fe-S Cluster Formation Regulated? Annu. Rev. Microbiol. 2015 69 505 526
    • (2015) Annu. Rev. Microbiol. , vol.69 , pp. 505-526
    • Mettert, E.L.1    Kiley, P.J.2
  • 21
    • 84908097207 scopus 로고    scopus 로고
    • Iron-sulfur clusters as biological sensors: The chemistry of reactions with molecular oxygen and nitric oxide
    • J. C. Crack J. Green A. J. Thomson N. E. Le Brun Iron-sulfur clusters as biological sensors: the chemistry of reactions with molecular oxygen and nitric oxide Acc. Chem. Res. 2014 47 3196 3205
    • (2014) Acc. Chem. Res. , vol.47 , pp. 3196-3205
    • Crack, J.C.1    Green, J.2    Thomson, A.J.3    Le Brun, N.E.4
  • 23
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • L. Macomber J. A. Imlay The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity Proc. Natl. Acad. Sci. U. S. A. 2009 106 8344 8349
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8344-8349
    • MacOmber, L.1    Imlay, J.A.2
  • 24
    • 84935016527 scopus 로고    scopus 로고
    • Iron-sulfur proteins hiding in plain sight
    • T. A. Rouault Iron-sulfur proteins hiding in plain sight Nat. Chem. Biol. 2015 11 442 445
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 442-445
    • Rouault, T.A.1
  • 25
    • 66349089690 scopus 로고    scopus 로고
    • New pulsed EPR methods and their application to characterize mitochondrial complex i
    • T. Maly K. Zwicker A. Cernescu U. Brandt T. F. Prisner New pulsed EPR methods and their application to characterize mitochondrial complex I Biochim. Biophys. Acta 2009 1787 584 592
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 584-592
    • Maly, T.1    Zwicker, K.2    Cernescu, A.3    Brandt, U.4    Prisner, T.F.5
  • 27
    • 43149119755 scopus 로고    scopus 로고
    • X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi
    • A. Karcher A. Schele K. P. Hopfner X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi J. Biol. Chem. 2008 283 7962 7971
    • (2008) J. Biol. Chem. , vol.283 , pp. 7962-7971
    • Karcher, A.1    Schele, A.2    Hopfner, K.P.3
  • 31
    • 84856367380 scopus 로고    scopus 로고
    • Radical S -adenosylmethionine enzymes: Mechanism, control and function
    • M. R. Challand R. C. Driesener P. L. Roach Radical S -adenosylmethionine enzymes: mechanism, control and function Nat. Prod. Rep. 2011 28 1696 1721
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1696-1721
    • Challand, M.R.1    Driesener, R.C.2    Roach, P.L.3
  • 32
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • H. J. Sofia G. Chen B. G. Hetzler J. F. Reyes-Spindola N. E. Miller Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods Nucleic Acids Res. 2001 29 1097 1106
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 36
    • 84963667993 scopus 로고    scopus 로고
    • Exploiting Bacterial Operons to Illuminate Human Iron-Sulfur Proteins
    • C. Andreini L. Banci A. Rosato Exploiting Bacterial Operons To Illuminate Human Iron-Sulfur Proteins J. Proteome Res. 2016 15 1308 1322
    • (2016) J. Proteome Res. , vol.15 , pp. 1308-1322
    • Andreini, C.1    Banci, L.2    Rosato, A.3
  • 37
    • 84895735383 scopus 로고    scopus 로고
    • Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery
    • N. Maio A. Singh H. Uhrigshardt N. Saxena W. H. Tong T. A. Rouault Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery Cell Metab. 2014 19 445 457
    • (2014) Cell Metab. , vol.19 , pp. 445-457
    • Maio, N.1    Singh, A.2    Uhrigshardt, H.3    Saxena, N.4    Tong, W.H.5    Rouault, T.A.6
  • 39
    • 0022227668 scopus 로고
    • Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster
    • K. E. Brigle W. E. Newton D. R. Dean Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster Gene 1985 37 37 44
    • (1985) Gene , vol.37 , pp. 37-44
    • Brigle, K.E.1    Newton, W.E.2    Dean, D.R.3
  • 40
    • 0022339866 scopus 로고
    • Azotobacter vinelandii nifD- and nifE-encoded polypeptides share structural homology
    • D. R. Dean K. E. Brigle Azotobacter vinelandii nifD- and nifE-encoded polypeptides share structural homology Proc. Natl. Acad. Sci. U. S. A. 1985 82 5720 5723
