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Volumn 288, Issue 7, 2013, Pages 4819-4830

Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding

Author keywords

[No Author keywords available]

Indexed keywords

CRYO-ELECTRON MICROSCOPY; HIGH AFFINITY BINDING; MULTIMODES; MULTIPLE MODES; N-TERMINALS; NON-NATIVE; SMALL HEAT SHOCK PROTEINS; STRUCTURAL BASIS; STRUCTURAL CHANGE; SUBSTRATE BINDING; T4 LYSOZYME;

EID: 84874101818     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.388132     Document Type: Article
Times cited : (35)

References (55)
  • 1
    • 84858003372 scopus 로고    scopus 로고
    • Small heat shock proteins and α-crystallins. Dynamic proteins with flexible functions
    • Basha, E., O'Neill, H., and Vierling, E. (2012) Small heat shock proteins and α-crystallins. Dynamic proteins with flexible functions. Trends Biochem. Sci. 37, 106-117
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 106-117
    • Basha, E.1    O'Neill, H.2    Vierling, E.3
  • 2
    • 66149117827 scopus 로고    scopus 로고
    • Structure and mechanism of protein stability sensors. Chaperone activity of small heat shock proteins
    • McHaourab, H. S., and Godar., J. A., and Stewart, P. L. (2009) Structure and mechanism of protein stability sensors. Chaperone activity of small heat shock proteins. Biochemistry 48, 3828-3837
    • (2009) Biochemistry , vol.48 , pp. 3828-3837
    • McHaourab, H.S.1    Godar, J.A.2    Stewart, P.L.3
  • 4
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human α crystallin gene CRYAA
    • Litt, M., Kramer, P., LaMorticella, D. M., Murphey, W., and Lovrien., E. W., and Weleber, R. G. (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human α crystallin gene CRYAA. Hum. Mol. Genet. 7, 471-474
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 7
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • Haley, D. A., and Bova., M. P., Huang, Q. L., Mchaourab, H. S., and Stewart, P. L. (2000) Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J. Mol. Biol. 298, 261-272
    • (2000) J. Mol. Biol. , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    Mchaourab, H.S.4    Stewart, P.L.5
  • 8
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim, K. K., Kim, R., and Kim, S. H. (1998) Crystal structure of a small heat-shock protein. Nature 394, 595-599
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 9
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, aB-crystallin, has a variable quaternary structure
    • Haley, D. A., Horwitz, J., and Stewart, P. L. (1998) The small heat-shock protein, aB-crystallin, has a variable quaternary structure. J. Mol. Biol. 277, 27-35
    • (1998) J. Mol. Biol. , vol.277 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 11
    • 0033607618 scopus 로고    scopus 로고
    • Folding pattern of the α-crystallin domain in aA-crystallin determined by site-directed spin labeling
    • Koteiche, H. A., and Mchaourab, H. S. (1999) Folding pattern of the α-crystallin domain in aA-crystallin determined by site-directed spin labeling. J. Mol. Biol. 294, 561-577
    • (1999) J. Mol. Biol. , vol.294 , pp. 561-577
    • Koteiche, H.A.1    Mchaourab, H.S.2
  • 12
  • 14
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the α-crystallin-small heat-shock protein superfamily
    • de Jong, W. W., Caspers, G.J., and Leunissen, J. A. (1998) Genealogy of the α-crystallin-small heat-shock protein superfamily. Int. J. Biol. Macromol. 22, 151-162
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • De Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 15
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones
    • Van Montfort, R., Slingsby, C, and Vierling, E. (2001) Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. Adv. Protein Chem. 59, 105-156
    • (2001) Adv. Protein Chem. , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 16
    • 84862905389 scopus 로고    scopus 로고
    • Crystal structure of an activated variant of small heat shock protein hsp16.5
    • McHaourab, H. S., Lin, Y., and Spiller, B. W. (2012) Crystal structure of an activated variant of small heat shock protein Hsp16.5. Biochemistry 25, 5105-5112
    • (2012) Biochemistry , vol.25 , pp. 5105-5112
    • McHaourab, H.S.1    Lin, Y.2    Spiller, B.W.3
  • 17
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee, G. J., and Roseman., A. M., Saibil, H. R., and Vierling, E. (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBOJ. 16, 659-671
    • (1997) EMBOJ , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 18
    • 0037174851 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by aA-crystallin
