Molecular Chaperones and Proteolytic Machineries Regulate Protein Homeostasis in Aging Cells

Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially provided by the cell proteostasis network, which consists of molecular chaperones, a ubiquitin-proteasome system of degradation and autophagy. The...

Full description

Saved in:
Bibliographic Details
Published inCells (Basel, Switzerland) Vol. 9; no. 5; p. 1308
Main Authors Margulis, Boris, Tsimokha, Anna, Zubova, Svetlana, Guzhova, Irina
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 24.05.2020
MDPI
Subjects
Online AccessGet full text
ISSN2073-4409
2073-4409
DOI10.3390/cells9051308

Cover

Loading…
Abstract Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially provided by the cell proteostasis network, which consists of molecular chaperones, a ubiquitin-proteasome system of degradation and autophagy. The cooperation of these systems impacts the correct function of protein synthesis/modification/transport machinery starting from the adaption of nascent polypeptides to cellular overcrowding until the utilization of damaged or needless proteins. Eventually, aging cells, in parallel to the accumulation of flawed proteins, gradually lose their proteostasis mechanisms, and this loss leads to the degeneration of large cellular masses and to number of age-associated pathologies and ultimately death. In this review, we describe the function of proteostasis mechanisms with an emphasis on the possible associations between them.
AbstractList Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially provided by the cell proteostasis network, which consists of molecular chaperones, a ubiquitin-proteasome system of degradation and autophagy. The cooperation of these systems impacts the correct function of protein synthesis/modification/transport machinery starting from the adaption of nascent polypeptides to cellular overcrowding until the utilization of damaged or needless proteins. Eventually, aging cells, in parallel to the accumulation of flawed proteins, gradually lose their proteostasis mechanisms, and this loss leads to the degeneration of large cellular masses and to number of age-associated pathologies and ultimately death. In this review, we describe the function of proteostasis mechanisms with an emphasis on the possible associations between them.Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially provided by the cell proteostasis network, which consists of molecular chaperones, a ubiquitin-proteasome system of degradation and autophagy. The cooperation of these systems impacts the correct function of protein synthesis/modification/transport machinery starting from the adaption of nascent polypeptides to cellular overcrowding until the utilization of damaged or needless proteins. Eventually, aging cells, in parallel to the accumulation of flawed proteins, gradually lose their proteostasis mechanisms, and this loss leads to the degeneration of large cellular masses and to number of age-associated pathologies and ultimately death. In this review, we describe the function of proteostasis mechanisms with an emphasis on the possible associations between them.
Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially provided by the cell proteostasis network, which consists of molecular chaperones, a ubiquitin-proteasome system of degradation and autophagy. The cooperation of these systems impacts the correct function of protein synthesis/modification/transport machinery starting from the adaption of nascent polypeptides to cellular overcrowding until the utilization of damaged or needless proteins. Eventually, aging cells, in parallel to the accumulation of flawed proteins, gradually lose their proteostasis mechanisms, and this loss leads to the degeneration of large cellular masses and to number of age-associated pathologies and ultimately death. In this review, we describe the function of proteostasis mechanisms with an emphasis on the possible associations between them.
Author Margulis, Boris
Tsimokha, Anna
Guzhova, Irina
Zubova, Svetlana
AuthorAffiliation Institute of Cytology of the Russian Academy of Sciences, St. Petersburg 194064, Russia; margulis@incras.ru (B.M.); atsimokha@incras.ru (A.T.); egretta_julia@mail.ru (S.Z.)
AuthorAffiliation_xml – name: Institute of Cytology of the Russian Academy of Sciences, St. Petersburg 194064, Russia; margulis@incras.ru (B.M.); atsimokha@incras.ru (A.T.); egretta_julia@mail.ru (S.Z.)
Author_xml – sequence: 1
  givenname: Boris
  surname: Margulis
  fullname: Margulis, Boris
– sequence: 2
  givenname: Anna
  surname: Tsimokha
  fullname: Tsimokha, Anna
– sequence: 3
  givenname: Svetlana
  surname: Zubova
  fullname: Zubova, Svetlana
– sequence: 4
  givenname: Irina
  orcidid: 0000-0002-8775-7713
  surname: Guzhova
  fullname: Guzhova, Irina
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32456366$$D View this record in MEDLINE/PubMed
BookMark eNptks1rFDEUwINUbK29eZYBLz24mu-ZXISyqC20KKI3IWSSN7NZZpM1yQj97812W9kWc8nH-70fL3l5iY5CDIDQa4LfM6bwBwvTlBUWhOHuGTqhuGULzrE6Olgfo7Oc17iOjkiCxQt0zCgXkkl5gn7dxAnsPJnULFdmC6n6c2OCa76lWCBOt8Xb5sbYlQ-QfI19h7HiBfaAD81l3EDMxWSfm7q9GH0Ym-WusFfo-WCmDGf38yn6-fnTj-Xl4vrrl6vlxfXC8rYri8EJyQnBSoIVMPRESkzF4EAY4VTfM85N3ylhWmmhJUwJ4Ea1lLlW9tQxdoqu9l4XzVpvk9-YdKuj8fruIKZRm1TvMYF2gwDD-5b2puXc4p5zJ6VkXGI-AHbV9XHv2s79BpyFUJKZHkkfR4Jf6TH-0S1VhApeBef3ghR_z5CL3vi865MJEOesKa-NIYxiUtG3T9B1nFOoT3VHSa4k6Sr15rCif6U8NLECdA_YFHNOMGjriyk-7gr0kyZY7z6LPvwsNendk6QH73_xvx8MwUc
CitedBy_id crossref_primary_10_3390_cells11111772
crossref_primary_10_31857_S0041377123030100
crossref_primary_10_1007_s10555_023_10085_3
crossref_primary_10_3390_cells13242101
crossref_primary_10_1016_j_crstbi_2022_11_002
crossref_primary_10_3390_ijms25115608
crossref_primary_10_1093_dnares_dsae031
crossref_primary_10_3390_nu13082843
crossref_primary_10_1002_2211_5463_13049
crossref_primary_10_1111_acel_13834
crossref_primary_10_3390_ph15080923
crossref_primary_10_14336_AD_2021_1213
crossref_primary_10_3390_ijms23020649
crossref_primary_10_1016_j_mad_2021_111430
crossref_primary_10_18632_aging_205109
crossref_primary_10_1134_S1990519X23050139
crossref_primary_10_1016_j_jbc_2021_100338
crossref_primary_10_31857_S0041377123040090
crossref_primary_10_1186_s12979_022_00274_z
crossref_primary_10_3389_fragi_2022_861686
crossref_primary_10_1134_S1990519X23060093
