216 related articles for article (PubMed ID: 30701485)
1. Computational Investigation on Electrostatic Loop Mutants Instigating Destabilization and Aggregation on Human SOD1 Protein Causing Amyotrophic Lateral Sclerosis.
Srinivasan E; Rajasekaran R
Protein J; 2019 Feb; 38(1):37-49. PubMed ID: 30701485
[TBL] [Abstract][Full Text] [Related]
2. A theoretical study on Zn binding loop mutants instigating destabilization and metal binding loss in human SOD1 protein.
Srinivasan E; Sethumadhavan R; Rajasekaran R
J Mol Model; 2017 Apr; 23(4):103. PubMed ID: 28271284
[TBL] [Abstract][Full Text] [Related]
3. Computational investigation of the human SOD1 mutant, Cys146Arg, that directs familial amyotrophic lateral sclerosis.
Srinivasan E; Rajasekaran R
Mol Biosyst; 2017 Jul; 13(8):1495-1503. PubMed ID: 28621357
[TBL] [Abstract][Full Text] [Related]
4. Molecular binding response of naringin and naringenin to H46R mutant SOD1 protein in combating protein aggregation using density functional theory and discrete molecular dynamics.
Srinivasan E; Rajasekaran R
Prog Biophys Mol Biol; 2019 Aug; 145():40-51. PubMed ID: 30543828
[TBL] [Abstract][Full Text] [Related]
5. Changes in hydrophobicity mainly promotes the aggregation tendency of ALS associated SOD1 mutants.
Tompa DR; Kadhirvel S
Int J Biol Macromol; 2020 Feb; 145():904-913. PubMed ID: 31669277
[TBL] [Abstract][Full Text] [Related]
6. Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis.
Srinivasan E; Rajasekaran R
Proteins; 2017 Jul; 85(7):1276-1286. PubMed ID: 28321933
[TBL] [Abstract][Full Text] [Related]
7. Cysteine to Serine Conversion at 111th Position Renders the Disaggregation and Retains the Stabilization of Detrimental SOD1 A4V Mutant Against Amyotrophic Lateral Sclerosis in Human-A Discrete Molecular Dynamics Study.
Srinivasan E; Rajasekaran R
Cell Biochem Biophys; 2018 Jun; 76(1-2):231-241. PubMed ID: 28952073
[TBL] [Abstract][Full Text] [Related]
8. A mechanism for propagated SOD1 misfolding from frustration analysis of a G85R mutant protein assembly.
Healy EF
Biochem Biophys Res Commun; 2016 Sep; 478(4):1634-9. PubMed ID: 27591900
[TBL] [Abstract][Full Text] [Related]
9. β-Methylamino-L-alanine substitution of serine in SOD1 suggests a direct role in ALS etiology.
Proctor EA; Mowrey DD; Dokholyan NV
PLoS Comput Biol; 2019 Jul; 15(7):e1007225. PubMed ID: 31323035
[TBL] [Abstract][Full Text] [Related]
10. Alterations in local stability and dynamics of A4V SOD1 in the presence of trifluoroethanol.
Kumar V; Prakash A; Lynn AM
Biopolymers; 2018 Mar; 109(3):e23102. PubMed ID: 29369331
[TBL] [Abstract][Full Text] [Related]
11. Destabilization of the metal site as a hub for the pathogenic mechanism of five ALS-linked mutants of copper, zinc superoxide dismutase.
Mera-Adasme R; Erdmann H; Bereźniak T; Ochsenfeld C
Metallomics; 2016 Oct; 8(10):1141-1150. PubMed ID: 27603566
[TBL] [Abstract][Full Text] [Related]
12. Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.
Tompa DR; Kadhirvel S
J Biomol Struct Dyn; 2018 Nov; 36(15):4085-4098. PubMed ID: 29157189
[TBL] [Abstract][Full Text] [Related]
13. SOD1 in amyotrophic lateral sclerosis development - in silico analysis and molecular dynamics of A4F and A4V variants.
Da Silva ANR; Pereira GRC; Moreira LGA; Rocha CF; De Mesquita JF
J Cell Biochem; 2019 Oct; 120(10):17822-17830. PubMed ID: 31134679
[TBL] [Abstract][Full Text] [Related]
14. Molecular dynamics of far positioned surface mutations of Cu/Zn SOD1 promotes altered structural stability and metal-binding site: Structural clues to the pathogenesis of amyotrophic lateral sclerosis.
Tompa DR; Muthusamy S; Srikanth S; Kadhirvel S
J Mol Graph Model; 2020 Nov; 100():107678. PubMed ID: 32768728
[TBL] [Abstract][Full Text] [Related]
15. A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis.
Anzai I; Tokuda E; Mukaiyama A; Akiyama S; Endo F; Yamanaka K; Misawa H; Furukawa Y
Protein Sci; 2017 Mar; 26(3):484-496. PubMed ID: 27977888
[TBL] [Abstract][Full Text] [Related]
16. Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosis.
Pereira GRC; Vieira BAA; De Mesquita JF
PLoS One; 2021; 16(2):e0247841. PubMed ID: 33630959
[TBL] [Abstract][Full Text] [Related]
17. A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation.
Fay JM; Zhu C; Proctor EA; Tao Y; Cui W; Ke H; Dokholyan NV
Structure; 2016 Nov; 24(11):1898-1906. PubMed ID: 27667694
[TBL] [Abstract][Full Text] [Related]
18. SOD1 in neurotoxicity and its controversial roles in SOD1 mutation-negative ALS.
Hayashi Y; Homma K; Ichijo H
Adv Biol Regul; 2016 Jan; 60():95-104. PubMed ID: 26563614
[TBL] [Abstract][Full Text] [Related]
19. Superoxide Dismutase 1 (SOD1)-Derived Peptide Inhibits Amyloid Aggregation of Familial Amyotrophic Lateral Sclerosis SOD1 Mutants.
Banerjee V; Shani T; Katzman B; Vyazmensky M; Papo N; Israelson A; Engel S
ACS Chem Neurosci; 2016 Nov; 7(11):1595-1606. PubMed ID: 27540759
[TBL] [Abstract][Full Text] [Related]
20. Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.
Broom HR; Rumfeldt JA; Meiering EM
Essays Biochem; 2014; 56():149-65. PubMed ID: 25131593
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]