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Volumn 78, Issue 6, 2010, Pages 1594-1600

Structure of human CLIC3 at Åresolution

Author keywords

CLIC3; Crystallography; Glutathione transferase; GST; X ray

Indexed keywords

CHLORIDE CHANNEL; CHLORIDE CHANNEL CLIC3; COMPLEMENTARY DNA; MITOGEN ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 77951235871     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22675     Document Type: Article
Times cited : (22)

References (36)
  • 1
    • 62549164694 scopus 로고    scopus 로고
    • Chloride intracellular channel protein-4 functions in angiogenesis by supporting acidification of vacuoles along the intracellular tubulogenic pathway
    • Ulmasov B, Bruno J, Gordon N, Hartnett ME, Edwards JC. Chloride intracellular channel protein-4 functions in angiogenesis by supporting acidification of vacuoles along the intracellular tubulogenic pathway. Am. J Pathol 2009;174:1084-1096.
    • (2009) Am. J Pathol , vol.174 , pp. 1084-1096
    • Ulmasov, B.1    Bruno, J.2    Gordon, N.3    Hartnett, M.E.4    Edwards, J.C.5
  • 3
    • 0034646626 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel chloride intracellular channel-related protein, parchorin, expressed in water-secreting cells
    • DOI 10.1074/jbc.275.15.11164
    • Nishizawa. T, Nagao T, Iwatsubo T, Forte JG, Urushidani. T. Molecular cloning and characterization of a novel chloride intracellular channel-related protein, parchorin, expressed in water-secreting cells. J Biol Chem 2000(275:11164-11173. (Pubitemid 30212760)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 11164-11173
    • Nishizawa, T.1    Nagao, T.2    Iwatsubo, T.3    Forte, J.G.4    Urushidani, T.5
  • 4
    • 0040737617 scopus 로고    scopus 로고
    • P53 and tumor necrosis factor α regulate the expression of a mitochondrial chloride channel protein
    • DOI 10.1074/jbc.274.51.36488
    • Fernandez-Salas E, Sagar M, Cheng C, Yuspa SH, Weinberg WC. p53 and tumor necrosis factor alpha regulate the expression of a mitochondrial chloride channel protein. J Biol Chem 1999(274: 36488-36497. (Pubitemid 30005257)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.51 , pp. 36488-36497
    • Fernandez-Salas, E.1    Sagar, M.2    Cheng, C.3    Yuspa, S.H.4    Weinberg, W.C.5
  • 5
    • 0345731467 scopus 로고    scopus 로고
    • A C. elegans CLIC-like protein required for intracellular tube formation and maintenance
    • Berry KL, Bulow HE, Hall DH, Hobert O. A C. elegans CLIC-like protein required for intracellular tube formation and maintenance. Science 2003;302:2134-2137.
    • (2003) Science , vol.302 , pp. 2134-2137
    • Berry, K.L.1    Bulow, H.E.2    Hall, D.H.3    Hobert, O.4
  • 6
    • 0030802421 scopus 로고    scopus 로고
    • Characterization of the osteoclast ruffled border chloride channel and its role in bone resorption
    • Schlesinger PH, Blair HC, Teitelbaum SL, Edwards JC. Characterization of the osteoclast ruffled border chloride channel and its role in bone resorption. J Biol Chem 1997;272:18636-18643.
    • (1997) J Biol Chem , vol.272 , pp. 18636-18643
    • Schlesinger, P.H.1    Blair, H.C.2    Teitelbaum, S.L.3    Edwards, J.C.4
  • 8
    • 0024393477 scopus 로고
    • Purification and reconstitution of chloride channels from kidney and trachea
    • Landry DW, Akabas MH, Redhead C, Edelman A, Cragoe EJ, Jr, AlAwqati Q, Purification and reconstitution of chloride channels from, kidney and trachea. Science .1989;244:1469-1472. (Pubitemid 19171679)
    • (1989) Science , vol.244 , Issue.4911 , pp. 1469-1472
    • Landry, D.W.1    Akabas, M.H.2    Redhead, C.3    Edelman, A.4    Cragoe Jr., E.J.5    Al-Awqati, Q.6
  • 9
    • 0026576591 scopus 로고
    • A ubiquitous 64-kDa protein is a component of a chloride channel of plasma, and intracellular membranes
    • Redhead CR, Edelman. AE, Brown D, Landry DW, al-Awqati Q. A ubiquitous 64-kDa protein is a component of a chloride channel of plasma, and intracellular membranes. Proc Natl Acad Sei USA. 1992;89:3716-3720.
    • (1992) Proc Natl Acad Sei USA. , vol.89 , pp. 3716-3720
    • Redhead, C.R.1    Edelman, A.E.2    Brown, D.3    Landry, D.W.4    Al-Awqati, Q.5
  • 13
    • 33847047801 scopus 로고    scopus 로고
    • CLIC4 (p64H1) and its putative transmembrane domain form poorly selective, redox-regulated ion channels
    • Singh H, Ashley RH. CLIC4 (p64H1) and its putative transmembrane domain form poorly selective, redox-regulated ion channels. Mol Membr Biol. 2007(24:41-52.
    • (2007) Mol Membr Biol. , vol.24 , pp. 41-52
    • Singh, H.1    Ashley, R.H.2
  • 14
    • 0036087412 scopus 로고    scopus 로고
    • CLIC1 inserts from the aqueous phase into phospholipid membranes, where it functions as an anion channel
    • TuIk BM, Kapadia S, Edwards JC. CLICl inserts from the aqueous phase into phospholipid membranes, where it functions as an anion channel. Am J Physiol Cell Physiol 2002;282:C1103-C1112. (Pubitemid 34663119)
    • (2002) American Journal of Physiology - Cell Physiology , vol.282