crossref_primary_10_3390_ijms25169090
crossref_primary_10_1134_S0026893321050022
crossref_primary_10_1134_S1062360422060091
crossref_primary_10_3390_molecules27248950
crossref_primary_10_1007_s11033_021_06744_9
crossref_primary_10_1039_D3NR06044F
crossref_primary_10_3390_cells14030222
crossref_primary_10_3390_ijms21186647
crossref_primary_10_1016_j_mam_2022_101157
crossref_primary_10_1016_j_ejmech_2021_113577
Cites_doi 10.1242/jcs.132605
10.1038/s41418-019-0480-9
10.1556/2060.105.2018.3.20
10.1111/acel.12446
10.1091/mbc.e03-12-0893
10.3389/fnmol.2017.00177
10.1080/15548627.2019.1603545
10.1016/j.cell.2018.04.028
10.1007/s12192-017-0787-8
10.1074/jbc.M301048200
10.1379/CSC-119R.1
10.1074/jbc.RA119.011280
10.1016/j.exer.2006.12.002
10.1006/excr.1998.4069
10.1007/s12192-017-0765-1
10.1096/fj.04-2578fje
10.1146/annurev-biochem-060614-033955
10.1016/j.cell.2005.11.007
10.1016/j.biocel.2007.01.002
10.1007/s12264-015-1543-7
10.1096/fj.06-6751com
10.1038/onc.2011.5
10.1016/j.abb.2003.10.010
10.15252/embj.201796697
10.1513/pats.200909-102JS
10.1016/j.mad.2005.01.008
10.1016/j.freeradbiomed.2011.06.015
10.1080/15548627.2016.1248018
10.3389/fmolb.2019.00030
10.1016/j.redox.2017.07.008
10.1016/S0306-4522(00)00067-1
10.3389/fnagi.2019.00049
10.1007/s00018-018-2836-6
10.1093/emboj/cdg529
10.1002/pmic.201900408
10.3390/ijms18112351
10.1128/MCB.00426-18
10.1093/hmg/ddu073
10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2
10.1016/j.jprot.2013.06.025
10.1016/j.cell.2013.05.039
10.1371/journal.pone.0017369
10.1006/abbi.2001.2663
10.1038/s41467-019-13540-4
10.1016/j.bbrc.2014.02.124
10.1016/j.jss.2005.09.019
10.1080/15548627.2020.1725404
10.1021/acs.jmedchem.9b00101
10.1096/fj.03-0164fje
10.1038/npp.2015.219
10.1038/s41467-019-14187-x
10.1016/S0531-5565(02)00134-1
10.1146/annurev-genet-111212-133232
10.1016/j.exger.2011.05.002
10.15252/embj.201796699
10.1128/MCB.02070-07
10.1093/emboj/19.21.5720
10.1038/onc.2010.171
10.1096/fj.03-0395fje
10.1002/path.2697
10.1126/science.273.5274.501
10.1016/S0047-6374(98)00052-9
10.4161/auto.5269
10.1016/j.bbadis.2018.09.001
10.1038/s41580-019-0101-y
10.1038/nature10604
10.1126/science.1083701
10.3389/fnmol.2016.00093
10.3390/cells3030674
10.1016/j.celrep.2014.09.042
10.1074/jbc.M002102200
10.1007/s10522-008-9135-9
10.1016/j.neulet.2010.01.049
10.1016/j.celrep.2016.12.033
10.1016/j.molcel.2015.05.030
10.1038/nature04723
10.1042/BCJ20160005
10.3390/ijms20184507
10.18632/aging.100613
10.18632/aging.100939
10.1093/emboj/18.21.5943
10.1093/emboj/cdg349
10.1016/j.tips.2014.09.001
10.1016/j.freeradbiomed.2011.08.001
10.1007/s00018-008-7535-2
10.1016/j.cell.2014.05.045
10.1016/j.celrep.2019.03.044
10.1038/nature05925
10.1007/s10522-018-9773-5
10.1016/j.molcel.2017.05.031
10.3390/ijms20246195
10.1016/j.cell.2012.06.031
10.1096/fj.04-3084fje
10.1038/s41467-018-03509-0
10.1074/jbc.273.35.22284
10.1016/j.tcb.2017.08.002
10.1038/sj.emboj.7601360
10.1002/mus.10094
10.1152/ajpregu.1991.260.4.R663
10.4161/auto.20649
10.1038/s41467-017-00314-z
10.1016/j.cell.2017.04.003
10.1002/1873-3468.12750
10.1038/s41580-018-0033-y
10.1242/jcs.210724
10.1016/j.exger.2016.03.015
10.1016/j.tibs.2013.08.001
10.1016/j.biocel.2012.04.010
10.1242/jcs.001073
10.1074/jbc.M413007200
10.1074/jbc.M506096200
10.1016/j.mad.2009.10.003
10.1007/978-981-15-0602-4_4
10.15252/embj.201489062
10.3389/fendo.2018.00778
10.1038/s41467-019-14164-4
10.1111/j.1474-9726.2008.00401.x
10.4161/auto.5618
10.1016/j.cell.2007.06.044
10.1038/emboj.2009.29
10.1146/annurev-biochem-060815-014922
10.1016/j.mad.2009.09.004
10.1379/1466-1268(2004)009<0049:MHSSSP>2.0.CO;2
10.1016/j.tem.2019.09.007
10.3390/ijms20225815
10.1089/ars.2011.4394
10.1016/S0531-5565(02)00128-6
10.1016/0197-4580(92)90088-F
10.1016/j.abb.2007.03.034
10.1523/JNEUROSCI.0699-18.2018
10.1007/s12192-018-0877-2
10.1371/journal.pone.0007719
10.1091/mbc.e07-10-1048
10.1038/jid.2010.383
10.1016/j.bbadis.2005.08.003
10.1016/j.abb.2004.05.006
10.1111/j.1471-4159.2004.02453.x
10.1016/S0014-5793(03)00582-9
10.20944/preprints201807.0137.v1
10.1016/j.bbamcr.2009.11.012
10.1155/2020/9369524
ContentType Journal Article
Copyright 2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
2020 by the authors. 2020
Copyright_xml – notice: 2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: 2020 by the authors. 2020
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
8FD
8FE
8FH
ABUWG
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
FR3
GNUQQ
HCIFZ
LK8
M7P
P64
PHGZM
PHGZT
PIMPY
PKEHL
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
RC3
7X8
5PM
DOA
DOI 10.3390/cells9051308
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
Technology Research Database
ProQuest SciTech Collection
ProQuest Natural Science Collection
ProQuest Central
ProQuest Central UK/Ireland
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Natural Science Collection
ProQuest One
ProQuest Central
Engineering Research Database
ProQuest Central Student
SciTech Premium Collection
Biological Sciences
Biological Science Database
Biotechnology and BioEngineering Abstracts
ProQuest Central Premium
ProQuest One Academic (New)
Publicly Available Content Database
ProQuest One Academic Middle East (New)
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
Genetics Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
Publicly Available Content Database
ProQuest Central Student
Technology Research Database
ProQuest One Academic Middle East (New)
ProQuest Central Essentials
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Central China
ProQuest Central
ProQuest One Applied & Life Sciences
Genetics Abstracts
Natural Science Collection
ProQuest Central Korea
Biological Science Collection
ProQuest Central (New)
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
Biological Science Database
ProQuest SciTech Collection
Biotechnology and BioEngineering Abstracts
ProQuest One Academic UKI Edition
Engineering Research Database
ProQuest One Academic
ProQuest One Academic (New)
MEDLINE - Academic
DatabaseTitleList MEDLINE - Academic
MEDLINE


Publicly Available Content Database
CrossRef
Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 3
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 4
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2073-4409
ExternalDocumentID oai_doaj_org_article_df5ea4b72ba744c0b44d66634604fe0d
