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Volumn 27, Issue 10, 2016, Pages 1556-1560

Engineering therapeutic protein disaggregases

Author keywords

[No Author keywords available]

Indexed keywords

1 ETHYL 2 [[3 ETHYL 5 (3 METHYLBENZOTHIAZOLIN 2 YLIDENE) 4 OXOTHIAZOLIDIN 2 YLIDENE]METHYL]PYRIDINIUM CHLORIDE; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PEPTIDES AND PROTEINS; PROTEIN DISAGGREGASE; UNCLASSIFIED DRUG; ALPHA SYNUCLEIN; DNA BINDING PROTEIN; HEAT SHOCK PROTEIN; PROTEIN AGGREGATE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84968608566     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E15-10-0693     Document Type: Review
Times cited : (43)

References (75)
  • 2
    • 77953083350 scopus 로고    scopus 로고
    • Directed evolution of the DnaK chaperone: Mutations in the lid domain result in enhanced chaperone activity
    • Aponte RA, Zimmermann S, Reinstein J (2010). Directed evolution of the DnaK chaperone: mutations in the lid domain result in enhanced chaperone activity. J Mol Biol 399, 154-167.
    • (2010) J Mol Biol , vol.399 , pp. 154-167
    • Aponte, R.A.1    Zimmermann, S.2    Reinstein, J.3
  • 6
    • 84956929136 scopus 로고    scopus 로고
    • UK scientists gain licence to edit genes in human embryos
    • Callaway E (2016). UK scientists gain licence to edit genes in human embryos. Nature 530, 18.
    • (2016) Nature , vol.530 , pp. 18
    • Callaway, E.1
  • 8
    • 66149085161 scopus 로고    scopus 로고
    • Identification of tubulins as substrates of serine protease HtrA1 by mixture-based oriented peptide library screening
    • Chien J, He X, Shridhar V (2009). Identification of tubulins as substrates of serine protease HtrA1 by mixture-based oriented peptide library screening. J Cell Biochem 107, 253-263.
    • (2009) J Cell Biochem , vol.107 , pp. 253-263
    • Chien, J.1    He, X.2    Shridhar, V.3
  • 10
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: Blurring the divide between transmissibility and infectivity
    • Cushman M, Johnson BS, King OD, Gitler AD, Shorter J (2010). Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 123, 1191-1201.
    • (2010) J Cell Sci , vol.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3    Gitler, A.D.4    Shorter, J.5
  • 13
    • 84855207518 scopus 로고    scopus 로고
    • The elusive middle domain of Hsp104 and ClpB: Location and function
    • DeSantis ME, Shorter J (2012). The elusive middle domain of Hsp104 and ClpB: location and function. Biochim Biophys Acta 1823, 29-39.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 29-39
    • DeSantis, M.E.1    Shorter, J.2
  • 15
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit R, Ross JL, Goldman YE, Holzbaur EL (2008). Differential regulation of dynein and kinesin motor proteins by tau. Science 319, 1086-1089.
    • (2008) Science , vol.319 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 16
    • 10944241135 scopus 로고    scopus 로고
    • Hsp70 gene transfer by adeno-associated virus inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease
    • Dong Z, Wolfer DP, Lipp HP, Bueler H (2005). Hsp70 gene transfer by adeno-associated virus inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease. Mol Ther 11, 80-88.
    • (2005) Mol Ther , vol.11 , pp. 80-88
    • Dong, Z.1    Wolfer, D.P.2    Lipp, H.P.3    Bueler, H.4
  • 17
    • 84913594397 scopus 로고    scopus 로고
    • Genome editing. The new frontier of genome engineering with CRISPR-Cas9
    • Doudna JA, Charpentier E (2014). Genome editing. The new frontier of genome engineering with CRISPR-Cas9. Science 346, 1258096.
