BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

211 related articles for article (PubMed ID: 25083917)

  • 1. Cu,Zn-superoxide dismutase without Zn is folded but catalytically inactive.
    Nedd S; Redler RL; Proctor EA; Dokholyan NV; Alexandrova AN
    J Mol Biol; 2014 Dec; 426(24):4112-4124. PubMed ID: 25083917
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Unveiling the unfolding pathway of FALS associated G37R SOD1 mutant: a computational study.
    Milardi D; Pappalardo M; Grasso DM; La Rosa C
    Mol Biosyst; 2010 Jun; 6(6):1032-9. PubMed ID: 20485746
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Study of mutation and misfolding of Cu-Zn SOD1 protein.
    Keerthana SP; Kolandaivel P
    J Biomol Struct Dyn; 2015; 33(1):167-83. PubMed ID: 24320678
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis.
    Furukawa Y; Anzai I; Akiyama S; Imai M; Cruz FJ; Saio T; Nagasawa K; Nomura T; Ishimori K
    J Biol Chem; 2016 Feb; 291(8):4144-55. PubMed ID: 26694608
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.
    Kayatekin C; Zitzewitz JA; Matthews CR
    J Mol Biol; 2010 Apr; 398(2):320-31. PubMed ID: 20184893
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Protein charge ladders reveal that the net charge of ALS-linked superoxide dismutase can be different in sign and magnitude from predicted values.
    Shi Y; Abdolvahabi A; Shaw BF
    Protein Sci; 2014 Oct; 23(10):1417-33. PubMed ID: 25052939
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.
    Strange RW; Yong CW; Smith W; Hasnain SS
    Proc Natl Acad Sci U S A; 2007 Jun; 104(24):10040-4. PubMed ID: 17548825
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.
    Rakhit R; Chakrabartty A
    Biochim Biophys Acta; 2006; 1762(11-12):1025-37. PubMed ID: 16814528
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.
    Leal SS; Cristóvão JS; Biesemeier A; Cardoso I; Gomes CM
    Metallomics; 2015 Feb; 7(2):333-46. PubMed ID: 25554447
    [TBL] [Abstract][Full Text] [Related]  

  • 10. The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.
    Chattopadhyay M; Nwadibia E; Strong CD; Gralla EB; Valentine JS; Whitelegge JP
    J Biol Chem; 2015 Dec; 290(51):30624-36. PubMed ID: 26511321
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.
    Ding F; Furukawa Y; Nukina N; Dokholyan NV
    J Mol Biol; 2012 Aug; 421(4-5):548-60. PubMed ID: 22210350
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.
    Rotunno MS; Auclair JR; Maniatis S; Shaffer SA; Agar J; Bosco DA
    J Biol Chem; 2014 Oct; 289(41):28527-38. PubMed ID: 25164820
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes.
    Strange RW; Antonyuk SV; Hough MA; Doucette PA; Valentine JS; Hasnain SS
    J Mol Biol; 2006 Mar; 356(5):1152-62. PubMed ID: 16406071
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Voltage-Induced Misfolding of Zinc-Replete ALS Mutant Superoxide Dismutase-1.
    Shi Y; Acerson MJ; Shuford KL; Shaw BF
    ACS Chem Neurosci; 2015 Oct; 6(10):1696-707. PubMed ID: 26207449
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation.
    Ding F; Dokholyan NV
    Proc Natl Acad Sci U S A; 2008 Dec; 105(50):19696-701. PubMed ID: 19052230
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Engineering a monobody specific to monomeric Cu/Zn-superoxide dismutase associated with amyotrophic lateral sclerosis.
    Amesaka H; Hara M; Sakai Y; Shintani A; Sue K; Yamanaka T; Tanaka SI; Furukawa Y
    Protein Sci; 2024 Apr; 33(4):e4961. PubMed ID: 38511674
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Effect of metal loading and subcellular pH on net charge of superoxide dismutase-1.
    Shi Y; Mowery RA; Shaw BF
    J Mol Biol; 2013 Nov; 425(22):4388-404. PubMed ID: 23871896
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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]  

  • 19. Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation.
    Furukawa Y; O'Halloran TV
    J Biol Chem; 2005 Apr; 280(17):17266-74. PubMed ID: 15691826
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Dominant role of copper in the kinetic stability of Cu/Zn superoxide dismutase.
    Lynch SM; Colón W
    Biochem Biophys Res Commun; 2006 Feb; 340(2):457-61. PubMed ID: 16375856
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 11.