Pages that link to "Q43832036"

The following pages link to The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH. (Q43832036):

Displaying 32 items.

• Crystal structure of monomeric human  -2-microglobulin reveals clues to its amyloidogenic properties (Q27639361) (← links)
• The impact of protein disulfide bonds on the amyloid fibril morphology. (Q30360911) (← links)
• Systemic amyloidosis: lessons from β2-microglobulin. (Q30372510) (← links)
• Disorder-to-order conformational transitions in protein structure and its relationship to disease. (Q30376073) (← links)
• Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol (Q30453082) (← links)
• Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI). (Q30865816) (← links)
• Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains. (Q33214661) (← links)
• Systematic analysis of aggregates from 38 kinds of non disease-related proteins: identifying the intrinsic propensity of polypeptides to form amyloid fibrils (Q33283933) (← links)
• Protein fibrillation and nanoparticle interactions: opportunities and challenges (Q38086743) (← links)
• Exploring critical determinants of protein amyloidogenesis: a review (Q38123130) (← links)
• The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR. (Q38269751) (← links)
• Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein (Q38300383) (← links)
• Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6. (Q39494899) (← links)
• Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis (Q41849521) (← links)
• Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils (Q42181152) (← links)
• Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme (Q43169449) (← links)
• Unfolded-state structure and dynamics influence the fibril formation of human prion protein (Q43250700) (← links)
• Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond (Q43954441) (← links)
• Amyloidogenic synthetic peptides of β2-microglobulin—a role of the disulfide bond (Q44410252) (← links)
• Beta2-microglobulin amyloidosis: insights from conservation analysis and fibril modelling by protein docking techniques (Q44485309) (← links)
• Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH. (Q44512589) (← links)
• A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation (Q44512592) (← links)
• Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta2-microglobulin (Q44575256) (← links)
• Conformational stability of amyloid fibrils of beta2-microglobulin probed by guanidine-hydrochloride-induced unfolding (Q45118972) (← links)
• The role of the disulfide bond in amyloid-like fibrillogenesis in a model peptide system (Q46711788) (← links)
• Stabilization of an immunoglobulin fold domain by an engineered disulfide bond at the buried hydrophobic region (Q46954459) (← links)
• Role of the Disulfide Bond in Prion Protein Amyloid Formation: A Thermodynamic and Kinetic Analysis (Q51746419) (← links)
• Effects of N-Methylated Amyloid-β30-40 Peptides on the Fibrillation of Amyloid-β1-40. (Q52664757) (← links)
• The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism (Q57787220) (← links)
• Properties of Some Variants of Human β2-Microglobulin and Amyloidogenesis (Q60218583) (← links)
• Optimum amyloid fibril formation of a peptide fragment suggests the amyloidogenic preference of beta2-microglobulin under physiological conditions (Q75213192) (← links)
• Removal of intact β2‐microglobulin at neutral ph by using seed‐conjugated polymer beads prepared with β2‐microglobulin‐derived peptide (58–67) (Q83510581) (← links)