    • (2014) Science , vol.346 , pp. 1258096
    • Doudna, J.A.1    Charpentier, E.2
  • 18
    • 84863683967 scopus 로고    scopus 로고
    • Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans
    • Duennwald ML, Echeverria A, Shorter J (2012). Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10, e1001346.
    • (2012) PLoS Biol , vol.10 , pp. e1001346
    • Duennwald, M.L.1    Echeverria, A.2    Shorter, J.3
  • 20
    • 84923370377 scopus 로고    scopus 로고
    • Metabolic and chaperone gene loss marks the origin of animals: Evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients
    • Erives AJ, Fassler JS (2015). Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients. PLoS One 10, e0117192.
    • (2015) PLoS One , vol.10 , pp. e0117192
    • Erives, A.J.1    Fassler, J.S.2
  • 21
    • 33845981507 scopus 로고    scopus 로고
    • Altered specificity of a AAA+ protease
    • Farrell CM, Baker TA, Sauer RT (2007). Altered specificity of a AAA+ protease. Mol Cell 25, 161-166.
    • (2007) Mol Cell , vol.25 , pp. 161-166
    • Farrell, C.M.1    Baker, T.A.2    Sauer, R.T.3
  • 23
    • 84966515280 scopus 로고    scopus 로고
    • Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/ HSP110 chaperones
    • Finka A, Sharma SK, Goloubinoff P (2015). Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/ HSP110 chaperones. Front Mol Biosci 2, 29.
    • (2015) Front Mol Biosci , vol.2 , pp. 29
    • Finka, A.1    Sharma, S.K.2    Goloubinoff, P.3
  • 26
    • 84866181145 scopus 로고    scopus 로고
    • Administration of recombinant heat shock protein 70 delays peripheral muscle denervation in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Gifondorwa DJ, Jimenz-Moreno R, Hayes CD, Rouhani H, Robinson MB, Strupe JL, Caress J, Milligan C (2012). Administration of recombinant heat shock protein 70 delays peripheral muscle denervation in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis. Neurol Res Int 2012, 170426.
    • (2012) Neurol Res Int , vol.2012 , pp. 170426
    • Gifondorwa, D.J.1    Jimenz-Moreno, R.2    Hayes, C.D.3    Rouhani, H.4    Robinson, M.B.5    Strupe, J.L.6    Caress, J.7    Milligan, C.8
  • 28
    • 37349072946 scopus 로고    scopus 로고
    • Beer and bread to brains and beyond: Can yeast cells teach us about neurodegenerative disease?
    • Gitler AD (2008). Beer and bread to brains and beyond: can yeast cells teach us about neurodegenerative disease? Neurosignals 16, 52-62.
    • (2008) Neurosignals , vol.16 , pp. 52-62
    • Gitler, A.D.1
  • 29
    • 80052802585 scopus 로고    scopus 로고
    • RNA-binding proteins with prion-like domains in ALS and FTLD-U
    • Gitler AD, Shorter J (2011). RNA-binding proteins with prion-like domains in ALS and FTLD-U. Prion 5, 179-187.
    • (2011) Prion , vol.5 , pp. 179-187
    • Gitler, A.D.1    Shorter, J.2
  • 31
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo JL, Lee VM (2014). Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med 20, 130-138.
    • (2014) Nat Med , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.2
  • 33
    • 84907558479 scopus 로고    scopus 로고
    • Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins
    • Jackrel ME, Shorter J (2014). Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins. Dis Model Mech 7, 1175-1184.
    • (2014) Dis Model Mech , vol.7 , pp. 1175-1184
    • Jackrel, M.E.1    Shorter, J.2
  • 34
    • 84937567559 scopus 로고    scopus 로고
    • Engineering enhanced protein disaggregases for neurodegenerative disease
    • Jackrel ME, Shorter J (2015). Engineering enhanced protein disaggregases for neurodegenerative disease. Prion 9, 90-109.
