Early folding events protect aggregation-prone regions of a β-rich protein.

No abstract is available for this paper.

• Publication year

  2013

• Venue

  Structure

• Publication date

  2013-03-05

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.STR.2013.01.013PMID 23454187PMCID PMC3630246
• 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.

• Proteome folding and aggregation.

  2012cited by this paper
• Structure of an Intermediate State in Protein Folding and Aggregation

  2012cited by this paper
• A residue in helical conformation in the native state adopts a β‐strand conformation in the folding transition state despite its high and canonical ϕ‐value

  2012cited by this paper
• ExPASy: SIB bioinformatics resource portal

  2012cited by this paper
• Molecular chaperones in protein folding and proteostasis

  2011cited by this paper
• Functional interactions as a survival strategy against abnormal aggregation

  2011cited by this paper
• The transition state for folding of an outer membrane protein

  2010cited by this paper
• ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids

  2010cited by this paper
• Competition between folding, native-state dimerisation and amyloid aggregation in beta-lactoglobulin.

  2009cited by this paper
• The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.

  2009cited by this paper
• Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming Protein

  2009cited by this paper
• Amyloid formation by globular proteins under native conditions.

  2009cited by this paper
• The Zyggregator method for predicting protein aggregation propensities.

  2008influential reference
• Recent developments in the MAFFT multiple sequence alignment program

  2008cited by this paper
• Folding versus aggregation: Polypeptide conformations on competing pathways

  2008cited by this paper
• Malleability of protein folding pathways: a simple reason for complex behaviour.

  2007cited by this paper
• Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR

  2007cited by this paper
• The PASTA server for protein aggregation prediction.

  2007influential reference
• Bile acid interactions with rabbit ileal lipid binding protein and an engineered helixless variant reveal novel ligand binding properties of a versatile beta-clam shell protein scaffold.

  2007cited by this paper
• Multiple routes lead to the native state in the energy landscape of the β-trefoil family

  2006cited by this paper
• Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant

  2006cited by this paper
• Evolutionary coupling of structural and functional sequence information in the intracellular lipid‐binding protein family

  2006cited by this paper
• Do proteins with similar folds have similar transition state structures? A diffuse transition state of the 169 residue apoflavodoxin.

  2006cited by this paper
• Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment

  2005cited by this paper
• Transient structural disorder as a facilitator of protein-ligand binding: Native H/D exchange—Mass spectrometry study of cellular retinoic acid binding protein I

  2005cited by this paper
• Quantifying the roughness on the free energy landscape: entropic bottlenecks and protein folding rates.

  2004cited by this paper
• The folding transition state of the cold shock protein is strongly polarized.

  2004cited by this paper
• Protein folding in the cell: reshaping the folding funnel.

  2004cited by this paper
• Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns.

  2003cited by this paper
• Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family.

  2003cited by this paper
• Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns.

  2003cited by this paper
• Sequence and structural analysis of cellular retinoic acid‐binding proteins reveals a network of conserved hydrophobic interactions

  2003cited by this paper
• Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation

  2002cited by this paper
• The search for local native-like nucleation centers in the unfolded state of β-sheet proteins

  2002cited by this paper
• Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange.

  2002influential reference
• Hydrophobic core packing in the SH3 domain folding transition state

  2002cited by this paper
• Conformational plasticity in folding of the split beta-alpha-beta protein S6: evidence for burst-phase disruption of the native state.

  2002cited by this paper
• Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state

  2002cited by this paper
• Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.

  2001influential reference
• Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state.

  2001influential reference
• The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold.

  2001cited by this paper
• Multiple roles of prolyl residues in structure and folding.

  2000cited by this paper
• Engineering a compact non-native state of intestinal fatty acid-binding protein.

  2000cited by this paper
• Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding.

  2000cited by this paper
• The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology.

  2000cited by this paper
• Aggregation events occur prior to stable intermediate formation during refolding of interleukin 1beta.

  2000cited by this paper
• An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils.

  1999cited by this paper
• Contact order, transition state placement and the refolding rates of single domain proteins.

  1998cited by this paper
• Probing the folding pathway of a beta-clam protein with single-tryptophan constructs.

  1998cited by this paper
• Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment.

  1997cited by this paper
• Cavity formation before stable hydrogen bonding in the folding of a β-clam protein

  1997cited by this paper
• Intestinal fatty acid-binding protein: the structure and stability of a helix-less variant.

  1996cited by this paper
• Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding

  1995cited by this paper
• NMRPipe: A multidimensional spectral processing system based on UNIX pipes

  1995cited by this paper
• Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid.

  1995cited by this paper
• Lipid-binding proteins: a family of fatty acid and retinoid transport proteins.

  1994cited by this paper
• Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding.

  1993cited by this paper
• Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1 beta point mutant modified in a surface loop.

  1993cited by this paper
• Dynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR.

  1992cited by this paper
• The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.

  1992influential reference
• Determination and analysis of urea and guanidine hydrochloride denaturation curves.

  1986cited by this paper

• Opposing effects of CRABP1 and CRABP2 homologs on the proliferation of breast cancer cells and their sensitivity to retinoic acid

  2023cites this paper
• Opposite Effects of CRABP1 and CRABP2 Homologs on Proliferation of Breast Cancer Cells and Their Sensitivity to Retinoic Acid

  2023cites this paper
• Structural and Dynamic Determinants of Molecular Recognition in Bile Acid-Binding Proteins

  2022influential citation
• Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach.

  2021cites this paper
• Long-range Regulation of Partially Folded Amyloidogenic Peptides

  2020cites this paper
• Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment

  2019cites this paper
• Local and non‐local topological information in the denatured state ensemble of a β‐barrel protein

  2018cites this paper
• Conformational and Colloidal Stabilities of Human Immunoglobulin G Fc and Its Cyclized Variant: Independent and Compensatory Participation of Domains in Aggregation of Multidomain Proteins.

  2017cites this paper
• Protein Domain-Swapping Can Be a Consequence of Functional Residues.

  2016cites this paper
• Exploring the Impact of the E. coli Proteostasis Network on the Folding Fate of Proteins with Different Intrinsic Biophysical Properties

  2016influential citation
• Structure function relationship of recombinant sRAGE

  2016cites this paper
• Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.

  2015cites this paper
• Topological and sequence information predict that foldons organize a partially overlapped and hierarchical structure

  2015cites this paper
• Studies of early events of folding of a predominately β-sheet protein using fluorescence correlation spectroscopy and other biophysical methods.

  2014cites this paper
• Energy landscapes of functional proteins are inherently risky.

  2014cites this paper
• The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-Sheets.

  2013cites this paper
• Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein.

  2013cites this paper
• The unavoidable threat of aggregation: implications for folding and function of a beta-rich protein

  2013cites this paper