메뉴 건너뛰기




Volumn 15, Issue 4, 2016, Pages 1308-1322

Exploiting Bacterial Operons to Illuminate Human Iron-Sulfur Proteins

Author keywords

2Fe 2S; 4Fe 4S; biogenesis; bioinorganic chemistry; Fe2S2; Fe4S4; iron; mitochondrion; respiration

Indexed keywords

CYTOCHROME C OXIDASE; IRON SULFUR PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE); TRANSFER RNA; UBIQUINOL CYTOCHROME C REDUCTASE; BACTERIAL PROTEIN;

EID: 84963667993     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.6b00045     Document Type: Article
Times cited : (41)

References (86)
  • 1
    • 0033120863 scopus 로고    scopus 로고
    • Fe-S proteins in sensing and regulatory functions
    • Beinert, H.; Kiley, P. J. Fe-S proteins in sensing and regulatory functions Curr. Opin. Chem. Biol. 1999, 3, 152-157 10.1016/S1367-5931(99)80027-1
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 152-157
    • Beinert, H.1    Kiley, P.J.2
  • 4
    • 79952106944 scopus 로고    scopus 로고
    • Structural, Mechanistic and Coordination Chemistry of Relevance to the Biosynthesis of Iron-Sulfur and Related Iron Cofactors
    • Qi, W.; Cowan, J. A. Structural, Mechanistic and Coordination Chemistry of Relevance to the Biosynthesis of Iron-Sulfur and Related Iron Cofactors Coord. Chem. Rev. 2011, 255, 688-699 10.1016/j.ccr.2010.10.016
    • (2011) Coord. Chem. Rev. , vol.255 , pp. 688-699
    • Qi, W.1    Cowan, J.A.2
  • 8
    • 84939946161 scopus 로고    scopus 로고
    • Assembly of Fe/S proteins in bacterial systems: Biochemistry of the bacterial ISC system
    • Blanc, B.; Gerez, C.; Ollagnier de Choudens, S. Assembly of Fe/S proteins in bacterial systems: Biochemistry of the bacterial ISC system Biochim. Biophys. Acta, Mol. Cell Res. 2015, 1853, 1436-1447 10.1016/j.bbamcr.2014.12.009
    • (2015) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1853 , pp. 1436-1447
    • Blanc, B.1    Gerez, C.2    Ollagnier De Choudens, S.3
  • 9
    • 84926221250 scopus 로고    scopus 로고
    • Recent advances in the Suf Fe-S cluster biogenesis pathway: Beyond the Proteobacteria
    • Outten, F. W. Recent advances in the Suf Fe-S cluster biogenesis pathway: Beyond the Proteobacteria Biochim. Biophys. Acta, Mol. Cell Res. 2015, 1853, 1464-1469 10.1016/j.bbamcr.2014.11.001
    • (2015) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1853 , pp. 1464-1469
    • Outten, F.W.1
  • 11
    • 84896940877 scopus 로고    scopus 로고
    • Mechanism of nitrogen fixation by nitrogenase: The next stage
    • Hoffman, B. M.; Lukoyanov, D.; Yang, Z. Y.; Dean, D. R.; Seefeldt, L. C. Mechanism of nitrogen fixation by nitrogenase: the next stage Chem. Rev. 2014, 114, 4041-4062 10.1021/cr400641x
    • (2014) Chem. Rev. , vol.114 , pp. 4041-4062
    • Hoffman, B.M.1    Lukoyanov, D.2    Yang, Z.Y.3    Dean, D.R.4    Seefeldt, L.C.5
  • 13
    • 50149117370 scopus 로고    scopus 로고
    • Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor
    • Hernandez, J. A.; Curatti, L.; Aznar, C. P.; Perova, Z.; Britt, R. D.; Rubio, L. M. Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 11679-11684 10.1073/pnas.0803576105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 11679-11684
    • Hernandez, J.A.1    Curatti, L.2    Aznar, C.P.3    Perova, Z.4    Britt, R.D.5    Rubio, L.M.6
  • 14
    • 38649087966 scopus 로고    scopus 로고
    • Iron-sulfur protein folds, iron-sulfur chemistry, and evolution