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 5720-5723
    • Dean, D.R.1    Brigle, K.E.2
  • 41
    • 34147189950 scopus 로고    scopus 로고
    • Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems
    • P. C. Dos Santos D. C. Johnson B. E. Ragle M. C. Unciuleac D. R. Dean Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems J. Bacteriol. 2007 189 2854 2862
    • (2007) J. Bacteriol. , vol.189 , pp. 2854-2862
    • Dos Santos, P.C.1    Johnson, D.C.2    Ragle, B.E.3    Unciuleac, M.C.4    Dean, D.R.5
  • 42
    • 84939940637 scopus 로고    scopus 로고
    • Genetic approaches of the Fe-S cluster biogenesis process in bacteria: Historical account, methodological aspects and future challenges
    • B. Py F. Barras Genetic approaches of the Fe-S cluster biogenesis process in bacteria: historical account, methodological aspects and future challenges Biochim. Biophys. Acta 2015 1853 1429 1435
    • (2015) Biochim. Biophys. Acta , vol.1853 , pp. 1429-1435
    • Py, B.1    Barras, F.2
  • 43
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • W. H. Tong T. A. Rouault Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis Cell Metab. 2006 3 199 210
    • (2006) Cell Metab. , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 44
    • 84925285506 scopus 로고    scopus 로고
    • Mammalian iron-sulphur proteins: Novel insights into biogenesis and function
    • T. A. Rouault Mammalian iron-sulphur proteins: novel insights into biogenesis and function Nat. Rev. Mol. Cell Biol. 2015 16 45 55
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 45-55
    • Rouault, T.A.1
  • 46
    • 84930051032 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery
    • N. Maio T. A. Rouault Iron-sulfur cluster biogenesis in mammalian cells: new insights into the molecular mechanisms of cluster delivery Biochim. Biophys. Acta 2015 1853 1493 1512
    • (2015) Biochim. Biophys. Acta , vol.1853 , pp. 1493-1512
    • Maio, N.1    Rouault, T.A.2
  • 47
    • 84891379841 scopus 로고    scopus 로고
    • Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly
    • A. Pandey D. M. Gordon J. Pain T. L. Stemmler A. Dancis D. Pain Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly J. Biol. Chem. 2013 288 36773 36786
    • (2013) J. Biol. Chem. , vol.288 , pp. 36773-36786
    • Pandey, A.1    Gordon, D.M.2    Pain, J.3    Stemmler, T.L.4    Dancis, A.5    Pain, D.6
  • 48
    • 84896110237 scopus 로고    scopus 로고
    • Frataxin-bypassing Isu1: Characterization of the bypass activity in cells and mitochondria
    • H. Yoon S. A. Knight A. Pandey J. Pain Y. Zhang D. Pain A. Dancis Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondria Biochem. J. 2014 459 71 81
    • (2014) Biochem. J. , vol.459 , pp. 71-81
    • Yoon, H.1    Knight, S.A.2    Pandey, A.3    Pain, J.4    Zhang, Y.5    Pain, D.6    Dancis, A.7
  • 49
    • 84869029429 scopus 로고    scopus 로고
    • Persulfide formation on mitochondrial cysteine desulfurase: Enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis
    • A. Pandey R. Golla H. Yoon A. Dancis D. Pain Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis Biochem. J. 2012 448 171 187
    • (2012) Biochem. J. , vol.448 , pp. 171-187
    • Pandey, A.1    Golla, R.2    Yoon, H.3    Dancis, A.4    Pain, D.5
  • 50
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • D. C. Johnson D. R. Dean A. D. Smith M. K. Johnson Structure, function, and formation of biological iron-sulfur clusters Annu. Rev. Biochem. 2005 74 247 281
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 52
    • 84939992480 scopus 로고    scopus 로고
    • Iron loading site on the Fe-S cluster assembly scaffold protein is distinct from the active site
    • A. V. Rodrigues A. Kandegedara J. A. Rotondo A. Dancis T. L. Stemmler Iron loading site on the Fe-S cluster assembly scaffold protein is distinct from the active site Biometals 2015 28 567 576
    • (2015) Biometals , vol.28 , pp. 567-576
    • Rodrigues, A.V.1    Kandegedara, A.2    Rotondo, J.A.3    Dancis, A.4    Stemmler, T.L.5
  • 53
    • 84905674436 scopus 로고    scopus 로고
    • Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry
