These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

182 related articles for article (PubMed ID: 34010483)

  • 41. Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.
    DeSantis ME; Leung EH; Sweeny EA; Jackrel ME; Cushman-Nick M; Neuhaus-Follini A; Vashist S; Sochor MA; Knight MN; Shorter J
    Cell; 2012 Nov; 151(4):778-793. PubMed ID: 23141537
    [TBL] [Abstract][Full Text] [Related]  

  • 42. Mutable yeast prion variants are stabilized by a defective Hsp104 chaperone.
    Huang YW; Kushnirov VV; King CY
    Mol Microbiol; 2021 Apr; 115(4):774-788. PubMed ID: 33190361
    [TBL] [Abstract][Full Text] [Related]  

  • 43. Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.
    Hattendorf DA; Lindquist SL
    Proc Natl Acad Sci U S A; 2002 Mar; 99(5):2732-7. PubMed ID: 11867765
    [TBL] [Abstract][Full Text] [Related]  

  • 44. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease.
    Lo Bianco C; Shorter J; Régulier E; Lashuel H; Iwatsubo T; Lindquist S; Aebischer P
    J Clin Invest; 2008 Sep; 118(9):3087-97. PubMed ID: 18704197
    [TBL] [Abstract][Full Text] [Related]  

  • 45. Structural and kinetic basis for the regulation and potentiation of Hsp104 function.
    Ye X; Lin J; Mayne L; Shorter J; Englander SW
    Proc Natl Acad Sci U S A; 2020 Apr; 117(17):9384-9392. PubMed ID: 32277033
    [TBL] [Abstract][Full Text] [Related]  

  • 46. Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.
    Wang P; Li J; Weaver C; Lucius A; Sha B
    Acta Crystallogr D Struct Biol; 2017 Apr; 73(Pt 4):365-372. PubMed ID: 28375147
    [TBL] [Abstract][Full Text] [Related]  

  • 47. Structure of Calcarisporiella thermophila Hsp104 Disaggregase that Antagonizes Diverse Proteotoxic Misfolding Events.
    Michalska K; Zhang K; March ZM; Hatzos-Skintges C; Pintilie G; Bigelow L; Castellano LM; Miles LJ; Jackrel ME; Chuang E; Jedrzejczak R; Shorter J; Chiu W; Joachimiak A
    Structure; 2019 Mar; 27(3):449-463.e7. PubMed ID: 30595457
    [TBL] [Abstract][Full Text] [Related]  

  • 48. Hsp104 disaggregase at normal levels cures many [
    Gorkovskiy A; Reidy M; Masison DC; Wickner RB
    Proc Natl Acad Sci U S A; 2017 May; 114(21):E4193-E4202. PubMed ID: 28484020
    [TBL] [Abstract][Full Text] [Related]  

  • 49. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation.
    Tessarz P; Mogk A; Bukau B
    Mol Microbiol; 2008 Apr; 68(1):87-97. PubMed ID: 18312264
    [TBL] [Abstract][Full Text] [Related]  

  • 50. Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma.
    Ryan JJ; Sprunger ML; Holthaus K; Shorter J; Jackrel ME
    J Biol Chem; 2019 Jul; 294(29):11286-11296. PubMed ID: 31171724
    [TBL] [Abstract][Full Text] [Related]  

  • 51. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance.
    Jung G; Jones G; Masison DC
    Proc Natl Acad Sci U S A; 2002 Jul; 99(15):9936-41. PubMed ID: 12105276
    [TBL] [Abstract][Full Text] [Related]  

  • 52. Hydrogen exchange reveals Hsp104 architecture, structural dynamics, and energetics in physiological solution.
    Ye X; Lin J; Mayne L; Shorter J; Englander SW
    Proc Natl Acad Sci U S A; 2019 Apr; 116(15):7333-7342. PubMed ID: 30918129
    [TBL] [Abstract][Full Text] [Related]  

  • 53. Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation.
    Moosavi B; Wongwigkarn J; Tuite MF
    Yeast; 2010 Mar; 27(3):167-79. PubMed ID: 20014008
    [TBL] [Abstract][Full Text] [Related]  

  • 54. AAA+ Protein-Based Technologies to Counter Neurodegenerative Disease.
    March ZM; Mack KL; Shorter J
    Biophys J; 2019 Apr; 116(8):1380-1385. PubMed ID: 30952364
    [TBL] [Abstract][Full Text] [Related]  

  • 55. Structural basis for the disaggregase activity and regulation of Hsp104.
    Heuck A; Schitter-Sollner S; Suskiewicz MJ; Kurzbauer R; Kley J; Schleiffer A; Rombaut P; Herzog F; Clausen T
    Elife; 2016 Nov; 5():. PubMed ID: 27901467
    [TBL] [Abstract][Full Text] [Related]  

  • 56. Heat shock protein 104 (Hsp104)-mediated curing of [
    Zhao X; Rodriguez R; Silberman RE; Ahearn JM; Saidha S; Cummins KC; Eisenberg E; Greene LE
    J Biol Chem; 2017 May; 292(21):8630-8641. PubMed ID: 28373280
    [TBL] [Abstract][Full Text] [Related]  

  • 57. Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.
    Bösl B; Grimminger V; Walter S
    J Biol Chem; 2005 Nov; 280(46):38170-6. PubMed ID: 16135516
    [TBL] [Abstract][Full Text] [Related]  

  • 58. The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy.
    Ohta S; Kawai-Noma S; Kitamura A; Pack CG; Kinjo M; Taguchi H
    Biochem Biophys Res Commun; 2013 Dec; 442(1-2):28-32. PubMed ID: 24216111
    [TBL] [Abstract][Full Text] [Related]  

  • 59. Heat shock protein 104 (HSP104) chaperones soluble Tau via a mechanism distinct from its disaggregase activity.
    Zhang X; Zhang S; Zhang L; Lu J; Zhao C; Luo F; Li D; Li X; Liu C
    J Biol Chem; 2019 Mar; 294(13):4956-4965. PubMed ID: 30718279
    [TBL] [Abstract][Full Text] [Related]  

  • 60. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.
    Shorter J; Lindquist S
    Mol Cell; 2006 Aug; 23(3):425-38. PubMed ID: 16885031
    [TBL] [Abstract][Full Text] [Related]  

    [Previous]   [Next]    [New Search]
    of 10.