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Volumn 1834, Issue 12, 2013, Pages 2502-2511

The interplay between protein stability and dynamics in conformational diseases: The case of hPGK1 deficiency

Author keywords

Conformational disease; Mutations; Protein stability; Proteolysis

Indexed keywords

PHOSPHOGLYCERATE KINASE; PHOSPHOGLYCERATE KINASE 1; STABILIZING AGENT; UNCLASSIFIED DRUG;

EID: 84884638405     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.07.011     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • W.E. Balch, R.I. Morimoto, A. Dillin, and J.W. Kelly Adapting proteostasis for disease intervention Science 319 2008 916 919 (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 3
    • 84874905513 scopus 로고    scopus 로고
    • Protein misfolding in disease and small molecule therapies
    • C.M. Gomes Protein misfolding in disease and small molecule therapies Curr. Top. Med. Chem. 12 2012 2460 2469
    • (2012) Curr. Top. Med. Chem. , vol.12 , pp. 2460-2469
    • Gomes, C.M.1
  • 5
    • 33845499042 scopus 로고    scopus 로고
    • PGK deficiency
    • DOI 10.1111/j.1365-2141.2006.06351.x
    • E. Beutler PGK deficiency Br. J. Haematol. 136 2007 3 11 (Pubitemid 44912583)
    • (2007) British Journal of Haematology , vol.136 , Issue.1 , pp. 3-11
    • Beutler, E.1
  • 6
    • 0023091937 scopus 로고
    • Human testis-specific PGK gene lacks introns and possesses characteristics of a processed gene
    • DOI 10.1038/326501a0
    • J.R. McCarrey, and K. Thomas Human testis-specific PGK gene lacks introns and possesses characteristics of a processed gene Nature 326 1987 501 505 (Pubitemid 17055493)
    • (1987) Nature , vol.326 , Issue.6112 , pp. 501-505
    • McCarrey, J.R.1    Thomas, K.2
  • 7
    • 0022339843 scopus 로고
    • Regional localization of the phosphoglycerate kinase gene and pseudogene on the human X chromosome and assignment of a related DNA sequence to chromosome 19
    • H.F. Willard, S.J. Goss, M.T. Holmes, and D.L. Munroe Regional localization of the phosphoglycerate kinase gene and pseudogene on the human X chromosome and assignment of a related DNA sequence to chromosome 19 Hum. Genet. 71 1985 138 143 (Pubitemid 16178880)
    • (1985) Human Genetics , vol.71 , Issue.2 , pp. 138-143
    • Willard, H.F.1    Goss, S.J.2    Holmes, M.T.3    Munroe, D.L.4
  • 9
    • 34247239927 scopus 로고    scopus 로고
    • Comparison of Proteolytic Susceptibility in Phosphoglycerate Kinases from Yeast and E. Coli: Modulation of Conformational Ensembles Without Altering Structure or Stability
    • DOI 10.1016/j.jmb.2007.02.077, PII S0022283607002823
    • T.A. Young, E. Skordalakes, and S. Marqusee Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability J. Mol. Biol. 368 2007 1438 1447 (Pubitemid 46617591)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1438-1447
    • Young, T.A.1    Skordalakes, E.2    Marqusee, S.3
  • 13
    • 84874101765 scopus 로고    scopus 로고
    • Structural and energetic basis of protein kinetic destabilization in human phosphoglycerate kinase 1 deficiency
    • A.L. Pey, N. Mesa-Torres, L.R. Chiarelli, and G. Valentini Structural and energetic basis of protein kinetic destabilization in human phosphoglycerate kinase 1 deficiency Biochemistry 52 2013 1160 1170
    • (2013) Biochemistry , vol.52 , pp. 1160-1170
    • Pey, A.L.1    Mesa-Torres, N.2    Chiarelli, L.R.3    Valentini, G.4
  • 14
    • 6344285316 scopus 로고    scopus 로고
    • Probing the high energy states in proteins by proteolysis
    • DOI 10.1016/j.jmb.2004.08.085, PII S002228360401085X
    • C. Park, and S. Marqusee Probing the high energy states in proteins by proteolysis J. Mol. Biol. 343 2004 1467 1476 (Pubitemid 39387837)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1467-1476
    • Park, C.1    Marqusee, S.2
  • 15
    • 77949607255 scopus 로고    scopus 로고
    • Proteolytic scanning calorimetry: A novel methodology that probes the fundamental features of protein kinetic stability
    • G. Tur-Arlandis, D. Rodriguez-Larrea, B. Ibarra-Molero, and J.M. Sanchez-Ruiz Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability Biophys. J. 98 2010 L12 14
    • (2010) Biophys. J. , vol.98 , pp. 12-14
    • Tur-Arlandis, G.1    Rodriguez-Larrea, D.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 16
    • 0031042332 scopus 로고    scopus 로고
    • Kinetic and thermodynamic thermal stabilities of ribonuclease a and ribonuclease b
    • DOI 10.1021/bi962723u
