Published in J Mol Biol on February 22, 2007
Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci U S A (2008) 2.90
Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci (2008) 2.63
Identifying polyglutamine protein species in situ that best predict neurodegeneration. Nat Chem Biol (2011) 2.24
Toward understanding Machado-Joseph disease. Prog Neurobiol (2011) 1.42
In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence. J Biol Chem (2007) 1.19
Functional interactions as a survival strategy against abnormal aggregation. FASEB J (2010) 1.13
Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation. Proc Natl Acad Sci U S A (2010) 1.11
A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation. PLoS One (2011) 1.05
Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies. Biophys J (2009) 1.02
Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity. PLoS One (2009) 1.01
Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model. PLoS Genet (2013) 0.97
Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders. Philos Trans R Soc Lond B Biol Sci (2013) 0.94
The structural impact of a polyglutamine tract is location-dependent. Biophys J (2008) 0.93
Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein. Protein Sci (2011) 0.93
Energy landscapes of functional proteins are inherently risky. Nat Chem Biol (2014) 0.92
Trinucleotide repeats: a structural perspective. Front Neurol (2013) 0.89
Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation. Nat Commun (2015) 0.88
The Josephin domain determines the morphological and mechanical properties of ataxin-3 fibrils. Biophys J (2011) 0.87
Amyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host protein. PLoS One (2012) 0.84
Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. Mol Cell Proteomics (2015) 0.81
Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3. PLoS One (2012) 0.81
A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected. PLoS One (2013) 0.80
The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli. PLoS One (2012) 0.78
Location trumps length: polyglutamine-mediated changes in folding and aggregation of a host protein. Biophys J (2011) 0.78
Enhanced Molecular Mobility of Ordinarily Structured Regions Drives Polyglutamine Disease. J Biol Chem (2015) 0.78
Investigation of the Josephin Domain protein-protein interaction by molecular dynamics. PLoS One (2014) 0.77
Josephin Domain Structural Conformations Explored by Metadynamics in Essential Coordinates. PLoS Comput Biol (2016) 0.76
Conformational behavior and aggregation of ataxin-3 in SDS. PLoS One (2013) 0.75
Conformational stability of the RNP domain controls fibril formation of PABPN1. Protein Sci (2015) 0.75
Thermodynamic and kinetic stability of the Josephin Domain closed arrangement: evidences from replica exchange molecular dynamics. Biol Direct (2017) 0.75
Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch. Front Neurosci (2017) 0.75
A common fold mediates vertebrate defense and bacterial attack. Science (2007) 3.43
Functional insights from the distribution and role of homopeptide repeat-containing proteins. Genome Res (2005) 1.70
The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. J Biol Chem (2006) 1.66
The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. Structure (2003) 1.61
Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway. FASEB J (2005) 1.51
A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production. BMC Biotechnol (2006) 1.48
Molecular gymnastics: serpin structure, folding and misfolding. Curr Opin Struct Biol (2006) 1.47
Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion. J Exp Med (2004) 1.43
Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor. Immunity (2009) 1.40
Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. EMBO Rep (2011) 1.37
MyD88 adapter-like (Mal)/TIRAP interaction with TRAF6 is critical for TLR2- and TLR4-mediated NF-kappaB proinflammatory responses. J Biol Chem (2009) 1.34
Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems. J Biol Chem (2010) 1.32
The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix. J Biol Chem (2005) 1.21
The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins. J Biol Chem (2005) 1.20
Formation of a high affinity lipid-binding intermediate during the early aggregation phase of alpha-synuclein. Biochemistry (2008) 1.18
Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation. J Biol Chem (2002) 1.17
Enhancing the stability and solubility of TEV protease using in silico design. Protein Sci (2007) 1.17
Structural and functional analysis of the Josephin domain of the polyglutamine protein ataxin-3. Biochem Biophys Res Commun (2004) 1.14
Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions. J Biol Chem (2010) 1.14
Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins. Protein Eng Des Sel (2009) 1.12
Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation. Proc Natl Acad Sci U S A (2010) 1.11
The subtilisin-like protease AprV2 is required for virulence and uses a novel disulphide-tethered exosite to bind substrates. PLoS Pathog (2010) 1.10
Kinetic instability of the serpin Z alpha1-antitrypsin promotes aggregation. J Mol Biol (2009) 1.10
Protein expression and refolding--a practical guide to getting the most out of inclusion bodies. Biotechnol Annu Rev (2004) 1.08
The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram-negative bacteria. Mol Microbiol (2011) 1.07
Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. J Biol Chem (2004) 1.07
Acid Denaturation of alpha1-antitrypsin: characterization of a novel mechanism of serpin polymerization. J Mol Biol (2002) 1.06
Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition. Biochemistry (2004) 1.06
Antithrombin: in control of coagulation. Int J Biochem Cell Biol (2004) 1.03
The matrix refolded. Nat Methods (2005) 1.01
Human embryonic stem cell models of Huntington disease. Reprod Biomed Online (2009) 0.99
REFOLD: an analytical database of protein refolding methods. Protein Expr Purif (2005) 0.99
Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease. J Mol Biol (2004) 0.98
Stabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptide. Biophys J (2007) 0.98
The N terminus of the serpin, tengpin, functions to trap the metastable native state. EMBO Rep (2007) 0.97
Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: engineering alpha(1)-antitrypsin to inhibit cathepsin proteases. Biochemistry (2002) 0.96
Purification of polyglutamine proteins. Methods Enzymol (2006) 0.94
Probing the role of the F-helix in serpin stability through a single tryptophan substitution. Biochemistry (2002) 0.94
X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation. EMBO J (2006) 0.94
The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes. J Biol Chem (2009) 0.94
Physical characterization of serpin conformations. Methods (2004) 0.93
A protein family under 'stress' - serpin stability, folding and misfolding. Front Biosci (2005) 0.93
Crystal structure of a UDP-glucose-specific glycosyltransferase from a Mycobacterium species. J Biol Chem (2008) 0.93
Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein. Protein Sci (2011) 0.93
The structural impact of a polyglutamine tract is location-dependent. Biophys J (2008) 0.93
DNA accelerates the inhibition of human cathepsin V by serpins. J Biol Chem (2007) 0.92
Production of recombinant serpins in Escherichia coli. Methods (2004) 0.92
PolyQ: a database describing the sequence and domain context of polyglutamine repeats in proteins. Nucleic Acids Res (2010) 0.91
Expression, purification and characterization of recombinant Z alpha(1)-antitrypsin--the most common cause of alpha(1)-antitrypsin deficiency. Protein Expr Purif (2009) 0.91
Serpin polymerization and its role in disease--the molecular basis of alpha1-antitrypsin deficiency. IUBMB Life (2009) 0.91
Structural change in β-sheet A of Z α(1)-antitrypsin is responsible for accelerated polymerization and disease. J Mol Biol (2011) 0.90
PFD: a database for the investigation of protein folding kinetics and stability. Nucleic Acids Res (2005) 0.90
The structure of H-2K(b) and K(bm8) complexed to a herpes simplex virus determinant: evidence for a conformational switch that governs T cell repertoire selection and viral resistance. J Immunol (2004) 0.90
Promiscuous beta-strand interactions and the conformational diseases. Curr Med Chem (2004) 0.90
The REFOLD database: a tool for the optimization of protein expression and refolding. Nucleic Acids Res (2006) 0.89
The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition. J Biol Chem (2004) 0.88
A structural basis for loop C-sheet polymerization in serpins. J Mol Biol (2008) 0.87
In vitro and in silico design of alpha1-antitrypsin mutants with different conformational stabilities. J Mol Biol (2003) 0.86
Antagonism of antiviral and allogeneic activity of a human public CTL clonotype by a single altered peptide ligand: implications for allograft rejection. J Immunol (2005) 0.86
Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap. J Biol Chem (2007) 0.86
How do proteins avoid becoming too stable? Biophysical studies into metastable proteins. Eur Biophys J (2003) 0.86
Structural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidis. J Biol Chem (2008) 0.85
The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity. J Biol Chem (2003) 0.85
Conformational properties of the disease-causing Z variant of α1-antitrypsin revealed by theory and experiment. Biophys J (2012) 0.85
A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway. J Biol Chem (2004) 0.85
Observation and characterization of the interaction between a single immunoglobulin binding domain of protein L and two equivalents of human kappa light chains. J Biol Chem (2003) 0.84
Preventing serpin aggregation: the molecular mechanism of citrate action upon antitrypsin unfolding. Protein Sci (2008) 0.83
The role of protein misfolding in the pathogenesis of human diseases. IUBMB Life (2004) 0.83
Identification of residual structure within denatured antichymotrypsin: implications for serpin folding and misfolding. Biochem Biophys Res Commun (2004) 0.82
The rate of polyQ-mediated aggregation is dramatically affected by the number and location of surrounding domains. J Mol Biol (2011) 0.82
Recombinant protein quality evaluation: proposal for a minimal information standard. Stand Genomic Sci (2011) 0.82
The roles of helix I and strand 5A in the folding, function and misfolding of α1-antitrypsin. PLoS One (2013) 0.82
Molecular determinants of the mechanism underlying acceleration of the interaction between antithrombin and factor Xa by heparin pentasaccharide. J Biol Chem (2002) 0.81
Nucleocytoplasmic coagulation: an injury-induced aggregation event that disulfide crosslinks proteins and facilitates their removal by plasmin. Cell Rep (2012) 0.81
Refolding your protein with a little help from REFOLD. Methods Mol Biol (2011) 0.81
Structural biology: Serpins' mystery solved. Nature (2008) 0.80
The loss of tryptophan 194 in antichymotrypsin lowers the kinetic barrier to misfolding. FEBS J (2007) 0.79
Tracking the unfolding pathway of a multirepeat protein via tryptophan scanning: evidence of localized instability in the mitochondrial import receptor Tom70. J Biol Chem (2006) 0.79
Conformational change in the chromatin remodelling protein MENT. PLoS One (2009) 0.78
Methods to measure the kinetics of protease inhibition by serpins. Methods Enzymol (2011) 0.78
Serpins: finely balanced conformational traps. IUBMB Life (2002) 0.77
Molecular pathways to polyglutamine aggregation. Adv Exp Med Biol (2012) 0.77
Determination of the P1', P2' and P3' subsite-specificity of factor Xa. Int J Biochem Cell Biol (2003) 0.77
Introduction of a mutation in the shutter region of antithrombin (Phe77 --> Leu) increases affinity for heparin and decreases thermal stability. Biochemistry (2003) 0.77
The human serpin proteinase inhibitor-9 self-associates at physiological temperatures. Protein Sci (2004) 0.76
Identification of a dimeric intermediate in the unfolding pathway for the calcium-binding protein S100B. J Mol Biol (2008) 0.76
Intracellular production of recombinant serpins in yeast. Methods Enzymol (2011) 0.76
Discovery of amino acid motifs for thrombin cleavage and validation using a model substrate. Biochemistry (2011) 0.76
Amyloid formation from an α-helix peptide bundle is seeded by 3(10)-helix aggregates. Chemistry (2010) 0.76
Conformational behavior and aggregation of ataxin-3 in SDS. PLoS One (2013) 0.75
Serpin acceleration of amyloid fibril formation: a role for accessory proteins. J Mol Biol (2006) 0.75