PMC7291254
32456366
10_3390_cells9051308
Genre Research Support, Non-U.S. Gov't
Journal Article
Review
GroupedDBID 53G
5VS
8FE
8FH
AADQD
AAFWJ
AAYXX
ABDBF
ACUHS
ADBBV
AFKRA
AFPKN
AFZYC
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BBNVY
BCNDV
BENPR
BHPHI
CCPQU
CITATION
DIK
EBD
ESX
GROUPED_DOAJ
HCIFZ
HYE
IAO
IHR
KQ8
LK8
M48
M7P
MODMG
M~E
OK1
PGMZT
PHGZM
PHGZT
PIMPY
PROAC
RPM
CGR
CUY
CVF
ECM
EIF
NPM
PQGLB
8FD
ABUWG
AZQEC
DWQXO
FR3
GNUQQ
P64
PKEHL
PQEST
PQQKQ
PQUKI
PRINS
RC3
7X8
5PM
PUEGO
ID FETCH-LOGICAL-c478t-fd56411096ec5efb166025fde5a5d9bb344ab895a76ce71395e4a9723d76b2d33
IEDL.DBID DOA
ISSN 2073-4409
IngestDate Wed Aug 27 01:31:58 EDT 2025
Thu Aug 21 18:18:19 EDT 2025
Fri Jul 11 08:44:23 EDT 2025
Fri Jul 25 11:56:44 EDT 2025
Mon Jul 21 06:09:41 EDT 2025
Tue Jul 01 01:06:03 EDT 2025
Thu Apr 24 22:59:25 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 5
Keywords autophagy
aging
molecular chaperones
ubiquitin-proteasomal system
Language English
License https://creativecommons.org/licenses/by/4.0
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c478t-fd56411096ec5efb166025fde5a5d9bb344ab895a76ce71395e4a9723d76b2d33
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
ObjectType-Review-3
content type line 23
ORCID 0000-0002-8775-7713
OpenAccessLink https://doaj.org/article/df5ea4b72ba744c0b44d66634604fe0d
PMID 32456366
PQID 2407649618
PQPubID 2032536
ParticipantIDs doaj_primary_oai_doaj_org_article_df5ea4b72ba744c0b44d66634604fe0d
pubmedcentral_primary_oai_pubmedcentral_nih_gov_7291254
proquest_miscellaneous_2407313201
proquest_journals_2407649618
pubmed_primary_32456366
crossref_citationtrail_10_3390_cells9051308
crossref_primary_10_3390_cells9051308
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 20200524
PublicationDateYYYYMMDD 2020-05-24
PublicationDate_xml – month: 5
  year: 2020
  text: 20200524
  day: 24
PublicationDecade 2020
PublicationPlace Switzerland
PublicationPlace_xml – name: Switzerland
– name: Basel
PublicationTitle Cells (Basel, Switzerland)
PublicationTitleAlternate Cells
PublicationYear 2020
Publisher MDPI AG
MDPI
Publisher_xml – name: MDPI AG
– name: MDPI
References Zoubeidi (ref_54) 2012; 44
Connell (ref_92) 2000; 3
Dasuri (ref_116) 2011; 51
Ling (ref_50) 2017; 8
ref_12
Hipp (ref_5) 2019; 20
Cuervo (ref_85) 2000; 275
Lechler (ref_28) 2017; 18
Wen (ref_57) 2004; 15
Mayer (ref_43) 2013; 38
Imai (ref_127) 2003; 22
McDonough (ref_142) 2003; 8
Kawamata (ref_63) 2008; 19
Heydari (ref_31) 1993; 13
Njomen (ref_120) 2019; 62
Hsu (ref_23) 2003; 300
Athonvarangkul (ref_70) 2015; 847
Sha (ref_145) 2017; 36
Huang (ref_109) 2000; 98
Vernace (ref_99) 2007; 21
Santagata (ref_19) 2014; 158
Tomita (ref_98) 2018; 39
Galluzzi (ref_59) 2017; 36
ref_24
Chondrogianni (ref_117) 2003; 278
Grune (ref_126) 2011; 51
Guo (ref_146) 2015; 31
ref_22
Nijman (ref_91) 2005; 123
Nardai (ref_38) 2002; 37
Arias (ref_78) 2015; 59
ref_27
Taylor (ref_123) 2005; 10
Bandyopadhyay (ref_77) 2008; 28
Aguilera (ref_72) 2013; 47
Kabbage (ref_150) 2008; 65
Kabeya (ref_66) 2000; 19
Pardue (ref_30) 1992; 13
Motosugi (ref_119) 2019; 6
Gamerdinger (ref_152) 2009; 28
Cuervo (ref_86) 2012; 8
Karvinen (ref_40) 2016; 79
ref_73
Komatsu (ref_132) 2006; 441
Aparicio (ref_130) 2020; 16
Scott (ref_96) 2015; 41
Meng (ref_14) 2011; 30
Shang (ref_93) 2014; 446
Han (ref_139) 2016; 15
Taldone (ref_44) 2014; 35
Yamaguchi (ref_55) 2007; 62
Behl (ref_151) 2017; 10
ref_147
Suzuki (ref_67) 2013; 126
Kaushik (ref_83) 2008; 445
Heydari (ref_25) 1998; 241
Vasilaki (ref_37) 2002; 25
Brehme (ref_42) 2014; 9
Papaevgeniou (ref_9) 2016; 1449
Oda (ref_13) 2018; 131
Arias (ref_80) 2019; 31
Njemini (ref_35) 2008; 7
Frakes (ref_10) 2017; 66
Kametaka (ref_61) 1998; 273
Lee (ref_39) 2011; 46
Takayama (ref_149) 2001; 3
Rajasekaran (ref_58) 2007; 130
Lizama (ref_148) 2018; 38
Piec (ref_41) 2005; 19
Sigmond (ref_68) 2008; 4
Zeng (ref_113) 2005; 126
Chondrogianni (ref_118) 2005; 280
Greussing (ref_107) 2011; 131
Carra (ref_53) 2017; 22
Dai (ref_143) 2003; 22
Chung (ref_36) 2006; 1762
Ferrington (ref_114) 2005; 19
Dues (ref_11) 2016; 8
Husom (ref_102) 2004; 421
Zheng (ref_88) 2017; 86
Khan (ref_94) 2019; 1865
Barna (ref_128) 2018; 75
Mendillo (ref_18) 2012; 150
McArdle (ref_47) 2003; 18
Li (ref_138) 2019; 1206
Bossola (ref_103) 2008; 9
Carvalho (ref_3) 2016; 1449
Xiao (ref_21) 1999; 18
Blasco (ref_2) 2013; 153
Cuervo (ref_76) 1996; 273
Breusing (ref_110) 2009; 130
Vihervaara (ref_16) 2014; 127
Dong (ref_81) 2020; 11
Cassidy (ref_71) 2020; 11
Petropoulos (ref_106) 2000; 55
Ho (ref_82) 2019; 16
Labbadia (ref_4) 2015; 84
Arrigo (ref_52) 2017; 22
Fimia (ref_64) 2007; 447
Dasuri (ref_111) 2009; 130
Kim (ref_134) 2007; 462
Bejarano (ref_74) 2010; 7
Gupte (ref_56) 2010; 472
Nezis (ref_133) 2012; 17
Kevei (ref_6) 2017; 591
Glick (ref_65) 2010; 221
Viteri (ref_104) 2004; 427
Sarbassov (ref_135) 2005; 280
Walker (ref_20) 2003; 17
Ding (ref_121) 2003; 546
Kapphahn (ref_112) 2007; 84
Suryadinata (ref_89) 2014; 3
Tawo (ref_95) 2017; 169
Tandara (ref_34) 2006; 132
Yang (ref_60) 2020; 27
Fonager (ref_33) 2002; 37
Dai (ref_137) 2014; 34
Watanabe (ref_129) 2016; 13
Beedholm (ref_122) 2004; 9
Hansen (ref_8) 2018; 19
Ullah (ref_144) 2020; 295
Hwang (ref_97) 2007; 62
Bozaykut (ref_125) 2020; 2020
Echeverria (ref_46) 2010; 1803
Piskovatska (ref_140) 2018; 20
Prodromou (ref_48) 2016; 473
Carnemolla (ref_26) 2014; 23
Bulteau (ref_108) 2002; 397
McCormick (ref_153) 2018; 105
Bozaykut (ref_15) 2013; 89
ref_45
Loeffler (ref_75) 2019; 11
Kirisako (ref_90) 2006; 25
Andersson (ref_101) 2013; 5
Kiffin (ref_84) 2007; 120
Li (ref_17) 2017; 27
Blake (ref_29) 1991; 260
Neckers (ref_49) 2018; 23
LeComte (ref_124) 2010; 29
Joshi (ref_141) 2016; 9
Lopez (ref_32) 1998; 104
Koren (ref_87) 2018; 173
Su (ref_136) 2016; 18
Janssens (ref_51) 2019; 27
Kim (ref_62) 2011; 13
Alfaro (ref_79) 2019; 9
Kudryashova (ref_1) 2020; 20
Thibaudeau (ref_100) 2018; 9
Korovila (ref_7) 2017; 13
Simonsen (ref_69) 2007; 4
Kumsta (ref_131) 2019; 10
Ponnappan (ref_105) 2007; 39
Kabashi (ref_115) 2004; 89
References_xml – volume: 127
  start-page: 261
  year: 2014
  ident: ref_16
  article-title: HSF1 at a glance
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.132605
– volume: 27
  start-page: 858
  year: 2020
  ident: ref_60
  article-title: Autophagy and disease: Unanswered questions
  publication-title: Cell Death Differ.