    • U. Arnold, and R. Ulbrich-Hofmann Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B Biochemistry 36 1997 2166 2172 (Pubitemid 27104708)
    • (1997) Biochemistry , vol.36 , Issue.8 , pp. 2166-2172
    • Arnold, U.1    Ulbrich-Hofmann, R.2
  • 17
    • 84862234517 scopus 로고    scopus 로고
    • Cystathionine beta-synthase mutants exhibit changes in protein unfolding: Conformational analysis of misfolded variants in crude cell extracts
    • A. Hnizda, V. Jurga, K. Rakova, and V. Kozich Cystathionine beta-synthase mutants exhibit changes in protein unfolding: conformational analysis of misfolded variants in crude cell extracts J. Inherit. Metab. Dis. 35 2012 469 477
    • (2012) J. Inherit. Metab. Dis. , vol.35 , pp. 469-477
    • Hnizda, A.1    Jurga, V.2    Rakova, K.3    Kozich, V.4
  • 19
    • 0030745849 scopus 로고    scopus 로고
    • Are there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme?
    • DOI 10.1021/bi9703305
    • B. Ibarra-Molero, and J.M. Sanchez-Ruiz Are there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme? Biochemistry 36 1997 9616 9624 (Pubitemid 27347003)
    • (1997) Biochemistry , vol.36 , Issue.31 , pp. 9616-9624
    • Ibarra-Molero, B.1    Sanchez-Ruiz, J.M.2
  • 20
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin
    • R.F. Greene Jr., and C.N. Pace Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin J. Biol. Chem. 249 1974 5388 5393
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, Jr.R.F.1    Pace, C.N.2
  • 22
    • 0023053749 scopus 로고
    • Unfolding rates of globular proteins determined by kinetics of proteolysis
    • T. Imoto, H. Yamada, and T. Ueda Unfolding rates of globular proteins determined by kinetics of proteolysis J. Mol. Biol. 190 1986 647 649
    • (1986) J. Mol. Biol. , vol.190 , pp. 647-649
    • Imoto, T.1    Yamada, H.2    Ueda, T.3
  • 23
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • J.K. Myers, C.N. Pace, and J.M. Scholtz Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding Protein Sci. 4 1995 2138 2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 24
    • 0035933338 scopus 로고    scopus 로고
    • The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins
    • DOI 10.1006/jmbi.2001.4726
    • S.T. Whitten, J.O. Wooll, R. Razeghifard, E.B. Garcia-Moreno, and V.J. Hilser The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins J. Mol. Biol. 309 2001 1165 1175 (Pubitemid 32623315)
    • (2001) Journal of Molecular Biology , vol.309 , Issue.5 , pp. 1165-1175
    • Whitten, S.T.1    Wooll, J.O.2    Razeghifard, R.3    Garcia-Moreno, E.B.4    Hilser, V.J.5
  • 25
    • 0039224962 scopus 로고
    • Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease
    • F.X. Schmid, R. Grafl, A. Wrba, and J.J. Beintema Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease Proc. Nat. Acad. Sci. U.S.A. 83 1986
    • (1986) Proc. Nat. Acad. Sci. U.S.A. , vol.83
    • Schmid, F.X.1    Grafl, R.2    Wrba, A.3    Beintema, J.J.4
  • 26
    • 0026516420 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1
    • T. Kiefhaber, and F.X. Schmid Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1 J. Mol. Biol. 224 1992 217 229
    • (1992) J. Mol. Biol. , vol.224 , pp. 217-229
    • Kiefhaber, T.1    Schmid, F.X.2
  • 27
    • 0026716622 scopus 로고
    • The slow-refolding step of phosphoglycerate kinase as monitored by pulse proteolysis
    • J.M. Betton, D. Missiakas, and J.M. Yon The slow-refolding step of phosphoglycerate kinase as monitored by pulse proteolysis Arch. Biochem. Biophys. 296 1992 95 101
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 95-101
    • Betton, J.M.1    Missiakas, D.2    Yon, J.M.3
  • 28
    • 0027082567 scopus 로고
    • Kinetic studies of the refolding of yeast phosphoglycerate kinase: Comparison with the isolated engineered domains
    • D. Missiakas, J.M. Betton, A. Chaffotte, P. Minard, and J.M. Yon Kinetic studies of the refolding of yeast phosphoglycerate kinase: comparison with the isolated engineered domains Protein Sci. 1 1992 1485 1493 (Pubitemid 23012613)
    • (1992) Protein Science , vol.1 , Issue.11 , pp. 1485-1493
    • Missiakas, D.1    Betton, J.-M.2    Chaffotte, A.3    Minard, P.4    Yon, J.M.5
  • 29
    • 84876593406 scopus 로고    scopus 로고
    • The how's and why's of protein folding intermediates
    • M. Tsytlonok, and L.S. Itzhaki The how's and why's of protein folding intermediates Arch. Biochem. Biophys. 531 2013 14 23
    • (2013) Arch. Biochem. Biophys. , vol.531 , pp. 14-23