    • J. Bridwell-Rabb N. G. Fox C. L. Tsai A. M. Winn D. P. Barondeau Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry Biochemistry 2014 53 4904 4913
    • (2014) Biochemistry , vol.53 , pp. 4904-4913
    • Bridwell-Rabb, J.1    Fox, N.G.2    Tsai, C.L.3    Winn, A.M.4    Barondeau, D.P.5
  • 55
    • 79551514731 scopus 로고    scopus 로고
    • Mammalian frataxin: An essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex
    • S. Schmucker A. Martelli F. Colin A. Page M. Wattenhofer-Donze L. Reutenauer H. Puccio Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex PLoS One 2011 6 e16199
    • (2011) PLoS One , vol.6 , pp. e16199
    • Schmucker, S.1    Martelli, A.2    Colin, F.3    Page, A.4    Wattenhofer-Donze, M.5    Reutenauer, L.6    Puccio, H.7
  • 56
    • 69249084026 scopus 로고    scopus 로고
    • Oligomeric yeast frataxin drives assembly of core machinery for mitochondrial iron-sulfur cluster synthesis
    • H. Li O. Gakh D. Y. t. Smith G. Isaya Oligomeric yeast frataxin drives assembly of core machinery for mitochondrial iron-sulfur cluster synthesis J. Biol. Chem. 2009 284 21971 21980
    • (2009) J. Biol. Chem. , vol.284 , pp. 21971-21980
    • Li, H.1    Gakh, O.2    Isaya, G.3
  • 57
    • 84966319172 scopus 로고    scopus 로고
    • Architecture of the Yeast Mitochondrial Iron-Sulfur Cluster Assembly Machinery: The subcomplex formed by the iron donor, Yfh1 protein, and the scaffold, Isu1 protein
    • W. Ranatunga O. Gakh B. K. Galeano D. Y. t. Smith C. A. Soderberg S. Al-Karadaghi J. R. Thompson G. Isaya Architecture of the Yeast Mitochondrial Iron-Sulfur Cluster Assembly Machinery: The subcomplex formed by the iron donor, Yfh1 protein, and the scaffold, Isu1 protein J. Biol. Chem. 2016 291 10378 10398
    • (2016) J. Biol. Chem. , vol.291 , pp. 10378-10398
    • Ranatunga, W.1    Gakh, O.2    Galeano, B.K.3    Soderberg, C.A.4    Al-Karadaghi, S.5    Thompson, J.R.6    Isaya, G.7
  • 58
    • 79954430645 scopus 로고    scopus 로고
    • Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange
    • W. Qi J. A. Cowan Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange Chem. Commun. 2011 47 4989 4991
    • (2011) Chem. Commun. , vol.47 , pp. 4989-4991
    • Qi, W.1    Cowan, J.A.2
  • 59
    • 84855766784 scopus 로고    scopus 로고
    • Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis
    • Y. Shi M. Ghosh G. Kovtunovych D. R. Crooks T. A. Rouault Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis Biochim. Biophys. Acta 2012 1823 484 492
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 484-492
    • Shi, Y.1    Ghosh, M.2    Kovtunovych, G.3    Crooks, D.R.4    Rouault, T.A.5
  • 62
    • 80155203873 scopus 로고    scopus 로고
    • Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange
    • F. Bonomi S. Iametti A. Morleo D. Ta L. E. Vickery Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange Biochemistry 2011 50 9641 9650
    • (2011) Biochemistry , vol.50 , pp. 9641-9650
    • Bonomi, F.1    Iametti, S.2    Morleo, A.3    Ta, D.4    Vickery, L.E.5
  • 63
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • L. E. Vickery J. R. Cupp-Vickery Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation Crit. Rev. Biochem. Mol. Biol. 2007 42 95 111
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 67
    • 0034608935 scopus 로고    scopus 로고
    • Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
    • K. G. Hoff J. J. Silberg L. E. Vickery Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 2000 97 7790 7795
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.E.3
  • 68
    • 77956513437 scopus 로고    scopus 로고
    • Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis
    • H. Uhrigshardt A. Singh G. Kovtunovych M. Ghosh T. A. Rouault Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis Hum. Mol. Genet. 2010 19 3816 3834
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3816-3834
    • Uhrigshardt, H.1    Singh, A.2    Kovtunovych, G.3    Ghosh, M.4    Rouault, T.A.5
  • 69
    • 0036809412 scopus 로고    scopus 로고
    • A specialized mitochondrial molecular chaperone system: A role in formation of Fe/S centers