    • Meyer, J. Iron-sulfur protein folds, iron-sulfur chemistry, and evolution JBIC, J. Biol. Inorg. Chem. 2008, 13, 157-170 10.1007/s00775-007-0318-7
    • (2008) JBIC, J. Biol. Inorg. Chem. , vol.13 , pp. 157-170
    • Meyer, J.1
  • 15
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Natures modular, multipurpose structures
    • Beinert, H.; Holm, R. H.; Munck, E. Iron-sulfur clusters: natures modular, multipurpose structures Science 1997, 277, 653-659 10.1126/science.277.5326.653
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 16
    • 23044477952 scopus 로고    scopus 로고
    • Organization of iron-sulfur clusters in respiratory complex i
    • Hinchliffe, P.; Sazanov, L. A. Organization of iron-sulfur clusters in respiratory complex I Science 2005, 309, 771-774 10.1126/science.1113988
    • (2005) Science , vol.309 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 18
    • 84857029886 scopus 로고    scopus 로고
    • Iron-sulphur clusters in nucleic acid processing enzymes
    • White, M. F.; Dillingham, M. S. Iron-sulphur clusters in nucleic acid processing enzymes Curr. Opin. Struct. Biol. 2012, 22, 94-100 10.1016/j.sbi.2011.11.004
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 94-100
    • White, M.F.1    Dillingham, M.S.2
  • 20
    • 84899732999 scopus 로고    scopus 로고
    • DNA-mediated signaling by proteins with 4Fe-4S clusters is necessary for genomic integrity
    • Grodick, M. A.; Segal, H. M.; Zwang, T. J.; Barton, J. K. DNA-mediated signaling by proteins with 4Fe-4S clusters is necessary for genomic integrity J. Am. Chem. Soc. 2014, 136, 6470-6478 10.1021/ja501973c
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 6470-6478
    • Grodick, M.A.1    Segal, H.M.2    Zwang, T.J.3    Barton, J.K.4
  • 21
    • 84908097207 scopus 로고    scopus 로고
    • Iron-sulfur clusters as biological sensors: The chemistry of reactions with molecular oxygen and nitric oxide
    • Crack, J. C.; Green, J.; Thomson, A. J.; Le Brun, N. E. Iron-sulfur clusters as biological sensors: the chemistry of reactions with molecular oxygen and nitric oxide Acc. Chem. Res. 2014, 47, 3196-3205 10.1021/ar5002507
    • (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
  • 22
    • 34248653740 scopus 로고    scopus 로고
    • Metabolic regulation of citrate and iron by aconitases: Role of iron-sulfur cluster biogenesis
    • Tong, W. H.; Rouault, T. A. Metabolic regulation of citrate and iron by aconitases: role of iron-sulfur cluster biogenesis BioMetals 2007, 20, 549-564 10.1007/s10534-006-9047-6
    • (2007) BioMetals , vol.20 , pp. 549-564
    • Tong, W.H.1    Rouault, T.A.2
  • 23
    • 70350348305 scopus 로고    scopus 로고
    • Metalloproteomes: A bioinformatic approach
    • Andreini, C.; Bertini, I.; Rosato, A. Metalloproteomes: a bioinformatic approach Acc. Chem. Res. 2009, 42, 1471-1479 10.1021/ar900015x
    • (2009) Acc. Chem. Res. , vol.42 , pp. 1471-1479
    • Andreini, C.1    Bertini, I.2    Rosato, A.3
  • 25
    • 38649097521 scopus 로고    scopus 로고
    • Occurence of copper through the three domains of life: A bioinformatic approach
    • Andreini, C.; Banci, L.; Bertini, I.; Rosato, A. Occurence of copper through the three domains of life: a bioinformatic approach J.Proteome Res. 2008, 7, 209-216 10.1021/pr070480u
    • (2008) J.Proteome Res. , vol.7 , pp. 209-216
