123 related articles for article (PubMed ID: 37941487)
1. Mutations of evolutionarily conserved aromatic residues suggest that misfolding of the mouse prion protein may commence in multiple ways.
Pal S; Udgaonkar JB
J Neurochem; 2023 Dec; 167(5):696-710. PubMed ID: 37941487
[TBL] [Abstract][Full Text] [Related]
2. Evolutionarily Conserved Proline Residues Impede the Misfolding of the Mouse Prion Protein by Destabilizing an Aggregation-competent Partially Unfolded Form.
Pal S; Udgaonkar JB
J Mol Biol; 2022 Dec; 434(23):167854. PubMed ID: 36228749
[TBL] [Abstract][Full Text] [Related]
3. Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.
Moulick R; Das R; Udgaonkar JB
J Biol Chem; 2015 Oct; 290(42):25227-40. PubMed ID: 26306043
[TBL] [Abstract][Full Text] [Related]
4. Identification and Structural Characterization of the Precursor Conformation of the Prion Protein which Directly Initiates Misfolding and Oligomerization.
Moulick R; Udgaonkar JB
J Mol Biol; 2017 Mar; 429(6):886-899. PubMed ID: 28147229
[TBL] [Abstract][Full Text] [Related]
5. Pathogenic Mutations within the Disordered Palindromic Region of the Prion Protein Induce Structure Therein and Accelerate the Formation of Misfolded Oligomers.
Sabareesan AT; Udgaonkar JB
J Mol Biol; 2016 Oct; 428(20):3935-3947. PubMed ID: 27545411
[TBL] [Abstract][Full Text] [Related]
6. Expansion of the octarepeat domain alters the misfolding pathway but not the folding pathway of the prion protein.
Leliveld SR; Stitz L; Korth C
Biochemistry; 2008 Jun; 47(23):6267-78. PubMed ID: 18473442
[TBL] [Abstract][Full Text] [Related]
7. The Pathogenic Mutation T182A Converts the Prion Protein into a Molten Globule-like Conformation Whose Misfolding to Oligomers but Not to Fibrils Is Drastically Accelerated.
Singh J; Udgaonkar JB
Biochemistry; 2016 Jan; 55(3):459-69. PubMed ID: 26713717
[TBL] [Abstract][Full Text] [Related]
8. Mutation-Dependent Refolding of Prion Protein Unveils Amyloidogenic-Related Structural Ramifications: Insights from Molecular Dynamics Simulations.
Palaniappan C; Narayanan RC; Sekar K
ACS Chem Neurosci; 2021 Aug; 12(15):2810-2819. PubMed ID: 34296847
[TBL] [Abstract][Full Text] [Related]
9. Structural effects of multiple pathogenic mutations suggest a model for the initiation of misfolding of the prion protein.
Singh J; Udgaonkar JB
Angew Chem Int Ed Engl; 2015 Jun; 54(26):7529-33. PubMed ID: 25959220
[TBL] [Abstract][Full Text] [Related]
10. Temperature-Induced Misfolding in Prion Protein: Evidence of Multiple Partially Disordered States Stabilized by Non-Native Hydrogen Bonds.
Chamachi NG; Chakrabarty S
Biochemistry; 2017 Feb; 56(6):833-844. PubMed ID: 28102071
[TBL] [Abstract][Full Text] [Related]
11. Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.
Agarwal S; Döring K; Gierusz LA; Iyer P; Lane FM; Graham JF; Goldmann W; Pinheiro TJ; Gill AC
Sci Rep; 2015 Oct; 5():15528. PubMed ID: 26490404
[TBL] [Abstract][Full Text] [Related]
12. A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.
Kurt TD; Jiang L; Bett C; Eisenberg D; Sigurdson CJ
J Biol Chem; 2014 Apr; 289(15):10660-10667. PubMed ID: 24596090
[TBL] [Abstract][Full Text] [Related]
13. Unraveling the Molecular Mechanism of pH-Induced Misfolding and Oligomerization of the Prion Protein.
Singh J; Udgaonkar JB
J Mol Biol; 2016 Mar; 428(6):1345-1355. PubMed ID: 26854758
[TBL] [Abstract][Full Text] [Related]
14. Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein.
Sengupta I; Udgaonkar J
Elife; 2019 Jun; 8():. PubMed ID: 31232689
[TBL] [Abstract][Full Text] [Related]
15. Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.
Silva JL; Vieira TC; Gomes MP; Bom AP; Lima LM; Freitas MS; Ishimaru D; Cordeiro Y; Foguel D
Acc Chem Res; 2010 Feb; 43(2):271-9. PubMed ID: 19817406
[TBL] [Abstract][Full Text] [Related]
16. Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.
Sengupta I; Udgaonkar JB
Chem Commun (Camb); 2018 Jun; 54(49):6230-6242. PubMed ID: 29789820
[TBL] [Abstract][Full Text] [Related]
17. pH-Induced Misfolding Mechanism of Prion Protein: Insights from Microsecond-Accelerated Molecular Dynamics Simulations.
Zhou S; Shi D; Liu X; Yao X; Da LT; Liu H
ACS Chem Neurosci; 2019 Jun; 10(6):2718-2729. PubMed ID: 31070897
[TBL] [Abstract][Full Text] [Related]
18. Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro.
Kyle LM; John TR; Schätzl HM; Lewis RV
PLoS One; 2013; 8(6):e66715. PubMed ID: 23825561
[TBL] [Abstract][Full Text] [Related]
19. Mechanism of misfolding of the human prion protein revealed by a pathological mutation.
Sanz-Hernández M; Barritt JD; Sobek J; Hornemann S; Aguzzi A; De Simone A
Proc Natl Acad Sci U S A; 2021 Mar; 118(12):. PubMed ID: 33731477
[TBL] [Abstract][Full Text] [Related]
20. The folding energy landscape of apoflavodoxin is rugged: hydrogen exchange reveals nonproductive misfolded intermediates.
Bollen YJ; Kamphuis MB; van Mierlo CP
Proc Natl Acad Sci U S A; 2006 Mar; 103(11):4095-100. PubMed ID: 16537490
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