  doi: 10.1038/s41418-019-0480-9
– volume: 105
  start-page: 247
  year: 2018
  ident: ref_153
  article-title: The effect of aging on the autophagic and heat shock response in human peripheral blood mononuclear cells
  publication-title: Physiol. Int.
  doi: 10.1556/2060.105.2018.3.20
– volume: 1449
  start-page: 1
  year: 2016
  ident: ref_9
  article-title: UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review
  publication-title: Adv. Struct. Saf. Stud.
– volume: 15
  start-page: 416
  year: 2016
  ident: ref_139
  article-title: AMPK activation protects cells from oxidative stress-induced senescence via autophagic flux restoration and intracellular NAD + elevation
  publication-title: Aging Cell
  doi: 10.1111/acel.12446
– volume: 15
  start-page: 2335
  year: 2004
  ident: ref_57
  article-title: Desmin Aggregate Formation by R120G αB-Crystallin Is Caused by Altered Filament Interactions and Is Dependent upon Network Status in Cells
  publication-title: Mol. Boil. Cell
  doi: 10.1091/mbc.e03-12-0893
– volume: 10
  start-page: 177
  year: 2017
  ident: ref_151
  article-title: The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease
  publication-title: Front. Mol. Neurosci.
  doi: 10.3389/fnmol.2017.00177
– volume: 16
  start-page: 347
  year: 2019
  ident: ref_82
  article-title: Age-dependent accumulation of oligomeric SNCA/α-synuclein from impaired degradation in mutant LRRK2 knockin mouse model of Parkinson disease: Role for therapeutic activation of chaperone-mediated autophagy (CMA)
  publication-title: Autophagy
  doi: 10.1080/15548627.2019.1603545
– volume: 173
  start-page: 1622
  year: 2018
  ident: ref_87
  article-title: The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting C-Terminal Degrons
  publication-title: Cell
  doi: 10.1016/j.cell.2018.04.028
– volume: 22
  start-page: 601
  year: 2017
  ident: ref_53
  article-title: The growing world of small heat shock proteins: From structure to functions
  publication-title: Cell Stress Chaperones
  doi: 10.1007/s12192-017-0787-8
– volume: 278
  start-page: 28026
  year: 2003
  ident: ref_117
  article-title: Central Role of the Proteasome in Senescence and Survival of Human Fibroblasts
  publication-title: J. Boil. Chem.
  doi: 10.1074/jbc.M301048200
– volume: 10
  start-page: 230
  year: 2005
  ident: ref_123
  article-title: Proteasome activity or expression is not altered by activation of the heat shock transcription factor Hsf1 in cultured fibroblasts or myoblasts
  publication-title: Cell Stress Chaperones
  doi: 10.1379/CSC-119R.1
– volume: 126
  start-page: 2534
  year: 2013
  ident: ref_67
  article-title: Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae
  publication-title: J. Cell Sci.
– volume: 295
  start-page: 4696
  year: 2020
  ident: ref_144
  article-title: The E3 ubiquitin ligase STUB1 attenuates cell senescence by promoting the ubiquitination and degradation of the core circadian regulator BMAL1
  publication-title: J. Boil. Chem.
  doi: 10.1074/jbc.RA119.011280
– volume: 84
  start-page: 646
  year: 2007
  ident: ref_112
  article-title: Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina
  publication-title: Exp. Eye Res.
  doi: 10.1016/j.exer.2006.12.002
– volume: 241
  start-page: 404
  year: 1998
  ident: ref_25
  article-title: The Expression of Heat Shock Protein 70 Decreases with Cellular Senescencein Vitroand in Cells Derived from Young and Old Human Subjects
  publication-title: Exp. Cell Res.
  doi: 10.1006/excr.1998.4069
– volume: 22
  start-page: 517
  year: 2017
  ident: ref_52
  article-title: Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell
  publication-title: Cell Stress Chaperones
  doi: 10.1007/s12192-017-0765-1
– volume: 19
  start-page: 1
  year: 2005
  ident: ref_114
  article-title: Altered proteasome structure, function, and oxidation in aged muscle
  publication-title: FASEB J.
  doi: 10.1096/fj.04-2578fje
– volume: 84
  start-page: 435
  year: 2015
  ident: ref_4
  article-title: The biology of proteostasis in aging and disease
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev-biochem-060614-033955
– volume: 123
  start-page: 773
  year: 2005
  ident: ref_91
  article-title: A Genomic and Functional Inventory of Deubiquitinating Enzymes
  publication-title: Cell
  doi: 10.1016/j.cell.2005.11.007
– volume: 39
  start-page: 799
  year: 2007
  ident: ref_105
  article-title: Lower expression of catalytic and structural subunits of the proteasome contributes to decreased proteolysis in peripheral blood T lymphocytes during aging
  publication-title: Int. J. Biochem. Cell Boil.
  doi: 10.1016/j.biocel.2007.01.002
– volume: 31
  start-page: 469
  year: 2015
  ident: ref_146
  article-title: Regulation of autophagic flux by CHIP
  publication-title: Neurosci. Bull.
  doi: 10.1007/s12264-015-1543-7
– volume: 21
  start-page: 2672
  year: 2007
  ident: ref_99
  article-title: Aging perturbs 26S proteasome assembly in Drosophila melanogaster
  publication-title: FASEB J.
