Pages that link to "Q37276684"
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The following pages link to Crystallin proteins and amyloid fibrils (Q37276684):
Displaying 50 items.
- Protective role of the endoplasmic reticulum protein mitsugumin23 against ultraviolet C-induced cell death (Q24337569) (← links)
- The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment (Q24643585) (← links)
- Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function (Q27661297) (← links)
- Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers (Q27664218) (← links)
- N-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneity (Q27667422) (← links)
- Three-Dimensional Structure of α-Crystallin Domain Dimers of Human Small Heat Shock Proteins HSPB1 and HSPB6 (Q27668166) (← links)
- Atomic View of a Toxic Amyloid Small Oligomer (Q27677948) (← links)
- The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity (Q27683083) (← links)
- Lanosterol reverses protein aggregation in cataracts (Q28114922) (← links)
- Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation (Q28247808) (← links)
- Hold me tight: Role of the heat shock protein family of chaperones in cardiac disease (Q28296634) (← links)
- Quantification of anti-aggregation activity of chaperones: a test-system based on dithiothreitol-induced aggregation of bovine serum albumin (Q28533172) (← links)
- Ordered self-assembly mechanism of a spherical oncoprotein oligomer triggered by zinc removal and stabilized by an intrinsically disordered domain (Q28730047) (← links)
- Mass spectrometry quantifies protein interactions--from molecular chaperones to membrane porins. (Q30368236) (← links)
- Differentiation and Semiquantitative Analysis of an Isoaspartic Acid in Human α-Crystallin by Postsource Decay in a Curved Field Reflectron (Q30986578) (← links)
- Multifunctional antioxidants for the treatment of age-related diseases (Q33524505) (← links)
- Biophysical chemistry of the ageing eye lens (Q33639756) (← links)
- Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH. (Q33654425) (← links)
- UV-B induced fibrillization of crystallin protein mixtures (Q33727972) (← links)
- Analysis of chaperone mRNA expression in the adult mouse brain by meta analysis of the Allen Brain Atlas. (Q33742046) (← links)
- A retinal proteomics-based study identifies αA-crystallin as a sex steroid-regulated protein. (Q33825549) (← links)
- Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation. (Q33935094) (← links)
- Getting folded: chaperone proteins in muscle development, maintenance and disease (Q34055646) (← links)
- Defective Protein Folding and Aggregation as the Basis of Neurodegenerative Diseases: The Darker Aspect of Proteins (Q34185176) (← links)
- Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans (Q34313725) (← links)
- Cooperativity among short amyloid stretches in long amyloidogenic sequences (Q34326067) (← links)
- Hemoglobin interactions with αB crystallin: a direct test of sensitivity to protein instability (Q34344859) (← links)
- The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation (Q34389165) (← links)
- A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein Oligomers (Q34481801) (← links)
- αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide (Q34505802) (← links)
- Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency (Q34925450) (← links)
- Comparison of modification sites in glycated crystallin in vitro and in vivo. (Q35193424) (← links)
- Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation (Q35246361) (← links)
- A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining (Q35578928) (← links)
- SerpinB2 (PAI-2) Modulates Proteostasis via Binding Misfolded Proteins and Promotion of Cytoprotective Inclusion Formation (Q35666031) (← links)
- Two-dimensional IR spectroscopy and segmental 13 C labeling reveals the domain structure of human γD-crystallin amyloid fibrils (Q35807714) (← links)
- The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated. (Q36072725) (← links)
- Protective Effects of Acetylation on the Pathological Reactions of the Lens Crystallins with Homocysteine Thiolactone. (Q36153881) (← links)
- Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions (Q36287203) (← links)
- Novel roles for α-crystallins in retinal function and disease (Q36319863) (← links)
- Alzheimer disease periventricular white matter lesions exhibit specific proteomic profile alterations (Q36597843) (← links)
- The small heat shock proteins αB-crystallin and Hsp27 suppress SOD1 aggregation in vitro (Q36636450) (← links)
- Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27 (Q36832649) (← links)
- Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers. (Q36929132) (← links)
- αB-Crystallin overexpression in astrocytes modulates the phenotype of the BACHD mouse model of Huntington's disease (Q37178561) (← links)
- Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage (Q37384901) (← links)
- The interaction of Glu294 at the subunit interface is important for the activity and stability of goose delta-crystallin (Q37425251) (← links)
- A novel dominant D109A CRYAB mutation in a family with myofibrillar myopathy affects αB-crystallin structure. (Q37442928) (← links)
- Mechanism of suppression of protein aggregation by α-crystallin (Q37462264) (← links)
- Large Potentials of Small Heat Shock Proteins (Q37947562) (← links)