    • Tulk, B.M.1    Kapadia, S.2    Edwards, J.C.3
  • 16
    • 0033555610 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a mitogen-activated protein kinase-associated intracellular chloride channel
    • Qian Z, Okuhara D, Abe MK, Rosner MR. Molecular cloning and characterization of a mitogen-activated protein kinase-associated intracellular chloride channel. J Biol Chem 1999;274:1621-1627. (Pubitemid 129507755)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.3 , pp. 1621-1627
    • Qian, Z.1    Okuhara, D.2    Abe, M.K.3    Rosner, M.R.4
  • 18
    • 0026669302 scopus 로고
    • Characterization of squid crystallin genes. Comparison with mammalian glutathione-S-transferase genes
    • Tomarev SI, Zinovieva RD, Piatigorsky J. Characterization of squid crystallin genes. Comparison with mammalian glutathione-S-transferase genes. J Biol Chem 1992;267:8604-8612.
    • (1992) J Biol Chem , vol.267 , pp. 8604-8612
    • Tomarev, S.I.1    Zinovieva, R.D.2    Piatigorsky, J.3
  • 19
    • 0035943609 scopus 로고    scopus 로고
    • The folding and stability of human alpha class glutathione transferase a1-1 depend on distinct roles of a conserved n-capping box and hydrophobic staple motif
    • DOI 10.1074/jbc.M104057200
    • Coceo R, Stenberg G, Dragani B, Rossi Principe D, Paludi D, Mannervik B, Aceto A. The folding and stability of human alpha class glutathione transferase Al-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif. J Biol Chem 2001;276:32177-32183. (Pubitemid 37384880)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.34 , pp. 32177-32183
    • Cocco, R.1    Stenberg, G.2    Dragani, B.3    Principe, D.R.4    Paludi, D.5    Mannervik, B.6    Aceto, A.7
  • 21
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53(Part 3):240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 25
    • 0035919812 scopus 로고    scopus 로고
    • Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutethione-S-transferases
    • Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ. Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutethione-S-transferases. J Mol Biol 2001;310:907-918.
    • (2001) J Mol Biol , vol.310 , pp. 907-918
    • Xia, B.1    Vlamis-Gardikas, A.2    Holmgren, A.3    Wright, P.E.4    Dyson, H.J.5
  • 26
    • 30144438819 scopus 로고    scopus 로고
    • Characterization of the omega class of glutathione transferases
    • DOI 10.1016/S0076-6879(05)01005-0, PII S0076687905010050, 5, Gluthione Transferases and Gamma-Glutamyl Transpeptidases
    • Whitbread AK, Masoumi A, Tetlow N, Schmuck E, Coggan M, Board PG. Characterization of the omega class of glutathione transferases. Methods Enzymol 2005;401:78-99. (Pubitemid 43052387)
    • (2005) Methods in Enzymology , vol.401 , pp. 78-99
    • Whitbread, A.K.1    Masoumi, A.2    Tetlow, N.3    Schmuck, E.4    Coggan, M.5    Board, P.G.6
  • 28
    • 0035852844 scopus 로고    scopus 로고
    • Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity
    • DOI 10.1021/bi002249z
    • Polekhina G, Board PG, Blackburn AC, Parker MW. Crystal structure of maleyiacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry 2001;40:1567-1576. (Pubitemid 32144025)
    • (2001) Biochemistry , vol.40 , Issue.6 , pp. 1567-1576
    • Polekhina, G.1    Board, P.G.2    Blackburn, A.C.3    Parker, M.W.4
  • 29
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • Bousset L, Belrhali H, Janin J, Melki R, Morera S. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 2001;9:39-46.
    • (2001) Structure , vol.9 , pp. 39-46
    • Bousset, L.1    Belrhali, H.2    Janin, J.3    Melki, R.4    Morera, S.5
  • 31
    • 33749364627 scopus 로고    scopus 로고
    • The origami of thioredoxin-like folds
    • Pan JL, Bardwell JC. The origami of thioredoxin-like folds. Protein Sci 2006;15:2217-2227.
    • (2006) Protein Sci , vol.15 , pp. 2217-2227
    • Pan, J.L.1    Bardwell, J.C.2
  • 33
    • 40549090930 scopus 로고    scopus 로고
    • The crystal structure of human chloride intracellular channel protein 2: A disulfide bond with functional implications
    • DOI 10.1002/prot.21922
    • Mi W, Liang YH, Li L, Su XD. The crystal structure of human chloride intracellular channel protein 2: a disulfide bond with functional implications. Proteins 2008;71:509-513. (Pubitemid 351358629)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.1 , pp. 509-513
    • Mi, W.1    Liang, Y.-H.2    Li, L.3    Su, X.-D.4
  • 35
    • 33646058007 scopus 로고    scopus 로고
    • Trimeric structure of the wild, soluble chloride intracellular ion channel CL1C4 observed in crystals
    • Li Y, Li D, Zeng Z, Wang D. Trimeric structure of the wild, soluble chloride intracellular ion channel CL1C4 observed in crystals. Biochem Biophys Res Commun 2006;343:1272-1278.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 1272-1278
    • Li, Y.1    Li, D.2    Zeng, Z.3    Wang, D.4
  • 36
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinei E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007;372:774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.