    • Andreini, C.1    Banci, L.2    Bertini, I.3    Rosato, A.4
  • 26
    • 79953188035 scopus 로고    scopus 로고
    • A simple protocol for the comparative analysis of the structure and occurence of biochemical pathways across superkingdoms
    • Andreini, C.; Bertini, I.; Cavallaro, G.; Decaria, L.; Rosato, A. A simple protocol for the comparative analysis of the structure and occurence of biochemical pathways across superkingdoms J. Chem. Inf. Model. 2011, 51, 730-738 10.1021/ci100392q
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 730-738
    • Andreini, C.1    Bertini, I.2    Cavallaro, G.3    Decaria, L.4    Rosato, A.5
  • 29
    • 3142747652 scopus 로고    scopus 로고
    • A hint to search for metalloproteins in gene banks
    • Andreini, C.; Bertini, I.; Rosato, A. A hint to search for metalloproteins in gene banks Bioinformatics 2004, 20, 1373-1380 10.1093/bioinformatics/bth095
    • (2004) Bioinformatics , vol.20 , pp. 1373-1380
    • Andreini, C.1    Bertini, I.2    Rosato, A.3
  • 32
    • 84949215654 scopus 로고    scopus 로고
    • Comparative Protein Structure Modeling Using MODELLER
    • Webb, B.; Sali, A. Comparative Protein Structure Modeling Using MODELLER Curr.Protoc.Bioinformatics. 2014, 47, 5.6.1 10.1002/0471250953.bi0506s47
    • (2014) Curr.Protoc.Bioinformatics. , vol.47 , pp. 561
    • Webb, B.1    Sali, A.2
  • 33
    • 80051920557 scopus 로고    scopus 로고
    • A grid-enable web portal for NMR structure refinement with AMBER
    • Bertini, I.; Case, D. A.; Ferella, L.; Giachetti, A.; Rosato, A. A grid-enable web portal for NMR structure refinement with AMBER Bioinformatics 2011, 27, 2384-2390 10.1093/bioinformatics/btr415
    • (2011) Bioinformatics , vol.27 , pp. 2384-2390
    • Bertini, I.1    Case, D.A.2    Ferella, L.3    Giachetti, A.4    Rosato, A.5
  • 34
    • 67650358909 scopus 로고    scopus 로고
    • QMEAN server for protein model quality estimation
    • Benkert, P.; Kunzli, M.; Schwede, T. QMEAN server for protein model quality estimation Nucleic Acids Res. 2009, 37, W510-W514 10.1093/nar/gkp322
    • (2009) Nucleic Acids Res. , vol.37 , pp. W510-W514
    • Benkert, P.1    Kunzli, M.2    Schwede, T.3
  • 35
    • 84946069451 scopus 로고    scopus 로고
    • UniProt: A hub for protein information
    • The UniProt Consortium
    • The UniProt Consortium UniProt: a hub for protein information Nucleic Acids Res. 2015, 43, D204-D212 10.1093/nar/gku989
    • (2015) Nucleic Acids Res. , vol.43 , pp. D204-D212
  • 38
    • 84895735383 scopus 로고    scopus 로고
    • Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery
    • Maio, N.; Singh, A.; Uhrigshardt, H.; Saxena, N.; Tong, W. H.; Rouault, T. A. Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery Cell Metab. 2014, 19, 445-457 10.1016/j.cmet.2014.01.015
    • (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
    • 84925285506 scopus 로고    scopus 로고
    • Mammalian iron-sulphur proteins: Novel insights into biogenesis and function
    • Rouault, T. A. Mammalian iron-sulphur proteins: novel insights into biogenesis and function Nat. Rev. Mol. Cell Biol. 2014, 16, 45-55 10.1038/nrm3909
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 45-55
    • Rouault, T.A.1
  • 40
    • 84935016527 scopus 로고    scopus 로고
    • Iron-sulfur proteins hiding in plain sight