    • E. A. Craig J. Marszalek A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers Cell. Mol. Life Sci. 2002 59 1658 1665
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1658-1665
    • Craig, E.A.1    Marszalek, J.2
  • 70
    • 84885117582 scopus 로고    scopus 로고
    • Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)
    • K. Cai R. O. Frederick J. H. Kim N. M. Reinen M. Tonelli J. L. Markley Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU) J. Biol. Chem. 2013 288 28755 28770
    • (2013) J. Biol. Chem. , vol.288 , pp. 28755-28770
    • Cai, K.1    Frederick, R.O.2    Kim, J.H.3    Reinen, N.M.4    Tonelli, M.5    Markley, J.L.6
  • 71
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • H. H. Kampinga E. A. Craig The HSP70 chaperone machinery: J proteins as drivers of functional specificity Nat. Rev. Mol. Cell Biol. 2010 11 579 592
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 72
    • 51549120794 scopus 로고    scopus 로고
    • Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU
    • A. K. Fuzery M. Tonelli D. T. Ta G. Cornilescu L. E. Vickery J. L. Markley Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU Biochemistry 2008 47 9394 9404
    • (2008) Biochemistry , vol.47 , pp. 9394-9404
    • Fuzery, A.K.1    Tonelli, M.2    Ta, D.T.3    Cornilescu, G.4    Vickery, L.E.5    Markley, J.L.6
  • 74
    • 79251558426 scopus 로고    scopus 로고
    • Three hydrophobic amino acids in Escherichia coli HscB make the greatest contribution to the stability of the HscB-IscU complex
    • A. K. Fuzery J. J. Oh D. T. Ta L. E. Vickery J. L. Markley Three hydrophobic amino acids in Escherichia coli HscB make the greatest contribution to the stability of the HscB-IscU complex BMC Biochem. 2011 12 3
    • (2011) BMC Biochem. , vol.12 , pp. 3
    • Fuzery, A.K.1    Oh, J.J.2    Ta, D.T.3    Vickery, L.E.4    Markley, J.L.5
  • 75
    • 26444455549 scopus 로고    scopus 로고
    • How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins
    • F. Barras L. Loiseau B. Py How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins Adv. Microb. Physiol. 2005 50 41 101
    • (2005) Adv. Microb. Physiol. , vol.50 , pp. 41-101
    • Barras, F.1    Loiseau, L.2    Py, B.3
  • 76
    • 0034671178 scopus 로고    scopus 로고
    • Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli
    • J. R. Cupp-Vickery L. E. Vickery Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli J. Mol. Biol. 2000 304 835 845
    • (2000) J. Mol. Biol. , vol.304 , pp. 835-845
    • Cupp-Vickery, J.R.1    Vickery, L.E.2
  • 80
    • 84858212583 scopus 로고    scopus 로고
    • HSC20 interacts with frataxin and is involved in iron-sulfur cluster biogenesis and iron homeostasis
    • Y. Shan G. Cortopassi HSC20 interacts with frataxin and is involved in iron-sulfur cluster biogenesis and iron homeostasis Hum. Mol. Genet. 2012 21 1457 1469
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1457-1469
    • Shan, Y.1    Cortopassi, G.2
  • 81
    • 84912535660 scopus 로고    scopus 로고
    • The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations
    • T. R. Alderson J. H. Kim K. Cai R. O. Frederick M. Tonelli J. L. Markley The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations Biochemistry 2014 53 7148 7159
    • (2014) Biochemistry , vol.53 , pp. 7148-7159
    • Alderson, T.R.1    Kim, J.H.2    Cai, K.3    Frederick, R.O.4    Tonelli, M.5    Markley, J.L.6
  • 82
    • 3142653172 scopus 로고    scopus 로고
    • Preferential substrate binding orientation by the molecular chaperone HscA
    • T. L. Tapley L. E. Vickery Preferential substrate binding orientation by the molecular chaperone HscA J. Biol. Chem. 2004 279 28435 28442
    • (2004) J. Biol. Chem. , vol.279 , pp. 28435-28442
    • Tapley, T.L.1    Vickery, L.E.2
  • 83
    • 0037178878 scopus 로고    scopus 로고
    • Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU
    • K. G. Hoff D. T. Ta T. L. Tapley J. J. Silberg L. E. Vickery Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU J. Biol. Chem. 2002 277 27353 27359
    • (2002) J. Biol. Chem. , vol.277 , pp. 27353-27359
