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Items: 1 to 20 of 100

1.
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
Sebastian Specht, Stephanie B.M. Miller, Axel Mogk, Bernd Bukau
J Cell Biol. 2011 Nov 14; 195(4): 617–629. doi: 10.1083/jcb.201106037
PMCID:
PMC3257523
AbstractArticlePDF–3.5M
2.
ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo
Udhayabhaskar Sathyanarayanan, Marina Musa, Peter Bou Dib, Nuno Raimundo, Ira Milosevic, Anita Krisko
Nat Commun. 2020; 11: 5226. Published online 2020 Oct 16. doi: 10.1038/s41467-020-19104-1
Correction in:
Nat Commun. 2020; 11: 6414.
PMCID:
PMC7568574
AbstractArticlePDF–2.9M
3.
A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins
Tomas Grousl, Sophia Ungelenk, Stephanie Miller, Chi-Ting Ho, Maria Khokhrina, Matthias P. Mayer, Bernd Bukau, Axel Mogk
J Cell Biol. 2018 Apr 2; 217(4): 1269–1285. doi: 10.1083/jcb.201708116
PMCID:
PMC5881502
AbstractArticlePDF–2.6M
4.
Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P. Mayer, Axel Mogk, Bernd Bukau
Nat Commun. 2016; 7: 13673. Published online 2016 Nov 30. doi: 10.1038/ncomms13673
PMCID:
PMC5141385
AbstractArticlePDF–1.6M
5.
Small Heat-Shock Proteins Select ΔF508-CFTR for Endoplasmic Reticulum-associated Degradation
Annette Ahner, Kunio Nakatsukasa, Hui Zhang, Raymond A. Frizzell, Jeffrey L. Brodsky
Mol Biol Cell. 2007 Mar; 18(3): 806–814. doi: 10.1091/mbc.E06-05-0458
PMCID:
PMC1805084
AbstractArticlePDF–761K
6.
Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae
Martin Haslbeck, Nathalie Braun, Thusnelda Stromer, Bettina Richter, Natascha Model, Sevil Weinkauf, Johannes Buchner
EMBO J. 2004 Feb 11; 23(3): 638–649. Published online 2004 Jan 29. doi: 10.1038/sj.emboj.7600080
Correction in:
EMBO J. 2020 Jun 17; 39(12): e105112.
PMCID:
PMC1271810
AbstractArticlePDF–433K
7.
Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation
Zorana Carter, Declan Creamer, Aikaterini Kouvidi, Chris M. Grant
PLoS Genet. 2024 Feb; 20(2): e1011194. Published online 2024 Feb 29. doi: 10.1371/journal.pgen.1011194
PMCID:
PMC10931478
AbstractArticlePDF–3.0M
8.
The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells
I-Chun Liu, Sheng-Wen Chiu, Hsin-Yi Lee, Jun-Yi Leu
Mol Biol Cell. 2012 Apr 1; 23(7): 1231–1242. doi: 10.1091/mbc.E11-09-0752
PMCID:
PMC3315813
AbstractArticlePDF–2.2M
9.
Identification and Characterization of a Stress-Inducible and a Constitutive Small Heat-Shock Protein Targeted to the Matrix of Plant Peroxisomes
Changle Ma, Martin Haslbeck, Lavanya Babujee, Olaf Jahn, Sigrun Reumann
Plant Physiol. 2006 May; 141(1): 47–60. doi: 10.1104/pp.105.073841
PMCID:
PMC1459323
AbstractArticlePDF–491K
10.
A Chaperone Pathway in Protein Disaggregation: HSP26 ALTERS THE NATURE OF PROTEIN AGGREGATES TO FACILITATE REACTIVATION BY HSP104
Anil G. Cashikar, Martin Duennwald, Susan L. Lindquist
J Biol Chem. Author manuscript; available in PMC 2006 Mar 8.
Published in final edited form as: J Biol Chem. 2005 Jun 24; 280(25): 23869–23875. Published online 2005 Apr 20. doi: 10.1074/jbc.M502854200
Correction in:
J Biol Chem, volume 281 on page 8996
PMCID:
PMC1391974
AbstractArticlePDF–612K
11.
Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors
Shailesh Kumar, Elliot A. Dine, Ethan Paddock, Danielle N. Steinberg, Lois E. Greene, Daniel C. Masison
Mol Cell Biol. 2020 Nov; 40(21): e00294-20. Prepublished online 2020 Aug 31. Published online 2020 Oct 13. doi: 10.1128/MCB.00294-20
PMCID:
PMC7556844
AbstractArticlePDF–2.7M
12.
Small heat shock protein suppression of Vpr-induced cytoskeletal defects in budding yeast.
J Gu, M Emerman, S Sandmeyer
Mol Cell Biol. 1997 Jul; 17(7): 4033–4042. doi: 10.1128/mcb.17.7.4033
PMCID:
PMC232256
SummaryPDF–1.6M
13.
Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins
Davi Goncalves, Duong Long Duy, Sara Peffer, Kevin A. Morano
Mol Biol Cell. 2024 Apr 1; 35(4): ar53. Published online 2024 Mar 5. doi: 10.1091/mbc.E23-07-0296
PMCID:
PMC11064659
AbstractArticlePDF–1.6M
14.
Real-time imaging of yeast cells reveals several distinct mechanisms of curing of the [URE3] prion
Xiaohong Zhao, Jenna Lanz, Danielle Steinberg, Tyler Pease, Joseph M. Ahearn, Evgeny E. Bezsonov, Elena D. Staguhn, Evan Eisenberg, Daniel C. Masison, Lois E. Greene
J Biol Chem. 2018 Mar 2; 293(9): 3104–3117. Published online 2018 Jan 12. doi: 10.1074/jbc.M117.809079
PMCID:
PMC5836123
AbstractArticlePDF–3.9M
15.
Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments
Joydeep Roy, Sahana Mitra, Kaushik Sengupta, Atin K. Mandal
Mol Biol Cell. 2015 May 1; 26(9): 1583–1600. doi: 10.1091/mbc.E14-08-1262
PMCID:
PMC4436772
AbstractArticlePDF–8.0M
16.
Two alternative mechanisms regulate the onset of chaperone-mediated assembly of the proteasomal ATPases
Asrafun Nahar, Xinyi Fu, George Polovin, James D. Orth, Soyeon Park
J Biol Chem. 2019 Apr 19; 294(16): 6562–6577. Published online 2019 Feb 27. doi: 10.1074/jbc.RA118.006298
PMCID:
PMC6484131
AbstractArticlePDF–3.1M
17.
Protein aggregates are associated with replicative aging without compromising protein quality control
Juha Saarikangas, Yves Barral
eLife. 2015; 4: e06197. Published online 2015 Nov 6. doi: 10.7554/eLife.06197
PMCID:
PMC4635334
AbstractArticlePDF–5.4M
18.
Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants
Reed B. Wickner, Evgeny Bezsonov, David A. Bateman
Proc Natl Acad Sci U S A. 2014 Jul 1; 111(26): E2711–E2720. Published online 2014 Jun 17. doi: 10.1073/pnas.1409582111
PMCID:
PMC4084489
AbstractArticlePDF–1.7M
19.
Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis
Chi-ting Ho, Tomas Grousl, Oren Shatz, Areeb Jawed, Carmen Ruger-Herreros, Marije Semmelink, Regina Zahn, Karsten Richter, Bernd Bukau, Axel Mogk
Nat Commun. 2019; 10: 4851. Published online 2019 Oct 24. doi: 10.1038/s41467-019-12868-1
PMCID:
PMC6813348
AbstractArticlePDF–4.5M
20.
Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III
Urszula Natkańska, Adrianna Skoneczna, Marek Skoneczny
Cell Stress Chaperones. 2018 Jul; 23(4): 595–607. Published online 2017 Dec 20. doi: 10.1007/s12192-017-0868-8
PMCID:
PMC6045530
AbstractArticlePDF–4.3M

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