N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function.

[1]  Nicole R. Buan,et al.  The Identity of Proteins Associated with a Small Heat Shock Protein during Heat Stress in Vivo Indicates That These Chaperones Protect a Wide Range of Cellular Functions* , 2004, Journal of Biological Chemistry.

[2]  R. Stein,et al.  Mechanism of Chaperone Function in Small Heat-shock Proteins , 2003, Journal of Biological Chemistry.

[3]  J. Koretz,et al.  Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region. , 2003, Protein engineering.

[4]  P. Thampi,et al.  Influence of the C-Terminal Residues on Oligomerization of αA-Crystallin† , 2003 .

[5]  Y. Ha,et al.  Reinduced expression of developmental proteins (nestin, small heat shock protein) in and around cerebral arteriovenous malformations. , 2003, Clinical neuropathology.

[6]  B. Bukau,et al.  Refolding of Substrates Bound to Small Hsps Relies on a Disaggregation Reaction Mediated Most Efficiently by ClpB/DnaK* , 2003, Journal of Biological Chemistry.

[7]  L. Lai,et al.  On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[8]  D. Hilton,et al.  The clinicopathological spectrum of Rosenthal fibre encephalopathy and Alexander’s disease: a case report and review of the literature , 2003, Journal of neurology, neurosurgery, and psychiatry.

[9]  K. Shockley,et al.  Heat Shock Response by the Hyperthermophilic Archaeon Pyrococcus furiosus , 2003, Applied and Environmental Microbiology.

[10]  Péter Csermely,et al.  Apoptosis, necrosis and cellular senescence: chaperone occupancy as a potential switch , 2003, Aging cell.

[11]  V. Cryns,et al.  The Small Heat Shock Protein αB-crystallin Negatively Regulates Apoptosis during Myogenic Differentiation by Inhibiting Caspase-3 Activation* , 2002, The Journal of Biological Chemistry.

[12]  A. Valencia,et al.  p23 and HSP20/α‐crystallin proteins define a conserved sequence domain present in other eukaryotic protein families , 2002, FEBS letters.

[13]  M. Haslbeck.  sHsps and their role in the chaperone network , 2002, Cellular and Molecular Life Sciences CMLS.

[14]  J. Liao,et al.  C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine alphaB-crystallin. , 2002, Biochemical and biophysical research communications.

[15]  J. G. Guillemette,et al.  Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30. , 2002, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.

[16]  Christine Slingsby,et al.  Crystal structure and assembly of a eukaryotic small heat shock protein , 2001, Nature Structural Biology.

[17]  J. Koretz,et al.  Heat-induced quaternary transitions in hetero- and homo-polymers of alpha-crystallin. , 2001, Molecular vision.

[18]  S. Nakamura,et al.  The relationship between αB‐crystallin and neurofibrillary tangles in Alzheimer's disease , 2001 .

[19]  D. Svergun,et al.  A Novel Quaternary Structure of the Dimeric α-Crystallin Domain with Chaperone-like Activity* , 2001, The Journal of Biological Chemistry.

[20]  D. Toft,et al.  Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone* , 2000, The Journal of Biological Chemistry.

[21]  P. Stewart,et al.  Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. , 2000, Journal of molecular biology.

[22]  J. Koretz,et al.  Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature. , 2000, Biochemical and biophysical research communications.

[23]  V. Volloch,et al.  A natural extracellular factor that induces Hsp72, inhibits apoptosis, and restores stress resistance in aged human cells. , 1999, Experimental cell research.

[24]  H. Saibil,et al.  Hsp26: a temperature‐regulated chaperone , 1999, The EMBO journal.

[25]  W. W. Jong,et al.  The Molecular Chaperone aB-crystallin Enhances Amyloid Neurotoxicity , 1999 .

[26]  G. Bosman,et al.  Dementia, gliosis and expression of the small heat shock proteins hsp27 and alpha B-crystallin in Parkinson's disease. , 1999, Neuroreport.

[27]  Johannes Buchner,et al.  Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by Phosphorylation* , 1999, The Journal of Biological Chemistry.

[28]  A. Guimond,et al.  HSP27 Multimerization Mediated by Phosphorylation-sensitive Intermolecular Interactions at the Amino Terminus* , 1999, The Journal of Biological Chemistry.

[29]  P. Muchowski,et al.  AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress. , 1999, Investigative ophthalmology & visual science.

[30]  S H Kim,et al.  Small heat shock protein of Methanococcus jannaschii, a hyperthermophile. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[31]  J. Leunissen,et al.  Genealogy of the α-crystallin—small heat-shock protein superfamily , 1998 .

[32]  P. Stewart,et al.  The small heat-shock protein, αb-crystallin, has a variable quaternary structure , 1998 .

[33]  C. Almoguera,et al.  Dual regulation of a heat shock promoter during embryogenesis: stage-dependent role of heat shock elements. , 1998, The Plant Journal.

[34]  P. Mehlen,et al.  hsp27 as a Switch between Differentiation and Apoptosis in Murine Embryonic Stem Cells* , 1997, The Journal of Biological Chemistry.

[35]  M. Leroux,et al.  Structure-Function Studies on Small Heat Shock Protein Oligomeric Assembly and Interaction with Unfolded Polypeptides* , 1997, The Journal of Biological Chemistry.

[36]  M. Bova,et al.  Structure and Function of the Conserved Domain in αA-Crystallin. Site-Directed Spin Labeling Identifies a β-Strand Located near a Subunit Interface† , 1997 .

[37]  B. Chauffert,et al.  HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. , 1997, Cancer research.

[38]  Garrett J. Lee,et al.  A small heat shock protein stably binds heat‐denatured model substrates and can maintain a substrate in a folding‐competent state , 1997, The EMBO journal.

[39]  K. Schulze-Osthoff,et al.  Small Stress Proteins as Novel Regulators of Apoptosis , 1996, The Journal of Biological Chemistry.

[40]  B. Raman,et al.  Chaperone-like activity and quaternary structure of alpha-crystallin. , 1994, The Journal of biological chemistry.

[41]  J. Koretz,et al.  Biophysical characterization of α-crystallin aggregates : validation of the micelle hypothesis , 1992 .

[42]  J. Koretz,et al.  A possible structure for α‐crystallin , 1987 .

[43]  N. Gusev,et al.  Some properties of human small heat shock protein Hsp20 (HspB6). , 2004, European journal of biochemistry.

[44]  Garrett J. Lee,et al.  A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. , 2000, Plant physiology.

[45]  R. Mestril,et al.  Influence of phosphorylation and oligomerization on the protective role of the small heat shock protein 27 in rat adult cardiomyocytes. , 1999, Gene expression.

[46]  M. Bova,et al.  Lens alpha-crystallin: chaperone-like properties. , 1998, Methods in enzymology.