    • Mchaourab, H. S., and Dodson., E. K., and Koteiche, H. A. (2002) Mechanism of chaperone function in small heat-shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by aA-crystallin. J. Biol. Chem. 277, 40557-40566
    • (2002) J. Biol. Chem. , vol.277 , pp. 40557-40566
    • Mchaourab, H.S.1    Dodson, E.K.2    Koteiche, H.A.3
  • 19
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins. Dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme
    • Shashidharamurthy, R., and Koteiche., H. A., Dong, J., and McHaourab, H. S. (2005) Mechanism of chaperone function in small heat shock proteins. Dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme. J. Biol. Chem. 280, 5281-5289
    • (2005) J. Biol. Chem. , vol.280 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 21
    • 0242582458 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to aB-crystallin
    • Sathish, H. A., and Stein., R. A., Yang, G., and Mchaourab, H. S. (2003) Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to aB-crystallin. J. Biol. Chem. 278, 44214-44221
    • (2003) J. Biol. Chem. , vol.278 , pp. 44214-44221
    • Sathish, H.A.1    Stein, R.A.2    Yang, G.3    Mchaourab, H.S.4
  • 22
    • 33744903422 scopus 로고    scopus 로고
    • Mechanism of a hereditary cataract phenotype. Mutations in aA-crystallin activate substrate binding
    • Koteiche, H. A., and Mchaourab, H. S. (2006) Mechanism of a hereditary cataract phenotype. Mutations in aA-crystallin activate substrate binding. J. Biol. Chem. 281, 14273-14279
    • (2006) J. Biol. Chem. , vol.281 , pp. 14273-14279
    • Koteiche, H.A.1    Mchaourab, H.S.2
  • 23
    • 0038193547 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in aB-crystallin
    • Koteiche, H. A., and McHaourab, H. S. (2003) Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in aB-crystallin. J. Biol. Chem. 278, 10361-10367
    • (2003) J. Biol. Chem. , vol.278 , pp. 10361-10367
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 24
    • 33846019666 scopus 로고    scopus 로고
    • Cryoelectron microscopy and EPR analysis of engineered symmetric and poly-disperse hsp16.5 assemblies reveals determinants of polydispersity and substrate binding
    • Shi, J., and Koteiche., H. A., McHaourab, H. S., and Stewart, P. L. (2006) Cryoelectron microscopy and EPR analysis of engineered symmetric and poly-disperse Hsp16.5 assemblies reveals determinants of polydispersity and substrate binding. J. Biol. Chem. 281, 40420-40428
    • (2006) J. Biol. Chem. , vol.281 , pp. 40420-40428
    • Shi, J.1    Koteiche, H.A.2    McHaourab, H.S.3    Stewart, P.L.4
  • 25
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin. A structural and kinetic spectroscopic study
    • Carver, J. A., and Lindner., R. A., Lyon, C, Canet, D., Hernandez, H., Dobson, C. M., and Redfield, C. (2002) The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin. A structural and kinetic spectroscopic study. J. Mol. Biol. 318, 815-827
    • (2002) J. Mol. Biol. , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 26
    • 0034739275 scopus 로고    scopus 로고
    • The small heat-shock chaperone protein, α-crystallin, does not recognize stable molten globule states of cytosolic proteins
    • Treweek, T. M., and Lindner., R. A., Mariani, M., and Carver, J. A. (2000) The small heat-shock chaperone protein, α-crystallin, does not recognize stable molten globule states of cytosolic proteins. Biochim. Biophys. Acta 1481, 175-188
    • (2000) Biochim. Biophys. Acta , vol.1481 , pp. 175-188
    • Treweek, T.M.1    Lindner, R.A.2    Mariani, M.3    Carver, J.A.4
  • 27
    • 55549133282 scopus 로고    scopus 로고
    • Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry
    • Cheng, G., Basha, E., Wysocki, V. H., and Vierling, E. (2008) Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem. 283, 26634-26642
    • (2008) J. Biol. Chem. , vol.283 , pp. 26634-26642
    • Cheng, G.1    Basha, E.2    Wysocki, V.H.3    Vierling, E.4
  • 28
    • 15844414479 scopus 로고    scopus 로고
    • Conformational properties of substrate proteins bound to a molecular chaperone α-crystallin
    • Das, K. P., and Petrash., J. M., and Surewicz, W. K. (1996) Conformational properties of substrate proteins bound to a molecular chaperone α-crystallin. J. Biol. Chem. 271, 10449-10452
    • (1996) J. Biol. Chem. , vol.271 , pp. 10449-10452
    • Das, K.P.1    Petrash, J.M.2    Surewicz, W.K.3
  • 29
    • 37449009967 scopus 로고    scopus 로고
    • Structure and orientation of T4 lysozyme bound to the small heat shock protein α-crystallin
    • Claxton, D. P., Zou, P., and Mchaourab, H. S. (2008) Structure and orientation of T4 lysozyme bound to the small heat shock protein α-crystallin. J. Mol. Biol. 375, 1026-1039