    • Rouault, T. A. Iron-sulfur proteins hiding in plain sight Nat. Chem. Biol. 2015, 11, 442-445 10.1038/nchembio.1843
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 442-445
    • Rouault, T.A.1
  • 43
    • 80051817548 scopus 로고    scopus 로고
    • A 2-D gel reference map of the basic human heart proteome
    • Polden, J.; McManus, C. A.; Dos Remedios, C.; Dunn, M. J. A 2-D gel reference map of the basic human heart proteome Proteomics 2011, 11, 3582-3586 10.1002/pmic.201000182
    • (2011) Proteomics , vol.11 , pp. 3582-3586
    • Polden, J.1    McManus, C.A.2    Dos Remedios, C.3    Dunn, M.J.4
  • 44
    • 21244436773 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a human AIF-like gene with ability to induce apoptosis
    • Xie, Q.; Lin, T.; Zhang, Y.; Zheng, J.; Bonanno, J. A. Molecular cloning and characterization of a human AIF-like gene with ability to induce apoptosis J. Biol. Chem. 2005, 280, 19673-19681 10.1074/jbc.M409517200
    • (2005) J. Biol. Chem. , vol.280 , pp. 19673-19681
    • Xie, Q.1    Lin, T.2    Zhang, Y.3    Zheng, J.4    Bonanno, J.A.5
  • 48
    • 79954430645 scopus 로고    scopus 로고
    • Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange
    • Qi, W.; Cowan, J. A. Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange Chem. Commun. (Cambridge, U. K.) 2011, 47, 4989-4991 10.1039/c0cc05079b
    • (2011) Chem. Commun. (Cambridge, U. K.) , vol.47 , pp. 4989-4991
    • Qi, W.1    Cowan, J.A.2
  • 49
    • 84941879247 scopus 로고    scopus 로고
    • N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin
    • Banci, L.; Ciofi-Baffoni, S.; Gajda, K.; Muzzioli, R.; Peruzzini, R.; Winkelmann, J. N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin Nat. Chem. Biol. 2015, 11, 772-778 10.1038/nchembio.1892
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 772-778
    • Banci, L.1    Ciofi-Baffoni, S.2    Gajda, K.3    Muzzioli, R.4    Peruzzini, R.5    Winkelmann, J.6
  • 50
    • 0032951727 scopus 로고    scopus 로고
    • Glutamate synthase: A complex iron-sulfur flavoprotein
    • Vanoni, M. A.; Curti, B. Glutamate synthase: a complex iron-sulfur flavoprotein Cell. Mol. Life Sci. 1999, 55, 617-638 10.1007/s000180050319
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 617-638
    • Vanoni, M.A.1    Curti, B.2
  • 52
    • 84872956374 scopus 로고    scopus 로고
    • Iron/sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity
    • Roche, B.; Aussel, L.; Ezraty, B.; Mandin, P.; Py, B.; Barras, F. Iron/sulfur proteins biogenesis in prokaryotes: formation, regulation and diversity Biochim. Biophys. Acta, Bioenerg. 2013, 1827, 455-469 10.1016/j.bbabio.2012.12.010
    • (2013) Biochim. Biophys. Acta, Bioenerg. , vol.1827 , pp. 455-469
    • Roche, B.1    Aussel, L.2    Ezraty, B.3    Mandin, P.4    Py, B.5    Barras, F.6
  • 53
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng, L.; Cash, V. L.; Flint, D. H.; Dean, D. R. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii J. Biol. Chem. 1998, 273, 13264-13272 10.1074/jbc.273.21.13264
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 54
    • 84901940422 scopus 로고    scopus 로고
    • Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli
    • Kim, J. H.; Bothe, J. R.; Frederick, R. O.; Holder, J. C.; Markley, J. L. Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli J. Am. Chem. Soc. 2014, 136, 7933-7942 10.1021/ja501260h