    • (2015) Prion , vol.9 , pp. 90-109
    • Jackrel, M.E.1    Shorter, J.2
  • 35
    • 84911458202 scopus 로고    scopus 로고
    • Isolating potentiated Hsp104 variants using yeast proteinopathy models
    • Jackrel ME, Tariq A, Yee K, Weitzman R, Shorter J (2014b). Isolating potentiated Hsp104 variants using yeast proteinopathy models. J Vis Exp 93, e52089.
    • (2014) J Vis Exp , vol.93 , pp. e52089
    • Jackrel, M.E.1    Tariq, A.2    Yee, K.3    Weitzman, R.4    Shorter, J.5
  • 36
    • 84951920497 scopus 로고    scopus 로고
    • Disparate mutations confer therapeutic gain of Hsp104 function
    • Jackrel ME, Yee K, Tariq A, Chen AI, Shorter J (2015). Disparate mutations confer therapeutic gain of Hsp104 function. ACS Chem Biol 10, 2672-2679.
    • (2015) ACS Chem Biol , vol.10 , pp. 2672-2679
    • Jackrel, M.E.1    Yee, K.2    Tariq, A.3    Chen, A.I.4    Shorter, J.5
  • 37
    • 84918536555 scopus 로고    scopus 로고
    • Protoporphyrins enhance oligomerization and enzymatic activity of HtrA1 serine protease
    • Jo H, Patterson V, Stoessel S, Kuan CY, Hoh J (2014). Protoporphyrins enhance oligomerization and enzymatic activity of HtrA1 serine protease. PLoS One 9, e115362.
    • (2014) PLoS One , vol.9 , pp. e115362
    • Jo, H.1    Patterson, V.2    Stoessel, S.3    Kuan, C.Y.4    Hoh, J.5
  • 38
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • Johnson BS, McCaffery JM, Lindquist S, Gitler AD (2008). A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc Natl Acad Sci USA 105, 6439-6444.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6439-6444
    • Johnson, B.S.1    McCaffery, J.M.2    Lindquist, S.3    Gitler, A.D.4
  • 39
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker M, Walker LC (2011). Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 70, 532-540.
    • (2011) Ann Neurol , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 40
    • 84930574272 scopus 로고    scopus 로고
    • Toward stem cell-based phenotypic screens for neurodegenerative diseases
    • Khurana V, Tardiff DF, Chung CY, Lindquist S (2015). Toward stem cell-based phenotypic screens for neurodegenerative diseases. Nat Rev Neurol 11, 339-350.
    • (2015) Nat Rev Neurol , vol.11 , pp. 339-350
    • Khurana, V.1    Tardiff, D.F.2    Chung, C.Y.3    Lindquist, S.4
  • 42
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King OD, Gitler AD, Shorter J (2012). The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res 1462, 61-80.
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 44
    • 51349150684 scopus 로고    scopus 로고
    • Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease
    • Lo Bianco C, Shorter J, Regulier E, Lashuel H, Iwatsubo T, Lindquist S, Aebischer P (2008). Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. J Clin Invest 118, 3087-3097.
    • (2008) J Clin Invest , vol.118 , pp. 3087-3097
    • Lo Bianco, C.1    Shorter, J.2    Regulier, E.3    Lashuel, H.4    Iwatsubo, T.5    Lindquist, S.6    Aebischer, P.7
  • 45
    • 84968670491 scopus 로고    scopus 로고
    • Engineering and evolution of molecular chaperones and protein disaggregases with enhanced activity
    • Mack KL, Shorter J (2016). Engineering and evolution of molecular chaperones and protein disaggregases with enhanced activity. Front Mol Biosci 3, 8.
    • (2016) Front Mol Biosci , vol.3 , pp. 8
    • Mack, K.L.1    Shorter, J.2
  • 46
    • 84962106306 scopus 로고    scopus 로고
    • Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease
    • S0006-8993(16)30096-8
    • March ZM, King OD, Shorter J (2016). Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease. Brain Res 2016, S0006-8993(16)30096-8.