    • (2008) J. Mol. Biol. , vol.375 , pp. 1026-1039
    • Claxton, D.P.1    Zou, P.2    Mchaourab, H.S.3
  • 30
    • 27744485379 scopus 로고    scopus 로고
    • Interactive domains for chaperone activity in the small heat shock protein, human aB-crystallin
    • Ghosh, J. G., and Estrada., M. R., and Clark, J. I. (2005) Interactive domains for chaperone activity in the small heat shock protein, human aB-crystallin. Biochemistry 44, 14854-14869
    • (2005) Biochemistry , vol.44 , pp. 14854-14869
    • Ghosh, J.G.1    Estrada, M.R.2    Clark, J.I.3
  • 31
    • 14144255401 scopus 로고    scopus 로고
    • Insights into the domains required for dimerization and assembly of human aB-crystallin
    • Ghosh, J. G., and Clark, J. I. (2005) Insights into the domains required for dimerization and assembly of human aB-crystallin. Protein Sci. 14, 684-695
    • (2005) Protein Sci. , vol.14 , pp. 684-695
    • Ghosh, J.G.1    Clark, J.I.2
  • 32
    • 79953253901 scopus 로고    scopus 로고
    • Crystal structure of R120G disease mutant of human aB-crystallin domain dimer shows closure of a groove
    • Clark, A. R., and Naylor., C. E., Bagnéris, C, Keep, N. H., and Slingsby, C. (2011) Crystal structure of R120G disease mutant of human aB-crystallin domain dimer shows closure of a groove. J. Mol. Biol. 408, 118-134
    • (2011) J. Mol. Biol. , vol.408 , pp. 118-134
    • Clark, A.R.1    Naylor, C.E.2    Bagnéris, C.3    Keep, N.H.4    Slingsby, C.5
  • 33
    • 33846018601 scopus 로고    scopus 로고
    • The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity
    • Basha, E., and Friedrich., K. L., and Vierling, E. (2006) The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity. J. Biol. Chem. 281, 39943-39952
    • (2006) J. Biol. Chem. , vol.281 , pp. 39943-39952
    • Basha, E.1    Friedrich, K.L.2    Vierling, E.3
  • 34
    • 30044445875 scopus 로고    scopus 로고
    • Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity
    • Giese, K. C, Basha, E., Catague, B. Y., and Vierling, E. (2005) Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proc. Natl. Acad. Sci. U.S.A. 102, 18896-18901
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18896-18901
    • Giese, K.C.1    Basha, E.2    Catague, B.Y.3    Vierling, E.4
  • 35
    • 1642524277 scopus 로고    scopus 로고
    • Analysis of the regulation of the molecular chaperone hsp26 by temperature-induced dissociation. The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins
    • Stromer, T., Fischer, E., Richter, K., Haslbeck, M., and Buchner, J. (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation. The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins. J. Biol. Chem. 279, 11222-11228
    • (2004) J. Biol. Chem. , vol.279 , pp. 11222-11228
    • Stromer, T.1    Fischer, E.2    Richter, K.3    Haslbeck, M.4    Buchner, J.5
  • 36
    • 0038043235 scopus 로고    scopus 로고
    • Analysis of the interaction of small heat shock proteins with unfolding proteins
    • Stromer, T., Ehrnsperger, M., Gaestel, M., and Buchner, J. (2003) Analysis of the interaction of small heat shock proteins with unfolding proteins. J. Biol. Chem. 278, 18015-18021
    • (2003) J. Biol. Chem. , vol.278 , pp. 18015-18021
    • Stromer, T.1    Ehrnsperger, M.2    Gaestel, M.3    Buchner, J.4
  • 37
    • 0037157161 scopus 로고    scopus 로고
    • The determinants of the oligomeric structure in hsp16.5 are encoded in the α-crystallin domain
    • Koteiche, H. A., and Mchaourab, H. S. (2002) The determinants of the oligomeric structure in Hsp16.5 are encoded in the α-crystallin domain. FEBSLett. 519, 16-22
    • (2002) FEBSLett. , vol.519 , pp. 16-22
    • Koteiche, H.A.1    Mchaourab, H.S.2
  • 38
    • 0030741276 scopus 로고    scopus 로고
    • Structure and function of the conserved domain in aA-crystallin. Site-directed spin labeling identifies a β-strand located near a subunit interface
    • Berengian, A. R., and Bova., M. P., and Mchaourab, H. S. (1997) Structure and function of the conserved domain in aA-crystallin. Site-directed spin labeling identifies a β-strand located near a subunit interface. Biochemistry 36, 9951-9957
    • (1997) Biochemistry , vol.36 , pp. 9951-9957
    • Berengian, A.R.1    Bova, M.P.2    Mchaourab, H.S.3
  • 39
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in aB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova, M. P., Yaron, O., Huang, Q., Ding, L., and Haley., D. A., Stewart, P. L., and Horwitz, J. (1999) Mutation R120G in aB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc. Natl. Acad. Sci. U.S.A. 96, 6137-6142
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 40