    • Hoff, K.G.1    Ta, D.T.2    Tapley, T.L.3    Silberg, J.J.4    Vickery, L.E.5
  • 84
    • 0141844533 scopus 로고    scopus 로고
    • Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system
    • K. G. Hoff J. R. Cupp-Vickery L. E. Vickery Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system J. Biol. Chem. 2003 278 37582 37589
    • (2003) J. Biol. Chem. , vol.278 , pp. 37582-37589
    • Hoff, K.G.1    Cupp-Vickery, J.R.2    Vickery, L.E.3
  • 85
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • J. R. Cupp-Vickery J. C. Peterson D. T. Ta L. E. Vickery Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC J. Mol. Biol. 2004 342 1265 1278
    • (2004) J. Mol. Biol. , vol.342 , pp. 1265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 86
    • 84866139470 scopus 로고    scopus 로고
    • Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU)
    • J. H. Kim M. Tonelli R. O. Frederick D. C. Chow J. L. Markley Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU) J. Biol. Chem. 2012 287 31406 31413
    • (2012) J. Biol. Chem. , vol.287 , pp. 31406-31413
    • Kim, J.H.1    Tonelli, M.2    Frederick, R.O.3    Chow, D.C.4    Markley, J.L.5
  • 87
    • 33750445986 scopus 로고    scopus 로고
    • Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii
    • D. C. Johnson M. C. Unciuleac D. R. Dean Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii J. Bacteriol. 2006 188 7551 7561
    • (2006) J. Bacteriol. , vol.188 , pp. 7551-7561
    • Johnson, D.C.1    Unciuleac, M.C.2    Dean, D.R.3
  • 88
    • 0034911990 scopus 로고    scopus 로고
    • Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins
    • U. Tokumoto Y. Takahashi Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins J. Biochem. 2001 130 63 71
    • (2001) J. Biochem. , vol.130 , pp. 63-71
    • Tokumoto, U.1    Takahashi, Y.2
  • 89
    • 57049159293 scopus 로고    scopus 로고
    • Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones
    • F. Bonomi S. Iametti A. Morleo D. Ta L. E. Vickery Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones Biochemistry 2008 47 12795 12801
    • (2008) Biochemistry , vol.47 , pp. 12795-12801
    • Bonomi, F.1    Iametti, S.2    Morleo, A.3    Ta, D.4    Vickery, L.E.5
  • 90
    • 0035907297 scopus 로고    scopus 로고
    • J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins
    • R. Kim S. Saxena D. M. Gordon D. Pain A. Dancis J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins J. Biol. Chem. 2001 276 17524 17532
    • (2001) J. Biol. Chem. , vol.276 , pp. 17524-17532
    • Kim, R.1    Saxena, S.2    Gordon, D.M.3    Pain, D.4    Dancis, A.5
  • 91
    • 84876468556 scopus 로고    scopus 로고
    • Insertion mutants in Drosophila melanogaster Hsc20 halt larval growth and lead to reduced iron-sulfur cluster enzyme activities and impaired iron homeostasis
    • H. Uhrigshardt T. A. Rouault F. Missirlis Insertion mutants in Drosophila melanogaster Hsc20 halt larval growth and lead to reduced iron-sulfur cluster enzyme activities and impaired iron homeostasis JBIC, J. Biol. Inorg. Chem. 2013 18 441 449
    • (2013) JBIC, J. Biol. Inorg. Chem. , vol.18 , pp. 441-449
    • Uhrigshardt, H.1    Rouault, T.A.2    Missirlis, F.3
  • 93
    • 77958547635 scopus 로고    scopus 로고
    • Role of DnaJ G/F-rich domain in conformational recognition and binding of protein substrates
    • J. Perales-Calvo A. Muga F. Moro Role of DnaJ G/F-rich domain in conformational recognition and binding of protein substrates J. Biol. Chem. 2010 285 34231 34239
    • (2010) J. Biol. Chem. , vol.285 , pp. 34231-34239
    • Perales-Calvo, J.1    Muga, A.2    Moro, F.3
  • 94
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
    • A. Szabo R. Korszun F. U. Hartl J. Flanagan A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates EMBO J. 1996 15 408 417
    • (1996) EMBO J. , vol.15 , pp. 408-417
    • Szabo, A.1    Korszun, R.2    Hartl, F.U.3    Flanagan, J.4
  • 95
    • 0037077211 scopus 로고    scopus 로고
    • Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding
    • S. Lee C. Y. Fan J. M. Younger H. Ren D. M. Cyr Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding J. Biol. Chem. 2002 277 21675 21682