    • (2016) Brain Res , vol.2016
    • March, Z.M.1    King, O.D.2    Shorter, J.3
  • 47
    • 84880515581 scopus 로고    scopus 로고
    • Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates
    • Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P (2013). Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem 288, 21399-21411.
    • (2013) J Biol Chem , vol.288 , pp. 21399-21411
    • Mattoo, R.U.1    Sharma, S.K.2    Priya, S.3    Finka, A.4    Goloubinoff, P.5
  • 48
    • 84879767467 scopus 로고    scopus 로고
    • Synthesis and initial evaluation of YM-08, a blood-brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces tau levels
    • Miyata Y, Li X, Lee HF, Jinwal UK, Srinivasan SR, Seguin SP, Young ZT, Brodsky JL, Dickey CA, Sun D, et al. (2013). Synthesis and initial evaluation of YM-08, a blood-brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces tau levels. ACS Chem Neurosci 4, 930-939.
    • (2013) ACS Chem Neurosci , vol.4 , pp. 930-939
    • Miyata, Y.1    Li, X.2    Lee, H.F.3    Jinwal, U.K.4    Srinivasan, S.R.5    Seguin, S.P.6    Young, Z.T.7    Brodsky, J.L.8    Dickey, C.A.9    Sun, D.10
  • 49
    • 80051720813 scopus 로고    scopus 로고
    • Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thioldisulfide interchange in the heme/substrate binding cleft
    • Morishima Y, Lau M, Peng HM, Miyata Y, Gestwicki JE, Pratt WB, Osawa Y (2011). Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thioldisulfide interchange in the heme/substrate binding cleft. Biochemistry 50, 7146-7156.
    • (2011) Biochemistry , vol.50 , pp. 7146-7156
    • Morishima, Y.1    Lau, M.2    Peng, H.M.3    Miyata, Y.4    Gestwicki, J.E.5    Pratt, W.B.6    Osawa, Y.7
  • 50
    • 42249103388 scopus 로고    scopus 로고
    • Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease
    • Nagel F, Falkenburger BH, Tonges L, Kowsky S, Poppelmeyer C, Schulz JB, Bahr M, Dietz GP (2008). Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease. J Neurochem 105, 853-864.
    • (2008) J Neurochem , vol.105 , pp. 853-864
    • Nagel, F.1    Falkenburger, B.H.2    Tonges, L.3    Kowsky, S.4    Poppelmeyer, C.5    Schulz, J.B.6    Bahr, M.7    Dietz, G.P.8
  • 53
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • Outeiro TF, Lindquist S (2003). Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 302, 1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 55
    • 84910031803 scopus 로고    scopus 로고
    • Targeting Hsp90/ Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases
    • Pratt WB, Gestwicki JE, Osawa Y, Lieberman AP (2015). Targeting Hsp90/ Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases. Annu Rev Pharmacol Toxicol 55, 353-371.
    • (2015) Annu Rev Pharmacol Toxicol , vol.55 , pp. 353-371
    • Pratt, W.B.1    Gestwicki, J.E.2    Osawa, Y.3    Lieberman, A.P.4
  • 58
    • 84875441083 scopus 로고    scopus 로고
    • The changing scene of amyotrophic lateral sclerosis
    • Robberecht W, Philips T (2013). The changing scene of amyotrophic lateral sclerosis. Nat Rev Neurosci 14, 248-264.
    • (2013) Nat Rev Neurosci , vol.14 , pp. 248-264
    • Robberecht, W.1    Philips, T.2
  • 60
    • 79959685900 scopus 로고    scopus 로고
    • Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding
    • Schweizer RS, Aponte RA, Zimmermann S, Weber A, Reinstein J (2011). Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding. Chembiochem 12, 1559-1573.
    • (2011) Chembiochem , vol.12 , pp. 1559-1573
    • Schweizer, R.S.1    Aponte, R.A.2    Zimmermann, S.3    Weber, A.4    Reinstein, J.5
  • 61
    • 80054699747 scopus 로고    scopus 로고
    • The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
    • Shorter J (2011). The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6, e26319.