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 7933-7942
    • Kim, J.H.1    Bothe, J.R.2    Frederick, R.O.3    Holder, J.C.4    Markley, J.L.5
  • 55
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F.; Aravind, L.; Spouge, J. L.; Koonin, E. V. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes Genome Res. 1999, 9, 27-43 10.1101/gr.9.1.27
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 57
    • 3042703044 scopus 로고    scopus 로고
    • Analysis of genomic context: Prediction of functional associations from conserved bidirectionally transcribed gene pairs
    • Korbel, J. O.; Jensen, L. J.; von Mering, C.; Bork, P. Analysis of genomic context: prediction of functional associations from conserved bidirectionally transcribed gene pairs Nat. Biotechnol. 2004, 22, 911-917
    • (2004) Nat. Biotechnol. , vol.22 , pp. 911-917
    • Korbel, J.O.1    Jensen, L.J.2    Von Mering, C.3    Bork, P.4
  • 58
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: A fingerprint of proteins that physically interact
    • Dandekar, T.; Snel, B.; Huynen, M.; Bork, P. Conservation of gene order: a fingerprint of proteins that physically interact Trends Biochem. Sci. 1998, 23, 324-328 10.1016/S0968-0004(98)01274-2
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 324-328
    • Dandekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 59
    • 77952915341 scopus 로고    scopus 로고
    • Lipoic acid metabolism in microbial pathogens
    • Spalding, M. D.; Prigge, S. T. Lipoic acid metabolism in microbial pathogens Microbiol.Mol.Biol.Rev. 2010, 74, 200-228 10.1128/MMBR.00008-10
    • (2010) Microbiol.Mol.Biol.Rev. , vol.74 , pp. 200-228
    • Spalding, M.D.1    Prigge, S.T.2
  • 60
    • 24344504437 scopus 로고    scopus 로고
    • Endogenous production of lipoic acid is essential for mouse development
    • Yi, X.; Maeda, N. Endogenous production of lipoic acid is essential for mouse development Mol. Cell. Biol. 2005, 25, 8387-8392 10.1128/MCB.25.18.8387-8392.2005
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8387-8392
    • Yi, X.1    Maeda, N.2
  • 63
    • 84953439212 scopus 로고    scopus 로고
    • Elucidating the molecular function of human BOLA2in GRX3-Dependent anamorsin maturation pathway
    • Banci, L.; Camponeschi, F.; Ciofi-Baffoni, S.; Muzzioli, R. Elucidating the molecular function of human BOLA2in GRX3-Dependent anamorsin maturation pathway J. Am. Chem. Soc. 2015, 137, 16133-16134 10.1021/jacs.5b10592
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 16133-16134
    • Banci, L.1    Camponeschi, F.2    Ciofi-Baffoni, S.3    Muzzioli, R.4
  • 64
    • 0035856503 scopus 로고    scopus 로고
    • Human T cell leukemia virus type 1 Tax associates with a molecular chaperone complex containing hTid-1 and Hsp70
    • Cheng, H.; Cenciarelli, C.; Shao, Z.; Vidal, M.; Parks, W. P.; Pagano, M.; Cheng-Mayer, C. Human T cell leukemia virus type 1 Tax associates with a molecular chaperone complex containing hTid-1 and Hsp70 Curr. Biol. 2001, 11, 1771-1775 10.1016/S0960-9822(01)00540-1
    • (2001) Curr. Biol. , vol.11 , pp. 1771-1775
    • Cheng, H.1    Cenciarelli, C.2    Shao, Z.3    Vidal, M.4    Parks, W.P.5    Pagano, M.6    Cheng-Mayer, C.7
  • 68
    • 84924198377 scopus 로고    scopus 로고
    • BolA is a transcriptional switch that turns off motility and turns on biofilm development