    • (2002) J. Biol. Chem. , vol.277 , pp. 21675-21682
    • Lee, S.1    Fan, C.Y.2    Younger, J.M.3    Ren, H.4    Cyr, D.M.5
  • 96
    • 15944386011 scopus 로고    scopus 로고
    • Structure-based mutagenesis studies of the peptide substrate binding fragment of type i heat-shock protein 40
    • J. Li B. Sha Structure-based mutagenesis studies of the peptide substrate binding fragment of type I heat-shock protein 40 Biochem. J. 2005 386 453 460
    • (2005) Biochem. J. , vol.386 , pp. 453-460
    • Li, J.1    Sha, B.2
  • 108
    • 84939935355 scopus 로고    scopus 로고
    • Special issue on iron-sulfur proteins: Structure, function, biogenesis and diseases
    • R. Lill J. B. Broderick D. R. Dean Special issue on iron-sulfur proteins: structure, function, biogenesis and diseases Biochim. Biophys. Acta 2015 1853 1251 1252
    • (2015) Biochim. Biophys. Acta , vol.1853 , pp. 1251-1252
    • Lill, R.1    Broderick, J.B.2    Dean, D.R.3
  • 109
    • 84961832231 scopus 로고    scopus 로고
    • Mitochondrial iron overload: Causes and consequences
    • T. A. Rouault Mitochondrial iron overload: causes and consequences Curr. Opin. Genet. Dev. 2016 38 31 37
    • (2016) Curr. Opin. Genet. Dev. , vol.38 , pp. 31-37
    • Rouault, T.A.1
  • 110
    • 84879562737 scopus 로고    scopus 로고
    • The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation
    • M. A. Uzarska R. Dutkiewicz S. A. Freibert R. Lill U. Muhlenhoff The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation Mol. Biol. Cell 2013 24 1830 1841
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1830-1841
    • Uzarska, M.A.1    Dutkiewicz, R.2    Freibert, S.A.3    Lill, R.4    Muhlenhoff, U.5
  • 111
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • U. Muhlenhoff J. Gerber N. Richhardt R. Lill Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p EMBO J. 2003 22 4815 4825
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 112
    • 0037020228 scopus 로고    scopus 로고
    • Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein
    • G. Belli J. Polaina J. Tamarit M. A. De La Torre M. T. Rodriguez-Manzaneque J. Ros E. Herrero Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein J. Biol. Chem. 2002 277 37590 37596
    • (2002) J. Biol. Chem. , vol.277 , pp. 37590-37596
    • Belli, G.1    Polaina, J.2    Tamarit, J.3    De La Torre, M.A.4    Rodriguez-Manzaneque, M.T.5    Ros, J.6    Herrero, E.7
  • 113
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • M. T. Rodriguez-Manzaneque J. Tamarit G. Belli J. Ros E. Herrero Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes Mol. Biol. Cell 2002 13 1109 1121
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 116
    • 84861850380 scopus 로고    scopus 로고
    • Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis
    • H. Li C. E. Outten Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis Biochemistry 2012 51 4377 4389
    • (2012) Biochemistry , vol.51 , pp. 4377-4389
    • Li, H.1    Outten, C.E.2
  • 120
    • 33745872884 scopus 로고    scopus 로고
    • Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae
    • L. Ojeda G. Keller U. Muhlenhoff J. C. Rutherford R. Lill D. R. Winge Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae J. Biol. Chem. 2006 281 17661 17669
    • (2006) J. Biol. Chem. , vol.281 , pp. 17661-17669
    • Ojeda, L.1    Keller, G.2    Muhlenhoff, U.3    Rutherford, J.C.4    Lill, R.5    Winge, D.R.6
  • 121
    • 33751529756 scopus 로고    scopus 로고
    • Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae
    • N. Pujol-Carrion G. Belli E. Herrero A. Nogues M. A. de la Torre-Ruiz Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae J. Cell Sci. 2006 119 4554 4564
    • (2006) J. Cell Sci. , vol.119 , pp. 4554-4564
    • Pujol-Carrion, N.1    Belli, G.2    Herrero, E.3    Nogues, A.4    De La Torre-Ruiz, M.A.5
  • 126
    • 12744251555 scopus 로고    scopus 로고
    • Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin
    • M. A. Huynen C. A. Spronk T. Gabaldon B. Snel Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin FEBS Lett. 2005 579 591 596