  doi: 10.1096/fj.06-6751com
– volume: 30
  start-page: 2836
  year: 2011
  ident: ref_14
  article-title: Heat shock protein Hsp72 plays an essential role in Her2-induced mammary tumorigenesis
  publication-title: Oncogene
  doi: 10.1038/onc.2011.5
– volume: 421
  start-page: 67
  year: 2004
  ident: ref_102
  article-title: Altered proteasome function and subunit composition in aged muscle
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2003.10.010
– volume: 36
  start-page: 1811
  year: 2017
  ident: ref_59
  article-title: Molecular definitions of autophagy and related processes
  publication-title: Embo J.
  doi: 10.15252/embj.201796697
– volume: 7
  start-page: 29
  year: 2010
  ident: ref_74
  article-title: Chaperone-Mediated Autophagy
  publication-title: Proc. Am. Thorac. Soc.
  doi: 10.1513/pats.200909-102JS
– volume: 126
  start-page: 760
  year: 2005
  ident: ref_113
  article-title: Proteasomal activity in brain differs between species and brain regions and changes with age
  publication-title: Mech. Ageing Dev.
  doi: 10.1016/j.mad.2005.01.008
– volume: 51
  start-page: 1355
  year: 2011
  ident: ref_126
  article-title: HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
  publication-title: Free Radic. Boil. Med.
  doi: 10.1016/j.freeradbiomed.2011.06.015
– volume: 13
  start-page: 133
  year: 2016
  ident: ref_129
  article-title: HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis
  publication-title: Autophagy
  doi: 10.1080/15548627.2016.1248018
– volume: 6
  start-page: 30
  year: 2019
  ident: ref_119
  article-title: Dynamic Regulation of Proteasome Expression
  publication-title: Front. Mol. Biosci.
  doi: 10.3389/fmolb.2019.00030
– volume: 13
  start-page: 550
  year: 2017
  ident: ref_7
  article-title: Proteostasis, oxidative stress and aging
  publication-title: Redox Boil.
  doi: 10.1016/j.redox.2017.07.008
– volume: 98
  start-page: 149
  year: 2000
  ident: ref_109
  article-title: Decreased levels of proteasome activity and proteasome expression in aging spinal cord
  publication-title: Neuroscience
  doi: 10.1016/S0306-4522(00)00067-1
– volume: 11
  start-page: 49
  year: 2019
  ident: ref_75
  article-title: Influence of Normal Aging on Brain Autophagy: A Complex Scenario
  publication-title: Front. Aging Neurosci.
  doi: 10.3389/fnagi.2019.00049
– volume: 13
  start-page: 2909
  year: 1993
  ident: ref_31
  article-title: Expression of heat shock protein 70 is altered by age and diet at the level of transcription
  publication-title: Mol. Cell. Boil.
– volume: 75
  start-page: 2897
  year: 2018
  ident: ref_128
  article-title: Roles of heat shock factor 1 beyond the heat shock response
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-018-2836-6
– volume: 22
  start-page: 5446
  year: 2003
  ident: ref_143
  article-title: CHIP activates HSF1 and confers protection against apoptosis and cellular stress
  publication-title: Embo J.
  doi: 10.1093/emboj/cdg529
– volume: 20
  start-page: e1900408
  year: 2020
  ident: ref_1
  article-title: Aging Biomarkers: From Functional Tests to Multi-Omics Approaches
  publication-title: Proteomics
  doi: 10.1002/pmic.201900408
– ident: ref_73
  doi: 10.3390/ijms18112351
– volume: 39
  start-page: e00426-18
  year: 2018
  ident: ref_98
  article-title: Specific Modification of Aged Proteasomes Revealed by Tag-Exchangeable Knock-In Mice
  publication-title: Mol. Cell. Boil.
  doi: 10.1128/MCB.00426-18
– volume: 1449
  start-page: 71
  year: 2016
  ident: ref_3
  article-title: Review and Literature Mining on Proteostasis Factors and Cancer
  publication-title: Adv. Struct. Saf. Stud.
– volume: 23
  start-page: 3641
  year: 2014
  ident: ref_26
  article-title: Contesting the dogma of an age-related heat shock response impairment: Implications for cardiac-specific age-related disorders
  publication-title: Hum. Mol. Genet.
  doi: 10.1093/hmg/ddu073
– volume: 8
  start-page: 303
  year: 2003
  ident: ref_142
  article-title: CHIP: A link between the chaperone and proteasome systems
  publication-title: Cell Stress Chaperones
  doi: 10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2
– volume: 89
  start-page: 238
  year: 2013
  ident: ref_15
  article-title: The role of heat stress on the age related protein carbonylation
  publication-title: J. Proteom.
  doi: 10.1016/j.jprot.2013.06.025
– volume: 153
  start-page: 1194
  year: 2013
  ident: ref_2
  article-title: The Hallmarks of Aging
  publication-title: Cell
  doi: 10.1016/j.cell.2013.05.039
– ident: ref_24
  doi: 10.1371/journal.pone.0017369
– volume: 397
  start-page: 298
  year: 2002
  ident: ref_108
  article-title: Age-Dependent Declines in Proteasome Activity in the Heart
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1006/abbi.2001.2663
– volume: 10
  start-page: 1
  year: 2019
  ident: ref_131
  article-title: The autophagy receptor p62/SQST-1 promotes proteostasis and longevity in C. elegans by inducing autophagy
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-019-13540-4
– volume: 446
  start-page: 387
  year: 2014
  ident: ref_93
  article-title: Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2014.02.124
– volume: 132
  start-page: 32
  year: 2006
  ident: ref_34
  article-title: Age Effect on HSP70: Decreased Resistance to Ischemic and Oxidative Stress in HDF
  publication-title: J. Surg. Res.
  doi: 10.1016/j.jss.2005.09.019
– volume: 16
  start-page: 772
  year: 2020
  ident: ref_130
  article-title: The selective autophagy receptor SQSTM1/p62 improves lifespan and proteostasis in an evolutionarily conserved manner
  publication-title: Autophagy
  doi: 10.1080/15548627.2020.1725404
– volume: 62
  start-page: 6469
  year: 2019
  ident: ref_120
  article-title: Proteasome Activation as a New Therapeutic Approach to Target Proteotoxic Disorders
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.9b00101
– volume: 17
  start-page: 1
  year: 2003
  ident: ref_20
  article-title: Heat shock factor functions at the convergence of the stress response and developmental pathways in Caenorhabditis elegans
  publication-title: FASEB J.
  doi: 10.1096/fj.03-0164fje
– volume: 41
  start-page: 896
  year: 2015
  ident: ref_96
  article-title: Protein Expression of Proteasome Subunits in Elderly Patients with Schizophrenia
  publication-title: Neuropsychopharmacology
  doi: 10.1038/npp.2015.219
– volume: 11
  start-page: 307
  year: 2020
  ident: ref_71
  article-title: Temporal inhibition of autophagy reveals segmental reversal of ageing with increased cancer risk
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-019-14187-x
– volume: 37
  start-page: 1257
  year: 2002
  ident: ref_38
  article-title: Chaperone function and chaperone overload in the aged. A preliminary analysis
  publication-title: Exp. Gerontol.
  doi: 10.1016/S0531-5565(02)00134-1
– volume: 47
  start-page: 1
  year: 2013
  ident: ref_72
  article-title: Causes of Genome Instability
  publication-title: Annu. Rev. Genet.
