BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

208 related articles for article (PubMed ID: 31338686)

  • 1. The small heat shock proteins, HSPB1 and HSPB5, interact differently with lipid membranes.
    De Maio A; Cauvi DM; Capone R; Bello I; Egberts WV; Arispe N; Boelens W
    Cell Stress Chaperones; 2019 Sep; 24(5):947-956. PubMed ID: 31338686
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Analysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1).
    Simon S; Dimitrova V; Gibert B; Virot S; Mounier N; Nivon M; Kretz-Remy C; Corset V; Mehlen P; Arrigo AP
    PLoS One; 2013; 8(8):e70545. PubMed ID: 23950959
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets.
    Arrigo AP; Simon S; Gibert B; Kretz-Remy C; Nivon M; Czekalla A; Guillet D; Moulin M; Diaz-Latoud C; Vicart P
    FEBS Lett; 2007 Jul; 581(19):3665-74. PubMed ID: 17467701
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Chaperone activity of human small heat shock protein-GST fusion proteins.
    Arbach H; Butler C; McMenimen KA
    Cell Stress Chaperones; 2017 Jul; 22(4):503-515. PubMed ID: 28130664
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners.
    Hussein RM; Benjamin IJ; Kampinga HH
    PLoS One; 2015; 10(5):e0126761. PubMed ID: 25961584
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain.
    Dores-Silva PR; Cauvi DM; Coto ALS; Kiraly VTR; Borges JC; De Maio A
    Cell Stress Chaperones; 2020 Nov; 25(6):979-991. PubMed ID: 32725381
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes.
    Dores-Silva PR; Cauvi DM; Coto ALS; Silva NSM; Borges JC; De Maio A
    Cell Stress Chaperones; 2021 Jul; 26(4):671-684. PubMed ID: 34003451
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Interaction of heat shock protein 70 with membranes depends on the lipid environment.
    Armijo G; Okerblom J; Cauvi DM; Lopez V; Schlamadinger DE; Kim J; Arispe N; De Maio A
    Cell Stress Chaperones; 2014 Nov; 19(6):877-86. PubMed ID: 24789271
    [TBL] [Abstract][Full Text] [Related]  

  • 9. N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation.
    Selig EE; Zlatic CO; Cox D; Mok YF; Gooley PR; Ecroyd H; Griffin MDW
    J Biol Chem; 2020 Jul; 295(29):9838-9854. PubMed ID: 32417755
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8.
    Arrigo AP; Gibert B
    Int J Hyperthermia; 2013 Aug; 29(5):409-22. PubMed ID: 23697380
    [TBL] [Abstract][Full Text] [Related]  

  • 11. The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes.
    Csoboz B; Gombos I; Kóta Z; Dukic B; Klement É; Varga-Zsíros V; Lipinszki Z; Páli T; Vígh L; Török Z
    Int J Mol Sci; 2022 Jun; 23(13):. PubMed ID: 35806322
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Interaction of small heat shock proteins with light component of neurofilaments (NFL).
    Nefedova VV; Sudnitsyna MV; Gusev NB
    Cell Stress Chaperones; 2017 Jul; 22(4):467-479. PubMed ID: 28000086
    [TBL] [Abstract][Full Text] [Related]  

  • 13. The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8.
    Shatov VM; Weeks SD; Strelkov SV; Gusev NB
    Int J Mol Sci; 2018 Jul; 19(7):. PubMed ID: 30036999
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes.
    Lopez V; Cauvi DM; Arispe N; De Maio A
    Cell Stress Chaperones; 2016 Jul; 21(4):609-16. PubMed ID: 27075190
    [TBL] [Abstract][Full Text] [Related]  

  • 15. The small heat shock proteins αB-crystallin (HSPB5) and Hsp27 (HSPB1) inhibit the intracellular aggregation of α-synuclein.
    Cox D; Ecroyd H
    Cell Stress Chaperones; 2017 Jul; 22(4):589-600. PubMed ID: 28337642
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death.
    Acunzo J; Katsogiannou M; Rocchi P
    Int J Biochem Cell Biol; 2012 Oct; 44(10):1622-31. PubMed ID: 22521623
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Regulation of small heat-shock proteins by hetero-oligomer formation.
    Mymrikov EV; Riedl M; Peters C; Weinkauf S; Haslbeck M; Buchner J
    J Biol Chem; 2020 Jan; 295(1):158-169. PubMed ID: 31767683
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Phosphorylation-dependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in cultured hippocampal neurons.
    Schmidt T; Bartelt-Kirbach B; Golenhofen N
    Histochem Cell Biol; 2012 Sep; 138(3):407-18. PubMed ID: 22617993
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Neuropathy-causing mutations in HSPB1 impair autophagy by disturbing the formation of SQSTM1/p62 bodies.
    Haidar M; Asselbergh B; Adriaenssens E; De Winter V; Timmermans JP; Auer-Grumbach M; Juneja M; Timmerman V
    Autophagy; 2019 Jun; 15(6):1051-1068. PubMed ID: 30669930
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: role of the in vitro hetero-complex formation in chaperone activity.
    Skouri-Panet F; Michiel M; Férard C; Duprat E; Finet S
    Biochimie; 2012 Apr; 94(4):975-84. PubMed ID: 22210387
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 11.