249 related articles for article (PubMed ID: 21961598)
1. Chain collapse of an amyloidogenic intrinsically disordered protein.
Jain N; Bhattacharya M; Mukhopadhyay S
Biophys J; 2011 Oct; 101(7):1720-9. PubMed ID: 21961598
[TBL] [Abstract][Full Text] [Related]
2. Sensing Tryptophan Microenvironment of Amyloid Protein Utilizing Wavelength-Selective Fluorescence Approach.
Chakraborty H; Chattopadhyay A
J Fluoresc; 2017 Nov; 27(6):1995-2000. PubMed ID: 28687983
[TBL] [Abstract][Full Text] [Related]
3. Ordered water within the collapsed globules of an amyloidogenic intrinsically disordered protein.
Arya S; Mukhopadhyay S
J Phys Chem B; 2014 Aug; 118(31):9191-8. PubMed ID: 25035108
[TBL] [Abstract][Full Text] [Related]
4. Conformational transition of κ-casein in micellar environment: Insight from the tryptophan fluorescence.
Mishra S; Meher G; Chakraborty H
Spectrochim Acta A Mol Biomol Spectrosc; 2017 Nov; 186():99-104. PubMed ID: 28622544
[TBL] [Abstract][Full Text] [Related]
5. Formation of Heterotypic Amyloids: α-Synuclein in Co-Aggregation.
Bhasne K; Mukhopadhyay S
Proteomics; 2018 Nov; 18(21-22):e1800059. PubMed ID: 30216674
[TBL] [Abstract][Full Text] [Related]
6. The dissociated form of kappa-casein is the precursor to its amyloid fibril formation.
Ecroyd H; Thorn DC; Liu Y; Carver JA
Biochem J; 2010 Jul; 429(2):251-60. PubMed ID: 20441567
[TBL] [Abstract][Full Text] [Related]
7. Dynamics and dimension of an amyloidogenic disordered state of human β(2)-microglobulin.
Narang D; Sharma PK; Mukhopadhyay S
Eur Biophys J; 2013 Oct; 42(10):767-76. PubMed ID: 23974249
[TBL] [Abstract][Full Text] [Related]
8. Kinetics of fibril formation of bovine kappa-casein indicate a conformational rearrangement as a critical step in the process.
Leonil J; Henry G; Jouanneau D; Delage MM; Forge V; Putaux JL
J Mol Biol; 2008 Sep; 381(5):1267-80. PubMed ID: 18616951
[TBL] [Abstract][Full Text] [Related]
9. Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins.
Raskatov JA; Teplow DB
Sci Rep; 2017 Oct; 7(1):12433. PubMed ID: 28970487
[TBL] [Abstract][Full Text] [Related]
10. Aggregation and structural changes of α(S1)-, β- and κ-caseins induced by homocysteinylation.
Stroylova YY; Zimny J; Yousefi R; Chobert JM; Jakubowski H; Muronetz VI; Haertlé T
Biochim Biophys Acta; 2011 Oct; 1814(10):1234-45. PubMed ID: 21689790
[TBL] [Abstract][Full Text] [Related]
11. Molecular Dynamics Simulations Combined with Nuclear Magnetic Resonance and/or Small-Angle X-ray Scattering Data for Characterizing Intrinsically Disordered Protein Conformational Ensembles.
Chan-Yao-Chong M; Durand D; Ha-Duong T
J Chem Inf Model; 2019 May; 59(5):1743-1758. PubMed ID: 30840442
[TBL] [Abstract][Full Text] [Related]
12. Taurine Induces an Ordered but Functionally Inactive Conformation in Intrinsically Disordered Casein Proteins.
Bhat MY; Singh LR; Dar TA
Sci Rep; 2020 Feb; 10(1):3503. PubMed ID: 32103094
[TBL] [Abstract][Full Text] [Related]
13. The Dynamism of Intrinsically Disordered Proteins: Binding-Induced Folding, Amyloid Formation, and Phase Separation.
Mukhopadhyay S
J Phys Chem B; 2020 Dec; 124(51):11541-11560. PubMed ID: 33108190
[TBL] [Abstract][Full Text] [Related]
14. A β-hairpin-binding protein for three different disease-related amyloidogenic proteins.
Shaykhalishahi H; Mirecka EA; Gauhar A; Grüning CS; Willbold D; Härd T; Stoldt M; Hoyer W
Chembiochem; 2015 Feb; 16(3):411-4. PubMed ID: 25557164
[TBL] [Abstract][Full Text] [Related]
15. (-)-epigallocatechin-3-gallate (EGCG) maintains kappa-casein in its pre-fibrillar state without redirecting its aggregation pathway.
Hudson SA; Ecroyd H; Dehle FC; Musgrave IF; Carver JA
J Mol Biol; 2009 Sep; 392(3):689-700. PubMed ID: 19616561
[TBL] [Abstract][Full Text] [Related]
16. Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk α
Thorn DC; Bahraminejad E; Grosas AB; Koudelka T; Hoffmann P; Mata JP; Devlin GL; Sunde M; Ecroyd H; Holt C; Carver JA
Biophys Chem; 2021 Mar; 270():106530. PubMed ID: 33545456
[TBL] [Abstract][Full Text] [Related]
17. The Folding and Aggregation Energy Landscapes of Tethered RRM Domains of Human TDP-43 Are Coupled via a Metastable Molten Globule-like Oligomer.
Pillai M; Jha SK
Biochemistry; 2019 Feb; 58(6):608-620. PubMed ID: 30520297
[TBL] [Abstract][Full Text] [Related]
18. Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans.
Blancas-Mejía LM; Hammernik J; Marin-Argany M; Ramirez-Alvarado M
J Biol Chem; 2015 Feb; 290(8):4953-4965. PubMed ID: 25538238
[TBL] [Abstract][Full Text] [Related]
19. Dynamics and rigidity in an intrinsically disordered protein, β-casein.
Perticaroli S; Nickels JD; Ehlers G; Mamontov E; Sokolov AP
J Phys Chem B; 2014 Jul; 118(26):7317-26. PubMed ID: 24918971
[TBL] [Abstract][Full Text] [Related]
20. Methionine oxidation enhances κ-casein amyloid fibril formation.
Koudelka T; Dehle FC; Musgrave IF; Hoffmann P; Carver JA
J Agric Food Chem; 2012 Apr; 60(16):4144-55. PubMed ID: 22443319
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