    • (2005) FEBS Lett. , vol.579 , pp. 591-596
    • Huynen, M.A.1    Spronk, C.A.2    Gabaldon, T.3    Snel, B.4
  • 127
    • 67650999518 scopus 로고    scopus 로고
    • Evolution and diversity of glutaredoxins in photosynthetic organisms
    • J. Couturier J. P. Jacquot N. Rouhier Evolution and diversity of glutaredoxins in photosynthetic organisms CMLS, Cell. Mol. Life Sci. 2009 66 2539 2557
    • (2009) CMLS, Cell. Mol. Life Sci. , vol.66 , pp. 2539-2557
    • Couturier, J.1    Jacquot, J.P.2    Rouhier, N.3
  • 131
    • 0024834348 scopus 로고
    • Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene
    • M. Aldea T. Garrido C. Hernandez-Chico M. Vicente S. R. Kushner Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene EMBO J. 1989 8 3923 3931
    • (1989) EMBO J. , vol.8 , pp. 3923-3931
    • Aldea, M.1    Garrido, T.2    Hernandez-Chico, C.3    Vicente, M.4    Kushner, S.R.5
  • 133
    • 78650949287 scopus 로고    scopus 로고
    • Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast
    • H. Li D. T. Mapolelo N. N. Dingra G. Keller P. J. Riggs-Gelasco D. R. Winge M. K. Johnson C. E. Outten Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast J. Biol. Chem. 2011 286 867 876
    • (2011) J. Biol. Chem. , vol.286 , pp. 867-876
    • Li, H.1    Mapolelo, D.T.2    Dingra, N.N.3    Keller, G.4    Riggs-Gelasco, P.J.5    Winge, D.R.6    Johnson, M.K.7    Outten, C.E.8
  • 134
    • 66949146078 scopus 로고    scopus 로고
    • IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions
    • G. Tan J. Lu J. P. Bitoun H. Huang H. Ding IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions Biochem. J. 2009 420 463 472
    • (2009) Biochem. J. , vol.420 , pp. 463-472
    • Tan, G.1    Lu, J.2    Bitoun, J.P.3    Huang, H.4    Ding, H.5
  • 140
    • 84888424052 scopus 로고    scopus 로고
    • The evolutionarily conserved iron-sulfur protein INDH is required for complex i assembly and mitochondrial translation in Arabidopsis [corrected]
    • M. M. Wydro P. Sharma J. M. Foster K. Bych E. H. Meyer J. Balk The evolutionarily conserved iron-sulfur protein INDH is required for complex I assembly and mitochondrial translation in Arabidopsis [corrected] Plant cell 2013 25 4014 4027
    • (2013) Plant Cell , vol.25 , pp. 4014-4027
    • Wydro, M.M.1    Sharma, P.2    Foster, J.M.3    Bych, K.4    Meyer, E.H.5    Balk, J.6
  • 141
    • 0036666032 scopus 로고    scopus 로고
    • An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: What, when, and where?
    • R. Wadhwa K. Taira S. C. Kaul An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where? Cell Stress Chaperones 2002 7 309 316
    • (2002) Cell Stress Chaperones , vol.7 , pp. 309-316
    • Wadhwa, R.1    Taira, K.2    Kaul, S.C.3
  • 142
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • M. Daugaard M. Rohde M. Jaattela The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions FEBS Lett. 2007 581 3702 3710
    • (2007) FEBS Lett. , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 143
    • 84978127385 scopus 로고    scopus 로고
    • Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes
    • T. R. Alderson J. H. Kim J. L. Markley Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes Structure 2016 24 1014 1030
    • (2016) Structure , vol.24 , pp. 1014-1030
    • Alderson, T.R.1    Kim, J.H.2    Markley, J.L.3
  • 144
    • 0022425145 scopus 로고
    • The prosthetic groups of succinate dehydrogenase: 30 years from discovery to identification
    • T. P. Singer M. K. Johnson The prosthetic groups of succinate dehydrogenase: 30 years from discovery to identification FEBS Lett. 1985 190 189 198
    • (1985) FEBS Lett. , vol.190 , pp. 189-198
    • Singer, T.P.1    Johnson, M.K.2
  • 145
    • 0033840193 scopus 로고    scopus 로고
    • Late-onset optic atrophy, ataxia, and myopathy associated with a mutation of a complex II gene
    • M. A. Birch-Machin R. W. Taylor B. Cochran B. A. Ackrell D. M. Turnbull Late-onset optic atrophy, ataxia, and myopathy associated with a mutation of a complex II gene Ann. Neurol. 2000 48 330 335
    • (2000) Ann. Neurol. , vol.48 , pp. 330-335
