Pages that link to "Q35030203"

The following pages link to The "Correctly Folded" state of proteins: is it a metastable state? (Q35030203):

Displaying 47 items.

• Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: role of C-terminus of B-chain in association of fibrils (Q24318123) (← links)
• Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments (Q28287401) (← links)
• Hydrogen exchange mass spectrometry for studying protein structure and dynamics (Q28301471) (← links)
• Rational design of fiber forming supramolecular structures (Q28829633) (← links)
• Formation kinetics of insulin-based amyloid gels and the effect of added metalloporphyrins (Q34353100) (← links)
• The amyloid state and its association with protein misfolding diseases. (Q34421102) (← links)
• Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions (Q35051211) (← links)
• Charge transport and intrinsic fluorescence in amyloid-like fibrils. (Q36156726) (← links)
• Spontaneous structural transition and crystal formation in minimal supramolecular polymer model (Q36593562) (← links)
• Amyloid-a state in many guises: survival of the fittest fibril fold (Q37016493) (← links)
• Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins (Q37442810) (← links)
• Sodium dodecyl sulphate modulates the fibrillation of human serum albumin in a dose-dependent manner and impacts the PC12 cells retraction. (Q37579580) (← links)
• The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation. (Q37583331) (← links)
• Role of water in protein folding, oligomerization, amyloidosis and miniprotein (Q38237445) (← links)
• The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation (Q38240692) (← links)
• Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases (Q38338129) (← links)
• Formation of multimeric antibodies for self-delivery of active monomers (Q38718139) (← links)
• Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature (Q38869850) (← links)
• The role of the 14-20 domain of the islet amyloid polypeptide in amyloid formation (Q39125816) (← links)
• Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology. (Q39322110) (← links)
• Phosphorylation modifies the molecular stability of β-amyloid deposits. (Q40249589) (← links)
• Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy (Q40316537) (← links)
• On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils (Q41882869) (← links)
• Existence of different structural intermediates on the fibrillation pathway of human serum albumin. (Q42148091) (← links)
• Extension of the generic amyloid hypothesis to nonproteinaceous metabolite assemblies (Q42619969) (← links)
• Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study (Q43094949) (← links)
• An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid (Q44454039) (← links)
• Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides (Q46267450) (← links)
• The sequence dependence of fiber organization. A comparative molecular dynamics study of the islet amyloid polypeptide segments 22-27 and 22-29. (Q47613438) (← links)
• Steps towards the formation of a protocell: the possible role of short peptides (Q47841917) (← links)
• Seeding of proteins into amyloid structures by metabolite assemblies may clarify certain unexplained epidemiological associations (Q48172417) (← links)
• Metabolite amyloids: a new paradigm for inborn error of metabolism disorders (Q50238179) (← links)
• Helical Folding Competing with Unfolded Aggregation in Phenylene Ethynylene Foldamers (Q51270448) (← links)
• Search for Fibrous Aggregates Potentially Useful in Regenerative Medicine Formed under Physiological Conditions by Self-Assembling Short Peptides Containing Two Identical Aromatic Amino Acid Residues. (Q51736651) (← links)
• Structural Polymorphism in a Self-Assembled Tri-Aromatic Peptide System. (Q52646861) (← links)
• [PIN ]ing down the mechanism of prion appearance. (Q55260627) (← links)
• Mechanisms of Metabolite Amyloid Formation: Computational Studies for Drug Design against Metabolic Disorders (Q62630866) (← links)
• High-Pressure Response of Amyloid Folds (Q64093469) (← links)
• Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of Amyloid-like Fibrils (Q83037568) (← links)
• Reductionist Approach in Peptide-Based Nanotechnology (Q89168628) (← links)
• Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding (Q89551162) (← links)
• Different Synergy in Amyloids and Biologically Active Forms of Proteins (Q90041021) (← links)
• The metastable states of proteins (Q90724026) (← links)
• The Amyloid as a Ribbon-Like Micelle in Contrast to Spherical Micelles Represented by Globular Proteins (Q91807068) (← links)
• Proteome-wide observation of the phenomenon of life on the edge of solubility (Q92355998) (← links)
• Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation (Q92528700) (← links)
• Long-term stability of anti-vascular endothelial cell growth factor (a-VGEF) biologics under physiologically relevant conditions and its impact on the development of long-acting delivery systems (Q100501017) (← links)