    • Dressaire, C.; Moreira, R. N.; Barahona, S.; Alves de Matos, A. P.; Arraiano, C. M. BolA is a transcriptional switch that turns off motility and turns on biofilm development mBio 2015, 6, e02352-14 10.1128/mBio.02352-14
    • (2015) MBio , vol.6 , pp. e02352-e02414
    • Dressaire, C.1    Moreira, R.N.2    Barahona, S.3    Alves De Matos, A.P.4    Arraiano, C.M.5
  • 69
    • 10644230266 scopus 로고    scopus 로고
    • A genomic timescale of prokaryote evolution: Insights into the origin of methanogenesis, phototrophy, and the colonization of land
    • Battistuzzi, F. U.; Feijao, A.; Hedges, S. B. A genomic timescale of prokaryote evolution: insights into the origin of methanogenesis, phototrophy, and the colonization of land BMC Evol. Biol. 2004, 4, 44 10.1186/1471-2148-4-44
    • (2004) BMC Evol. Biol. , vol.4 , pp. 44
    • Battistuzzi, F.U.1    Feijao, A.2    Hedges, S.B.3
  • 70
    • 84938508489 scopus 로고    scopus 로고
    • Bioenergetic evolution in proteobacteria and mitochondria
    • Degli Esposti, M. Bioenergetic evolution in proteobacteria and mitochondria Genome Biol. Evol. 2014, 6, 3238-3251 10.1093/gbe/evu257
    • (2014) Genome Biol. Evol. , vol.6 , pp. 3238-3251
    • Degli Esposti, M.1
  • 71
    • 84894414901 scopus 로고    scopus 로고
    • Mortalin and DJ-1 coordinately regulate hematopoietic stem cell function through the control of oxidative stress
    • Tai-Nagara, I.; Matsuoka, S.; Ariga, H.; Suda, T. Mortalin and DJ-1 coordinately regulate hematopoietic stem cell function through the control of oxidative stress Blood 2014, 123, 41-50 10.1182/blood-2013-06-508333
    • (2014) Blood , vol.123 , pp. 41-50
    • Tai-Nagara, I.1    Matsuoka, S.2    Ariga, H.3    Suda, T.4
  • 72
    • 84879562737 scopus 로고    scopus 로고
    • The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation
    • Uzarska, M. A.; Dutkiewicz, R.; Freibert, S. A.; Lill, R.; Muhlenhoff, U. The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation Mol. Biol. Cell 2013, 24, 1830-1841 10.1091/mbc.E12-09-0644
    • (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
  • 73
    • 33646342998 scopus 로고    scopus 로고
    • The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p
    • Dutkiewicz, R.; Marszalek, J.; Schilke, B.; Craig, E. A.; Lill, R.; Muhlenhoff, U. The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p J. Biol. Chem. 2006, 281, 7801-7808 10.1074/jbc.M513301200
    • (2006) J. Biol. Chem. , vol.281 , pp. 7801-7808
    • Dutkiewicz, R.1    Marszalek, J.2    Schilke, B.3    Craig, E.A.4    Lill, R.5    Muhlenhoff, U.6
  • 74
    • 0033587716 scopus 로고    scopus 로고
    • TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions
    • Syken, J.; De-Medina, T.; Munger, K. TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions Proc. Natl. Acad. Sci. U. S. A. 1999, 96, 8499-8504 10.1073/pnas.96.15.8499
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8499-8504
    • Syken, J.1    De-Medina, T.2    Munger, K.3
  • 76
    • 84864517463 scopus 로고    scopus 로고
    • Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinsons disease
    • Goswami, A. V.; Samaddar, M.; Sinha, D.; Purushotham, J.; DSilva, P. Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinsons disease Hum. Mol. Genet. 2012, 21, 3317-3332 10.1093/hmg/dds162
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 3317-3332