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H. S., and Lietzow., M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35, 7692-7704
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 41
    • 0033534145 scopus 로고    scopus 로고
    • Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane
    • Mansoor, S. E., and McHaourab., H. S., and Farrens, D. L. (1999) Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane. Biochemistry 38, 16383-16393
    • (1999) Biochemistry , vol.38 , pp. 16383-16393
    • Mansoor, S.E.1    McHaourab, H.S.2    Farrens, D.L.3
  • 42
    • 0033377664 scopus 로고    scopus 로고
    • EMAN. Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., and Baldwin., P. R., and Chiu, W. (1999) EMAN. Semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 43
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J. A., and Grigorieff, N. (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 45
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN. High resolution refinement of single particles structures
    • Grigorieff, N. (2007) FREALIGN. High resolution refinement of single particles structures. J. Struct. Biol. 157, 117-125
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 46
    • 0027435124 scopus 로고
    • Aggregation state of spin-labeled cecropin AD in solution
    • Mchaourab, H. S., and Hyde., J. S., and Feix, J. B. (1993) Aggregation state of spin-labeled cecropin AD in solution. Biochemistry 32, 11895-11902
    • (1993) Biochemistry , vol.32 , pp. 11895-11902
    • Mchaourab, H.S.1    Hyde, J.S.2    Feix, J.B.3
  • 47
    • 1942437441 scopus 로고    scopus 로고
    • Binding of destabilized βB2-crystallin mutants to α-crystallin. The role of a folding intermediate
    • Sathish, H. A., and Koteiche., H. A., and McHaourab, H. S. (2004) Binding of destabilized βB2-crystallin mutants to α-crystallin. The role of a folding intermediate. J. Biol. Chem. 279, 16425-16432
    • (2004) J. Biol. Chem. , vol.279 , pp. 16425-16432
    • Sathish, H.A.1    Koteiche, H.A.2    McHaourab, H.S.3
  • 48
    • 0038105331 scopus 로고    scopus 로고
    • Activation mechanism of HSP16.5 from methanococcus jannaschii
    • Kim, D. R., Lee, I., Ha, S. C, and Kim, K. K. (2003) Activation mechanism of HSP16.5 from Methanococcus jannaschii. Biochem. Biophys. Res. Commun. 307, 991-998
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 991-998
    • Kim, D.R.1    Lee, I.2    Ha, S.C.3    Kim, K.K.4
  • 50
    • 80855144806 scopus 로고    scopus 로고
    • Toward the fourth dimension of membrane protein structure. Insight into dynamics from spin-labeling EPR spectroscopy
    • McHaourab, H. S., and Steed., P. R., and Kazmier, K. (2011) Toward the fourth dimension of membrane protein structure. Insight into dynamics from spin-labeling EPR spectroscopy. Structure 19, 1549-1561
    • (2011) Structure , vol.19 , pp. 1549-1561
    • McHaourab, H.S.1    Steed, P.R.2    Kazmier, K.3
  • 51
    • 23444433904 scopus 로고    scopus 로고
    • Atomic models by cryo-EM and site-directed spin labeling. Applicationtothe N-terminal region of hsp16.5
    • Koteiche, H. A., Chiu, S., Majdoch, R. L., and Stewart., P. L., and Mchaourab, H. S. (2005) Atomic models by cryo-EM and site-directed spin labeling. Applicationtothe N-terminal region of Hsp16.5. Structure 13, 1165-1171
    • (2005) Structure , vol.13 , pp. 1165-1171
    • Koteiche, H.A.1    Chiu, S.2    Majdoch, R.L.3    Stewart, P.L.4    Mchaourab, H.S.5
  • 52
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot. The structure and function of small heat-shock proteins
    • Haslbeck, M., Franzmann, T., Weinfurtner, D., and Buchner, J. (2005) Some like it hot. The structure and function of small heat-shock proteins. Nat. Struct. Mol. Biol. 12, 842-846
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 53
    • 84856820287 scopus 로고    scopus 로고
    • Sequence, structure, and dynamic determinants of hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain
    • McDonald, E. T., Bortolus, M., Koteiche, H. A., and Mchaourab, H. S. (2012) Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain. Biochemistry 51, 1257-1268
    • (2012) Biochemistry , vol.51 , pp. 1257-1268
    • McDonald, E.T.1    Bortolus, M.2    Koteiche, H.A.3    Mchaourab, H.S.4
  • 54
    • 0037064015 scopus 로고    scopus 로고
    • Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from methanococcus jannaschii
    • Bova, M. P., Huang, Q., Ding, L., and Horwitz, J. (2002) Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. J. Biol. Chem. 277, 38468-38475
    • (2002) J. Biol. Chem. , vol.277 , pp. 38468-38475
    • Bova, M.P.1    Huang, Q.2    Ding, L.3    Horwitz, J.4


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