    • (2011) PLoS One , vol.6 , pp. e26319
    • Shorter, J.1
  • 62
    • 84965057093 scopus 로고    scopus 로고
    • Chemical tools to investigate mechanisms associated with HSP90 and HSP70 in disease
    • Shrestha L, Patel HJ, Chiosis G (2016). Chemical tools to investigate mechanisms associated with HSP90 and HSP70 in disease. Cell Chem Biol 23, 158-172.
    • (2016) Cell Chem Biol , vol.23 , pp. 158-172
    • Shrestha, L.1    Patel, H.J.2    Chiosis, G.3
  • 63
    • 84928897102 scopus 로고    scopus 로고
    • Divergent evolution of a bifunctional de novo protein
    • Smith BA, Mularz AE, Hecht MH (2015). Divergent evolution of a bifunctional de novo protein. Protein Sci 24, 246-252.
    • (2015) Protein Sci , vol.24 , pp. 246-252
    • Smith, B.A.1    Mularz, A.E.2    Hecht, M.H.3
  • 65
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, Shorter J, Gitler AD (2011). Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol 9, e1000614.
    • (2011) PLoS Biol , vol.9 , pp. e1000614
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5    Shorter, J.6    Gitler, A.D.7
  • 66
    • 84964779274 scopus 로고    scopus 로고
    • Mechanistic and structural insights into the prion-disaggregase activity of Hsp104
    • S0022-2836(15)00678-6
    • Sweeny EA, Shorter J (2015). Mechanistic and structural insights into the prion-disaggregase activity of Hsp104. J Mol Biol 2015, S0022- 2836(15)00678-6.
    • (2015) J Mol Biol , vol.2015
    • Sweeny, E.A.1    Shorter, J.2
  • 68
    • 84876572472 scopus 로고    scopus 로고
    • The emerging roles of HTRA1 in musculoskeletal disease
    • Tiaden AN, Richards PJ (2013). The emerging roles of HTRA1 in musculoskeletal disease. Am J Pathol 182, 1482-1488.
    • (2013) Am J Pathol , vol.182 , pp. 1482-1488
    • Tiaden, A.N.1    Richards, P.J.2
  • 69
    • 84907833287 scopus 로고    scopus 로고
    • Suramin inhibits Hsp104 ATPase and disaggregase activity
    • Torrente MP, Castellano LM, Shorter J (2014). Suramin inhibits Hsp104 ATPase and disaggregase activity. PLoS One 9, e110115.
    • (2014) PLoS One , vol.9 , pp. e110115
    • Torrente, M.P.1    Castellano, L.M.2    Shorter, J.3
  • 71
    • 84893855426 scopus 로고    scopus 로고
    • The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins
    • Torrente MP, Shorter J (2013). The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins. Prion 7, 457-463.
    • (2013) Prion , vol.7 , pp. 457-463
    • Torrente, M.P.1    Shorter, J.2
  • 72
    • 27744491956 scopus 로고    scopus 로고
    • Pathological tau: A loss of normal function or a gain in toxicity?
    • Trojanowski JQ, Lee VM (2005). Pathological tau: a loss of normal function or a gain in toxicity? Nat Neurosci 8, 1136-1137.
    • (2005) Nat Neurosci , vol.8 , pp. 1136-1137
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 74
    • 0037184939 scopus 로고    scopus 로고
    • Directed evolution of substrate-optimized GroEL/S chaperonins
    • Wang JD, Herman C, Tipton KA, Gross CA, Weissman JS (2002). Directed evolution of substrate-optimized GroEL/S chaperonins. Cell 111, 1027-1039.
    • (2002) Cell , vol.111 , pp. 1027-1039
    • Wang, J.D.1    Herman, C.2    Tipton, K.A.3    Gross, C.A.4    Weissman, J.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.