    • Goswami, A.V.1    Samaddar, M.2    Sinha, D.3    Purushotham, J.4    Dsilva, P.5
  • 77
    • 78649309029 scopus 로고    scopus 로고
    • The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
    • Sharma, S. K.; De los Rios, P.; Christen, P.; Lustig, A.; Goloubinoff, P. The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase Nat. Chem. Biol. 2010, 6, 914-920 10.1038/nchembio.455
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 914-920
    • Sharma, S.K.1    De Los Rios, P.2    Christen, P.3    Lustig, A.4    Goloubinoff, P.5
  • 78
    • 84858955705 scopus 로고    scopus 로고
    • Reactivation of protein aggregates by mortalin and Tid1 - The human mitochondrial Hsp70 chaperone system
    • Iosefson, O.; Sharon, S.; Goloubinoff, P.; Azem, A. Reactivation of protein aggregates by mortalin and Tid1 - the human mitochondrial Hsp70 chaperone system Cell Stress Chaperones 2012, 17, 57-66 10.1007/s12192-011-0285-3
    • (2012) Cell Stress Chaperones , vol.17 , pp. 57-66
    • Iosefson, O.1    Sharon, S.2    Goloubinoff, P.3    Azem, A.4
  • 79
    • 77953230037 scopus 로고    scopus 로고
    • Deletion of PaAif2 and PaAmid2, two genes encoding mitochondrial AIF-like oxidoreductases of Podospora anserina, leads to increased stress tolerance and lifespan extension
    • Brust, D.; Hamann, A.; Osiewacz, H. D. Deletion of PaAif2 and PaAmid2, two genes encoding mitochondrial AIF-like oxidoreductases of Podospora anserina, leads to increased stress tolerance and lifespan extension Curr. Genet. 2010, 56, 225-235 10.1007/s00294-010-0295-1
    • (2010) Curr. Genet. , vol.56 , pp. 225-235
    • Brust, D.1    Hamann, A.2    Osiewacz, H.D.3
  • 81
    • 34248359155 scopus 로고    scopus 로고
    • MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity
    • Wiley, S. E.; Murphy, A. N.; Ross, S. A.; van der Geer, P.; Dixon, J. E. MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 5318-5323 10.1073/pnas.0701078104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5318-5323
    • Wiley, S.E.1    Murphy, A.N.2    Ross, S.A.3    Van Der Geer, P.4    Dixon, J.E.5
  • 83
    • 84894065572 scopus 로고    scopus 로고
    • Mitoneet mediates TNFalpha-induced necroptosis promoted by exposure to fructose and ethanol
    • Shulga, N.; Pastorino, J. G. Mitoneet mediates TNFalpha-induced necroptosis promoted by exposure to fructose and ethanol J. Cell Sci. 2014, 127, 896-907 10.1242/jcs.140764
    • (2014) J. Cell Sci. , vol.127 , pp. 896-907
    • Shulga, N.1    Pastorino, J.G.2
  • 84
    • 84892927300 scopus 로고    scopus 로고
    • Human apurinic/apyrimidinic endonuclease 1
    • Li, M.; Wilson, D. M., III Human apurinic/apyrimidinic endonuclease 1 Antioxid. Redox Signaling 2014, 20, 678-707 10.1089/ars.2013.5492
    • (2014) Antioxid. Redox Signaling , vol.20 , pp. 678-707
    • Li, M.1    Wilson, D.M.2
  • 86
    • 77956615040 scopus 로고    scopus 로고
    • Decisive role of apurinic/apyrimidinic endonuclease/Ref-1 in initiation of cell death
    • Cho, K. J.; Kim, H. J.; Park, S. C.; Kim, H. W.; Kim, G. W. Decisive role of apurinic/apyrimidinic endonuclease/Ref-1 in initiation of cell death Mol. Cell. Neurosci. 2010, 45, 267-276 10.1016/j.mcn.2010.07.001
    • (2010) Mol. Cell. Neurosci. , vol.45 , pp. 267-276
    • Cho, K.J.1    Kim, H.J.2    Park, S.C.3    Kim, H.W.4    Kim, G.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.