The determinants of the oligomeric structure in Hsp16.5 are encoded in the alpha-crystallin domain.

No abstract is available for this paper.

• Publication year

  2002

• Venue

  FEBS Letters

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  PMID 12023011
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts.

  2002cited by this paper
• Crystal structure and assembly of a eukaryotic small heat shock protein

  2001cited by this paper
• Subunit Exchange of Small Heat Shock Proteins

  2000cited by this paper
• Characterization of alpha-crystallin-plasma membrane binding.

  2000cited by this paper
• Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies.

  2000cited by this paper
• Site-directed spin labeling study of subunit interactions in the alpha-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in alphaA-crystallin, HSP 27, and HSP 16.3.

  1999cited by this paper
• Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling.

  1999cited by this paper
• A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy

  1998cited by this paper
• The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure.

  1998cited by this paper
• Crystal structure of a small heat-shock protein

  1998cited by this paper
• Recent advances in site-directed spin labeling of proteins.

  1998cited by this paper
• Genealogy of the alpha-crystallin--small heat-shock protein superfamily.

  1998cited by this paper
• A small heat shock protein stably binds heat‐denatured model substrates and can maintain a substrate in a folding‐competent state

  1997cited by this paper
• Subunit exchange of alphaA-crystallin.

  1997cited by this paper
• Structure and function of the conserved domain in alphaA-crystallin. Site-directed spin labeling identifies a beta-strand located near a subunit interface.

  1997cited by this paper
• Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the alpha-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface.

  1997cited by this paper
• Small Stress Proteins as Novel Regulators of Apoptosis

  1996cited by this paper
• Mycobacterium tuberculosis 16-kDa Antigen (Hsp16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation (*)

  1996cited by this paper
• The expanding small heat-shock protein family, and structure predictions of the conserved “α-crystallin domain”

  1995cited by this paper
• Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity.

  1994cited by this paper
• Evolution of the alpha-crystallin/small heat-shock protein family.

  1993cited by this paper
• The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins.

  1993cited by this paper
• Small heat shock proteins are molecular chaperones.

  1993cited by this paper
• Alpha-crystallin can function as a molecular chaperone.

  1992cited by this paper
• The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular-weight heat shock proteins

  1992cited by this paper
• Characterization of the major membrane protein of virulent Mycobacterium tuberculosis

  1992cited by this paper
• Alpha B-crystallin is a small heat shock protein.

  1991cited by this paper
• alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues.

  1989cited by this paper

• Cryo-EM structure of a 16.5-kDa small heat-shock protein from Methanocaldococcus jannaschii.

  2023cites this paper
• HspX promotes the polar localization of mycobacterial protein aggregates

  2019cites this paper
• Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity

  2018cites this paper
• Protein structure elucidation by combining computational and experimental methods

  2015cites this paper
• Hsp27 as a therapeutic target in cancers.

  2014cites this paper
• Small heat-shock proteins: paramedics of the cell.

  2013cites this paper
• Cryoelectron Microscopy Analysis of Small Heat Shock Protein 16.5 (Hsp16.5) Complexes with T4 Lysozyme Reveals the Structural Basis of Multimode Binding*

  2012cites this paper
• Crystal structure of an activated variant of small heat shock protein Hsp16.5.

  2012cites this paper
• Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain.

  2012cites this paper
• Biochemical Characterization and Evaluation of a Brugia malayi Small Heat Shock Protein as a Vaccine against Lymphatic Filariasis

  2012cites this paper
• Biologic Activities of Molecular Chaperones and Pharmacologic Chaperone Imidazole-Containing Dipeptide-Based Compounds: Natural Skin Care Help and the Ultimate Challenge. Implication for Adaptive Responses in the Skin

  2012cites this paper
• A survey and analysis of the role of molecular chaperone proteins and imidazole‐containing dipeptide‐based compounds as molecular escorts into the skin during stress, injury, water structuring and other types of cutaneous pathophysiology

  2011cites this paper
• RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

  2011cites this paper
• Roles of L5-7 loop in the structure and chaperone function of SsHSP14.1.

  2011cites this paper
• Water-structuring technology with the molecular chaperone proteins: indicated application of the α-crystallin domains and imidazole-containing peptidomimetics in cosmetic skin care systems or dermatological therapeutic drug carrier formulations.

  2011cites this paper
• Algorithm for selection of optimized EPR distance restraints for de novo protein structure determination.

  2011cites this paper
• Structure, Dynamics, and Substrate-induced Conformational Changes of the Multidrug Transporter EmrE in Liposomes*

  2010cites this paper
• Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization.

  2010cites this paper
• Investigation of the chaperone function of the small heat shock protein — AgsA

  2010cites this paper
• Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA.

  2009cites this paper
• The taming of small heat-shock proteins: crystallization of the alpha-crystallin domain from human Hsp27.

  2009cites this paper
• Disulfide cross‐links in the interaction of a cataract‐linked αA‐crystallin mutant with βB1‐crystallin

  2009cites this paper
• Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins.

  2009cites this paper
• Conformational cycle of the ABC transporter MsbA in liposomes: detailed analysis using double electron-electron resonance spectroscopy.

  2009cites this paper
• Alpha-crystallin.

  2008cites this paper
• Structural and functional roles for beta-strand 7 in the alpha-crystallin domain of p26, a polydisperse small heat shock protein from Artemia franciscana.

  2006cites this paper
• Cryoelectron Microscopy and EPR Analysis of Engineered Symmetric and Polydisperse Hsp16.5 Assemblies Reveals Determinants of Polydispersity and Substrate Binding*

  2006cites this paper
• Mechanism of a Hereditary Cataract Phenotype

  2006cites this paper
• Mechanism of Chaperone Function in Small Heat Shock Proteins

  2005cites this paper
• Structural instability caused by a mutation at a conserved arginine in the α-crystallin domain of Chinese hamster heat shock protein 27

  2005cites this paper
• Atomic models by cryo-EM and site-directed spin labeling: application to the N-terminal region of Hsp16.5.

  2005cites this paper
• A Dual Role for the N-terminal Region of Mycobacterium tuberculosis Hsp16.3 in Self-oligomerization and Binding Denaturing Substrate Proteins*

  2005cites this paper
• Small heat shock proteins: molecular structure and chaperone function

  2005cites this paper
• Insights into the domains required for dimerization and assembly of human αB crystallin

  2005cites this paper
• Essential Role of the NH2-terminal WD/EPF Motif in the Phosphorylation-activated Protective Function of Mammalian Hsp27*

  2004cites this paper
• Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-assembled via trimer and hexamer intermediates.

  2003cites this paper
• Multi-subunit assembly of the Pyrococcus furiosus small heat shock protein is essential for cellular protection at high temperature

  2003cites this paper
• Three-dimensional models corresponding to the C-terminal domain of human alphaA- and alphaB-crystallins based on the crystal structure of the small heat-shock protein HSP16.9 from wheat.

  2003cites this paper
• Activation mechanism of HSP16.5 from Methanococcus jannaschii.

  2003cites this paper
• On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii

  2003cites this paper
• Subunit Exchange, Conformational Stability, and Chaperone-like Function of the Small Heat Shock Protein 16.5 fromMethanococcus jannaschii *

  2002cites this paper
• Structure, function and evolution of small heat shock proteins

  2001cites this paper