  doi: 10.1146/annurev-genet-111212-133232
– volume: 46
  start-page: 768
  year: 2011
  ident: ref_39
  article-title: Heat shock protein 90 and its cochaperone, p23, are markedly increased in the aged gerbil hippocampus
  publication-title: Exp. Gerontol.
  doi: 10.1016/j.exger.2011.05.002
– volume: 36
  start-page: 2544
  year: 2017
  ident: ref_145
  article-title: STUB 1 regulates TFEB -induced autophagy-lysosome pathway
  publication-title: Embo J.
  doi: 10.15252/embj.201796699
– volume: 28
  start-page: 5747
  year: 2008
  ident: ref_77
  article-title: The Chaperone-Mediated Autophagy Receptor Organizes in Dynamic Protein Complexes at the Lysosomal Membrane
  publication-title: Mol. Cell. Boil.
  doi: 10.1128/MCB.02070-07
– volume: 19
  start-page: 5720
  year: 2000
  ident: ref_66
  article-title: LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
  publication-title: Embo J.
  doi: 10.1093/emboj/19.21.5720
– volume: 29
  start-page: 4216
  year: 2010
  ident: ref_124
  article-title: Roles of heat shock factor 1 and 2 in response to proteasome inhibition: Consequence on p53 stability
  publication-title: Oncogene
  doi: 10.1038/onc.2010.171
– volume: 18
  start-page: 1
  year: 2003
  ident: ref_47
  article-title: Overexpression of HSP70 in mouse skeletal muscle protects against muscle damage and age-related muscle dysfunction
  publication-title: FASEB J.
  doi: 10.1096/fj.03-0395fje
– volume: 221
  start-page: 3
  year: 2010
  ident: ref_65
  article-title: Autophagy: Cellular and molecular mechanisms
  publication-title: J. Pathol.
  doi: 10.1002/path.2697
– volume: 273
  start-page: 501
  year: 1996
  ident: ref_76
  article-title: A Receptor for the Selective Uptake and Degradation of Proteins by Lysosomes
  publication-title: Science
  doi: 10.1126/science.273.5274.501
– volume: 104
  start-page: 59
  year: 1998
  ident: ref_32
  article-title: Effect of age and dietary restriction on expression of heat shock protein 70 in rat alveolar macrophages
  publication-title: Mech. Ageing Dev.
  doi: 10.1016/S0047-6374(98)00052-9
– volume: 4
  start-page: 176
  year: 2007
  ident: ref_69
  article-title: Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
  publication-title: Autophagy
  doi: 10.4161/auto.5269
– volume: 1865
  start-page: 1745
  year: 2019
  ident: ref_94
  article-title: Conserved signaling pathways genetically associated with longevity across the species
  publication-title: Biochim. Et Biophys. Acta (BBA) Mol. Basis Dis.
  doi: 10.1016/j.bbadis.2018.09.001
– volume: 20
  start-page: 421
  year: 2019
  ident: ref_5
  article-title: The proteostasis network and its decline in ageing
  publication-title: Nat. Rev. Mol. Cell Boil.
  doi: 10.1038/s41580-019-0101-y
– volume: 13
  start-page: 132
  year: 2011
  ident: ref_62
  article-title: AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
  publication-title: Nature
  doi: 10.1038/nature10604
– volume: 300
  start-page: 1142
  year: 2003
  ident: ref_23
  article-title: Regulation of Aging and Age-Related Disease by DAF-16 and Heat-Shock Factor
  publication-title: Science
  doi: 10.1126/science.1083701
– volume: 9
  start-page: 5115
  year: 2016
  ident: ref_141
  article-title: A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?
  publication-title: Front. Mol. Neurosci.
  doi: 10.3389/fnmol.2016.00093
– volume: 445
  start-page: 227
  year: 2008
  ident: ref_83
  article-title: Chaperone-Mediated Autophagy
  publication-title: Breast Cancer
– volume: 3
  start-page: 674
  year: 2014
  ident: ref_89
  article-title: Mechanisms of Generating Polyubiquitin Chains of Different Topology
  publication-title: Cells
  doi: 10.3390/cells3030674
– volume: 9
  start-page: 1135
  year: 2014
  ident: ref_42
  article-title: A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.09.042
– volume: 275
  start-page: 31505
  year: 2000
  ident: ref_85
  article-title: Age-related Decline in Chaperone-mediated Autophagy
  publication-title: J. Boil. Chem.
  doi: 10.1074/jbc.M002102200
– volume: 9
  start-page: 261
  year: 2008
  ident: ref_103
  article-title: Proteasome activities in the rectus abdominis muscle of young and older individuals
  publication-title: Biogerontology
  doi: 10.1007/s10522-008-9135-9
– volume: 472
  start-page: 90
  year: 2010
  ident: ref_56
  article-title: Age-related changes in HSP25 expression in basal ganglia and cortex of F344/BN rats
  publication-title: Neurosci. Lett.
  doi: 10.1016/j.neulet.2010.01.049
– volume: 18
  start-page: 454
  year: 2017
  ident: ref_28
  article-title: Reduced Insulin/IGF-1 Signaling Restores the Dynamic Properties of Key Stress Granule Proteins during Aging
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2016.12.033
– volume: 59
  start-page: 270
  year: 2015
  ident: ref_78
  article-title: Lysosomal mTORC2/PHLPP1/Akt Regulate Chaperone-Mediated Autophagy
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2015.05.030
– volume: 441
  start-page: 880
  year: 2006
  ident: ref_132
  article-title: Loss of autophagy in the central nervous system causes neurodegeneration in mice
  publication-title: Nature
  doi: 10.1038/nature04723
– volume: 473
  start-page: 2439
  year: 2016
  ident: ref_48
  article-title: Mechanisms of Hsp90 regulation
  publication-title: Biochem. J.
  doi: 10.1042/BCJ20160005
– ident: ref_12
  doi: 10.3390/ijms20184507
– volume: 5
  start-page: 802
  year: 2013
  ident: ref_101
  article-title: Enhancing protein disaggregation restores proteasome activity in aged cells
  publication-title: Aging
  doi: 10.18632/aging.100613
– volume: 3
  start-page: E237
  year: 2001
  ident: ref_149
  article-title: Molecular chaperone targeting and regulation by BAG family proteins
  publication-title: Nature
– volume: 8
  start-page: 777
  year: 2016
  ident: ref_11
  article-title: Aging causes decreased resistance to multiple stresses and a failure to activate specific stress response pathways
  publication-title: Aging
  doi: 10.18632/aging.100939
– volume: 18
  start-page: 5943
  year: 1999
  ident: ref_21
  article-title: HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
  publication-title: Embo J.
  doi: 10.1093/emboj/18.21.5943
– volume: 22
  start-page: 3557
  year: 2003
  ident: ref_127
  article-title: The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome
  publication-title: Embo J.
  doi: 10.1093/emboj/cdg349
– volume: 55
  start-page: B220
  year: 2000
  ident: ref_106
  article-title: Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells
  publication-title: J. Gerontol. Ser. A Boil. Sci. Med. Sci.