    • Tsytlonok, M.1    Itzhaki, L.S.2
  • 34
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases
    • DOI 10.1002/(SICI)1097-0134(20000701)40:1<58::AID-PROT80>3.0.CO;2-M
    • I.M. Plaza del Pino, B. Ibarra-Molero, and J.M. Sanchez-Ruiz Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases Proteins 40 2000 58 70 (Pubitemid 30368582)
    • (2000) Proteins: Structure, Function and Genetics , vol.40 , Issue.1 , pp. 58-70
    • Plaza Del Pino, I.M.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3
  • 35
    • 77951977004 scopus 로고    scopus 로고
    • Protein kinetic stability
    • J.M. Sanchez-Ruiz Protein kinetic stability Biophys. Chem. 148 2010 1 15
    • (2010) Biophys. Chem. , vol.148 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 36
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
    • D.A. Parsell, and R.T. Sauer The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli J. Biol. Chem. 264 1989 7590 7595 (Pubitemid 19119177)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.13 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 37
    • 0029920369 scopus 로고    scopus 로고
    • Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala
    • P. Tougard, T.H. Le, P. Minard, M. Desmadril, J.M. Yon, T. Bizebard, G. Lebras, and C. Dumas Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala Protein Eng. 9 1996 181 187 (Pubitemid 26119299)
    • (1996) Protein Engineering , vol.9 , Issue.2 , pp. 181-187
    • Tougard, P.1    Le, T.H.2    Minard, P.3    Desmadril, M.4    Yon, J.M.5    Bizebard, T.6    Lebras, G.7    Dumas, C.8
  • 38
    • 84874929066 scopus 로고    scopus 로고
    • Phenylalanine hydroxylase misfolding and pharmacological chaperones
    • J. Underhaug, O. Aubi, and A. Martinez Phenylalanine hydroxylase misfolding and pharmacological chaperones Curr. Top. Med. Chem. 12 2012 2534 2545
    • (2012) Curr. Top. Med. Chem. , vol.12 , pp. 2534-2545
    • Underhaug, J.1    Aubi, O.2    Martinez, A.3
  • 39
    • 4344710278 scopus 로고    scopus 로고
    • Unfolding a folding disease: Folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II
    • DOI 10.1016/j.jmb.2004.07.024, PII S0022283604008514
    • K. Almstedt, M. Lundqvist, J. Carlsson, M. Karlsson, B. Persson, B.H. Jonsson, U. Carlsson, and P. Hammarstrom Unfolding a folding disease: folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II J. Mol. Biol. 342 2004 619 633 (Pubitemid 39149763)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.2 , pp. 619-633
    • Almstedt, K.1    Lundqvist, M.2    Carlsson, J.3    Karlsson, M.4    Persson, B.5    Jonsson, B.-H.6    Carlsson, U.7    Hammarstrom, P.8
  • 42
    • 84875457528 scopus 로고    scopus 로고
    • Localized structural fluctuations promote amyloidogenic conformations in transthyretin
    • K.H. Lim, H.J. Dyson, J.W. Kelly, and P.E. Wright Localized structural fluctuations promote amyloidogenic conformations in transthyretin J. Mol. Biol. 425 2013 977 988
    • (2013) J. Mol. Biol. , vol.425 , pp. 977-988
    • Lim, K.H.1    Dyson, H.J.2    Kelly, J.W.3    Wright, P.E.4
  • 43
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 44
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • F.U. Hartl, and M. Hayer-Hartl Converging concepts of protein folding in vitro and in vivo Nat. Struct. Mol. Biol. 16 2009 574 581
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 45
    • 33644546698 scopus 로고    scopus 로고
    • Native protein sequences are designed to destabilize folding intermediates
    • Y. Isogai Native protein sequences are designed to destabilize folding intermediates Biochemistry 45 2006 2488 2492
    • (2006) Biochemistry , vol.45 , pp. 2488-2492
    • Isogai, Y.1
  • 46
    • 52049112316 scopus 로고    scopus 로고
    • Increased folding stability of TEM-1 beta-lactamase by in vitro selection
    • I. Kather, R.P. Jakob, H. Dobbek, and F.X. Schmid Increased folding stability of TEM-1 beta-lactamase by in vitro selection J. Mol. Biol. 383 2008 238 251
    • (2008) J. Mol. Biol. , vol.383 , pp. 238-251
    • Kather, I.1    Jakob, R.P.2    Dobbek, H.3    Schmid, F.X.4
  • 47
    • 79954416821 scopus 로고    scopus 로고
    • Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases
    • D.S. Ong, and J.W. Kelly Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases Curr. Opin. Cell Biol. 23 2011 231 238
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 231-238
    • Ong, D.S.1    Kelly, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.