    • Birch-Machin, M.A.1    Taylor, R.W.2    Cochran, B.3    Ackrell, B.A.4    Turnbull, D.M.5
  • 150
    • 0030600143 scopus 로고    scopus 로고
    • A structural model for the membrane-integral domain of succinate: Quinone oxidoreductases
    • C. Hagerhall L. Hederstedt A structural model for the membrane-integral domain of succinate: quinone oxidoreductases FEBS Lett. 1996 389 25 31
    • (1996) FEBS Lett. , vol.389 , pp. 25-31
    • Hagerhall, C.1    Hederstedt, L.2
  • 151
    • 84904469894 scopus 로고    scopus 로고
    • A million peptide motifs for the molecular biologist
    • P. Tompa N. E. Davey T. J. Gibson M. M. Babu A million peptide motifs for the molecular biologist Mol. Cell 2014 55 161 169
    • (2014) Mol. Cell , vol.55 , pp. 161-169
    • Tompa, P.1    Davey, N.E.2    Gibson, T.J.3    Babu, M.M.4
  • 152
    • 84866463338 scopus 로고    scopus 로고
    • Structural biology. Versatility from protein disorder
    • M. M. Babu R. W. Kriwacki R. V. Pappu Structural biology. Versatility from protein disorder Science 2012 337 1460 1461
    • (2012) Science , vol.337 , pp. 1460-1461
    • Babu, M.M.1    Kriwacki, R.W.2    Pappu, R.V.3
  • 154
    • 84923045322 scopus 로고    scopus 로고
    • Eukaryotic LYR Proteins Interact with Mitochondrial Protein Complexes
    • H. Angerer Eukaryotic LYR Proteins Interact with Mitochondrial Protein Complexes Biology 2015 4 133 150
    • (2015) Biology , vol.4 , pp. 133-150
    • Angerer, H.1
  • 155
    • 68049086933 scopus 로고    scopus 로고
    • Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
    • Y. Shi M. C. Ghosh W. H. Tong T. A. Rouault Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis Hum. Mol. Genet. 2009 18 3014 3025
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3014-3025
    • Shi, Y.1    Ghosh, M.C.2    Tong, W.H.3    Rouault, T.A.4
  • 156
    • 84884600998 scopus 로고    scopus 로고
    • The superfamily of mitochondrial Complex1-LYR motif-containing (LYRM) proteins
    • H. Angerer The superfamily of mitochondrial Complex1-LYR motif-containing (LYRM) proteins Biochem. Soc. Trans. 2013 41 1335 1341
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1335-1341
    • Angerer, H.1
  • 157
    • 0033119486 scopus 로고    scopus 로고
    • Acn9 is a novel protein of gluconeogenesis that is located in the mitochondrial intermembrane space
    • R. A. Dennis M. T. McCammon Acn9 is a novel protein of gluconeogenesis that is located in the mitochondrial intermembrane space Eur. J. Biochem. 1999 261 236 243
    • (1999) Eur. J. Biochem. , vol.261 , pp. 236-243
    • Dennis, R.A.1    McCammon, M.T.2
  • 158
    • 0035794147 scopus 로고    scopus 로고
    • Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions
    • L. Lefebvre-Legendre J. Vaillier H. Benabdelhak J. Velours P. P. Slonimski J. P. di Rago Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions J. Biol. Chem. 2001 276 6789 6796
    • (2001) J. Biol. Chem. , vol.276 , pp. 6789-6796
    • Lefebvre-Legendre, L.1    Vaillier, J.2    Benabdelhak, H.3    Velours, J.4    Slonimski, P.P.5    Di Rago, J.P.6
  • 159
    • 84872100371 scopus 로고    scopus 로고
    • LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial complex III assembly in human cells
    • E. Sanchez T. Lobo J. L. Fox M. Zeviani D. R. Winge E. Fernandez-Vizarra LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial complex III assembly in human cells Biochim. Biophys. Acta 2013 1827 285 293
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 285-293
    • Sanchez, E.1    Lobo, T.2    Fox, J.L.3    Zeviani, M.4    Winge, D.R.5    Fernandez-Vizarra, E.6
  • 163
    • 3142716203 scopus 로고    scopus 로고
    • Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function
    • R. Dutkiewicz B. Schilke S. Cheng H. Knieszner E. A. Craig J. Marszalek Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function J. Biol. Chem. 2004 279 29167 29174
    • (2004) J. Biol. Chem. , vol.279 , pp. 29167-29174
    • Dutkiewicz, R.1    Schilke, B.2    Cheng, S.3    Knieszner, H.4    Craig, E.A.5    Marszalek, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.