– volume: 35
  start-page: 592
  year: 2014
  ident: ref_44
  article-title: Selective targeting of the stress chaperome as a therapeutic strategy
  publication-title: Trends Pharmacol. Sci.
  doi: 10.1016/j.tips.2014.09.001
– volume: 51
  start-page: 1727
  year: 2011
  ident: ref_116
  article-title: Proteasome alterations during adipose differentiation and aging: Links to impaired adipocyte differentiation and development of oxidative stress
  publication-title: Free Radic. Boil. Med.
  doi: 10.1016/j.freeradbiomed.2011.08.001
– volume: 65
  start-page: 1390
  year: 2008
  ident: ref_150
  article-title: The BAG proteins: A ubiquitous family of chaperone regulators
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-008-7535-2
– volume: 158
  start-page: 564
  year: 2014
  ident: ref_19
  article-title: The reprogramming of tumor stroma by HSF1 is a potent enabler of malignancy
  publication-title: Cell
  doi: 10.1016/j.cell.2014.05.045
– volume: 27
  start-page: 467
  year: 2019
  ident: ref_51
  article-title: Transcriptomics-Based Screening Identifies Pharmacological Inhibition of Hsp90 as a Means to Defer Aging
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2019.03.044
– volume: 447
  start-page: 1121
  year: 2007
  ident: ref_64
  article-title: Ambra1 regulates autophagy and development of the nervous system
  publication-title: Nature
  doi: 10.1038/nature05925
– volume: 20
  start-page: 33
  year: 2018
  ident: ref_140
  article-title: Metformin as a geroprotector: Experimental and clinical evidence
  publication-title: Biogerontology
  doi: 10.1007/s10522-018-9773-5
– volume: 66
  start-page: 761
  year: 2017
  ident: ref_10
  article-title: The UPR ER: Sensor and Coordinator of Organismal Homeostasis
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2017.05.031
– ident: ref_45
  doi: 10.3390/ijms20246195
– volume: 150
  start-page: 549
  year: 2012
  ident: ref_18
  article-title: HSF1 Drives a Transcriptional Program Distinct from Heat Shock to Support Highly Malignant Human Cancers
  publication-title: Cell
  doi: 10.1016/j.cell.2012.06.031
– volume: 19
  start-page: 1143
  year: 2005
  ident: ref_41
  article-title: Differential proteome analysis of aging in rat skeletal muscle
  publication-title: FASEB J.
  doi: 10.1096/fj.04-3084fje
– volume: 9
  start-page: 1097
  year: 2018
  ident: ref_100
  article-title: A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-018-03509-0
– volume: 273
  start-page: 22284
  year: 1998
  ident: ref_61
  article-title: Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.35.22284
– volume: 27
  start-page: 895
  year: 2017
  ident: ref_17
  article-title: Rethinking HSF1 in Stress, Development, and Organismal Health
  publication-title: Trends Cell Boil.
  doi: 10.1016/j.tcb.2017.08.002
– volume: 847
  start-page: 73
  year: 2015
  ident: ref_70
  article-title: Autophagy and aging
  publication-title: Single Mol. Single Cell Seq.
– volume: 25
  start-page: 4877
  year: 2006
  ident: ref_90
  article-title: A ubiquitin ligase complex assembles linear polyubiquitin chains
  publication-title: Embo J.
  doi: 10.1038/sj.emboj.7601360
– volume: 25
  start-page: 902
  year: 2002
  ident: ref_37
  article-title: Attenuated HSP70 response in skeletal muscle of aged rats following contractile activity
  publication-title: Muscle Nerve
  doi: 10.1002/mus.10094
– volume: 260
  start-page: R663
  year: 1991
  ident: ref_29
  article-title: Concomitant decline in heat-induced hyperthermia and HSP70 mRNA expression in aged rats
  publication-title: Am. J. Physiol. Integr. Comp. Physiol.
  doi: 10.1152/ajpregu.1991.260.4.R663
– volume: 8
  start-page: 1152
  year: 2012
  ident: ref_86
  article-title: Dietary lipids and aging compromise chaperone-mediated autophagy by similar mechanisms
  publication-title: Autophagy
  doi: 10.4161/auto.20649
– volume: 8
  start-page: 422
  year: 2017
  ident: ref_50
  article-title: Identification of HSP90 inhibitors as a novel class of senolytics
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-017-00314-z
– volume: 169
  start-page: 470
  year: 2017
  ident: ref_95
  article-title: The Ubiquitin Ligase CHIP Integrates Proteostasis and Aging by Regulation of Insulin Receptor Turnover
  publication-title: Cell
  doi: 10.1016/j.cell.2017.04.003
– volume: 591
  start-page: 2616
  year: 2017
  ident: ref_6
  article-title: Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis
  publication-title: FEBS Lett.
  doi: 10.1002/1873-3468.12750
– volume: 19
  start-page: 579
  year: 2018
  ident: ref_8
  article-title: Autophagy as a promoter of longevity: Insights from model organisms
  publication-title: Nat. Rev. Mol. Cell Boil.
  doi: 10.1038/s41580-018-0033-y
– volume: 131
  start-page: jcs210724
  year: 2018
  ident: ref_13
  article-title: Acute HSF1 depletion induces cellular senescence through the MDM2-p53-p21 pathway in human diploid fibroblasts
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.210724
– volume: 79
  start-page: 46
  year: 2016
  ident: ref_40
  article-title: Effects of intrinsic aerobic capacity, aging and voluntary running on skeletal muscle sirtuins and heat shock proteins
  publication-title: Exp. Gerontol.
  doi: 10.1016/j.exger.2016.03.015
– volume: 38
  start-page: 507
  year: 2013
  ident: ref_43
  article-title: Hsp70 chaperone dynamics and molecular mechanism
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2013.08.001
– volume: 44
  start-page: 1646
  year: 2012
  ident: ref_54
  article-title: Small heat shock proteins in cancer therapy and prognosis
  publication-title: Int. J. Biochem. Cell Boil.
  doi: 10.1016/j.biocel.2012.04.010
– volume: 120
  start-page: 782
  year: 2007
  ident: ref_84
  article-title: Altered dynamics of the lysosomal receptor for chaperone-mediated autophagy with age
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.001073
– volume: 280
  start-page: 11840
  year: 2005
  ident: ref_118
  article-title: Overexpression of Proteasome 5 Assembled Subunit Increases the Amount of Proteasome and Confers Ameliorated Response to Oxidative Stress and Higher Survival Rates
  publication-title: J. Boil. Chem.
  doi: 10.1074/jbc.M413007200
– volume: 18
  start-page: 527
  year: 2016
  ident: ref_136
  article-title: HSF1 critically attunes proteotoxic stress sensing by mTORC1 to combat stress and promote growth
  publication-title: Nature
– volume: 280
  start-page: 39505
  year: 2005
  ident: ref_135
  article-title: Redox Regulation of the Nutrient-sensitive Raptor-mTOR Pathway and Complex
  publication-title: J. Boil. Chem.
  doi: 10.1074/jbc.M506096200
– volume: 130
  start-page: 777
  year: 2009
  ident: ref_111
  article-title: Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver
  publication-title: Mech. Ageing Dev.
  doi: 10.1016/j.mad.2009.10.003
– volume: 1206
  start-page: 85
  year: 2019
  ident: ref_138
  article-title: AMPK and Autophagy
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-981-15-0602-4_4
– volume: 34
  start-page: 275
  year: 2014
  ident: ref_137
  article-title: Suppression of the HSF 1-mediated proteotoxic stress response by the metabolic stress sensor AMPK
  publication-title: Embo J.
  doi: 10.15252/embj.201489062
– volume: 9
  start-page: 778
  year: 2019
  ident: ref_79
  article-title: Chaperone Mediated Autophagy in the Crosstalk of Neurodegenerative Diseases and Metabolic Disorders
  publication-title: Front. Endocrinol.
  doi: 10.3389/fendo.2018.00778
– volume: 11
  start-page: 645
  year: 2020
  ident: ref_81
  article-title: Monitoring spatiotemporal changes in chaperone-mediated autophagy in vivo
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-019-14164-4
– volume: 7
  start-page: 498
  year: 2008
  ident: ref_35
  article-title: Aging-related differences in basal heatshock protein 70 levels in lymphocytes are linked to altered frequencies of lymphocyte subsets
  publication-title: Aging Cell
  doi: 10.1111/j.1474-9726.2008.00401.x
– volume: 4
  start-page: 330
  year: 2008
  ident: ref_68
  article-title: Longevity pathways converge on autophagy genes to regulate life span in Caenorhabditis elegans
  publication-title: Autophagy
  doi: 10.4161/auto.5618
– volume: 130
  start-page: 427
  year: 2007
  ident: ref_58
  article-title: Human αB-Crystallin Mutation Causes Oxido-Reductive Stress and Protein Aggregation Cardiomyopathy in Mice
  publication-title: Cell
  doi: 10.1016/j.cell.2007.06.044
– volume: 28
  start-page: 889
  year: 2009
  ident: ref_152
  article-title: Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
  publication-title: Embo J.
  doi: 10.1038/emboj.2009.29
– volume: 62
  start-page: 490
  year: 2007
  ident: ref_97
  article-title: Age-Associated Decrease in Proteasome Content and Activities in Human Dermal Fibroblasts: Restoration of Normal Level of Proteasome Subunits Reduces Aging Markers in Fibroblasts From Elderly Persons
  publication-title: J. Gerontol. Ser. A Boil. Sci. Med. Sci.
– volume: 86
  start-page: 129
  year: 2017
  ident: ref_88
  article-title: Ubiquitin Ligases: Structure, Function, and Regulation
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev-biochem-060815-014922
– volume: 130
  start-page: 748
  year: 2009
  ident: ref_110
  article-title: Inverse correlation of protein oxidation and proteasome activity in liver and lung
  publication-title: Mech. Ageing Dev.
  doi: 10.1016/j.mad.2009.09.004
– volume: 9
  start-page: 49
  year: 2004
  ident: ref_122
  article-title: Mild heat stress stimulates 20S proteasome and its 11S activator in human fibroblasts undergoing aging in vitro
  publication-title: Cell Stress Chaperones
  doi: 10.1379/1466-1268(2004)009<0049:MHSSSP>2.0.CO;2
– volume: 31
  start-page: 53
  year: 2019
  ident: ref_80
  article-title: Pros and Cons of Chaperone-Mediated Autophagy in Cancer Biology
  publication-title: Trends Endocrinol. Metab.
  doi: 10.1016/j.tem.2019.09.007
– ident: ref_22
  doi: 10.3390/ijms20225815
– volume: 17
  start-page: 786
  year: 2012
  ident: ref_133
  article-title: p62 at the Interface of Autophagy, Oxidative Stress Signaling, and Cancer
  publication-title: Antioxid. Redox Signal.
  doi: 10.1089/ars.2011.4394
– volume: 37
  start-page: 1223
  year: 2002
  ident: ref_33
  article-title: Mild stress-induced stimulation of heat-shock protein synthesis and improved functional ability of human fibroblasts undergoing aging in vitro
  publication-title: Exp. Gerontol.
  doi: 10.1016/S0531-5565(02)00128-6
– volume: 13
  start-page: 661
  year: 1992
  ident: ref_30
  article-title: Hsp70 mRNA induction is reduced in neurons of aged rat hippocampus after thermal stress
  publication-title: Neurobiol. Aging
  doi: 10.1016/0197-4580(92)90088-F
– volume: 462
  start-page: 245
  year: 2007
  ident: ref_134
  article-title: Selective degradation of mitochondria by mitophagy
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2007.03.034
– volume: 38
  start-page: 6825
  year: 2018
  ident: ref_148
  article-title: Neuronal Preconditioning Requires the Mitophagic Activity of C-terminus of HSC70-Interacting Protein
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.0699-18.2018
– volume: 3
  start-page: 93
  year: 2000
  ident: ref_92
  article-title: The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
  publication-title: Nature
– volume: 23
  start-page: 467
  year: 2018
  ident: ref_49
  article-title: Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development
  publication-title: Cell Stress Chaperones
  doi: 10.1007/s12192-018-0877-2
– ident: ref_27
  doi: 10.1371/journal.pone.0007719
– volume: 19
  start-page: 2039
  year: 2008
  ident: ref_63
  article-title: Organization of the Pre-autophagosomal Structure Responsible for Autophagosome Formation
  publication-title: Mol. Boil. Cell
  doi: 10.1091/mbc.e07-10-1048
– volume: 131
  start-page: 594
  year: 2011
  ident: ref_107
  article-title: Functional Interplay between Mitochondrial and Proteasome Activity in Skin Aging
  publication-title: J. Investig. Dermatol.
  doi: 10.1038/jid.2010.383
– volume: 1762
  start-page: 103
  year: 2006
  ident: ref_36
  article-title: Age-related alterations in expression of apoptosis regulatory proteins and heat shock proteins in rat skeletal muscle
  publication-title: Biochim. Et Biophys. Acta (BBA) Mol. Basis Dis.
  doi: 10.1016/j.bbadis.2005.08.003
– volume: 427
  start-page: 197
  year: 2004
  ident: ref_104
  article-title: Age-dependent protein modifications and declining proteasome activity in the human lens
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2004.05.006
– volume: 89
  start-page: 1325
  year: 2004
  ident: ref_115
  article-title: Focal dysfunction of the proteasome: A pathogenic factor in a mouse model of amyotrophic lateral sclerosis
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.2004.02453.x
– volume: 546
  start-page: 228
  year: 2003
  ident: ref_121
  article-title: Role of the proteasome in protein oxidation and neural viability following low-level oxidative stress
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(03)00582-9
– ident: ref_147
  doi: 10.20944/preprints201807.0137.v1
– volume: 62
  start-page: 481
  year: 2007
  ident: ref_55
  article-title: Age-related increase of insoluble, phosphorylated small heat shock proteins in human skeletal muscle
  publication-title: J. Gerontol. Ser. A Boil. Sci. Med. Sci.
– volume: 1803
  start-page: 641
  year: 2010
  ident: ref_46
  article-title: Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility
  publication-title: Biochim. Et Biophys. Acta (BBA) Bioenerg.
  doi: 10.1016/j.bbamcr.2009.11.012
– volume: 2020
  start-page: 9369524
  year: 2020
  ident: ref_125
  article-title: HSP70 Inhibition Leads to the Activation of Proteasomal System under Mild Hyperthermia Conditions in Young and Senescent Fibroblasts
  publication-title: Oxidative Med. Cell. Longev.
  doi: 10.1155/2020/9369524
SSID ssj0000816105
Score 2.2944124
SecondaryResourceType review_article
Snippet Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially...
SourceID doaj
pubmedcentral
proquest
pubmed
crossref
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Enrichment Source
StartPage 1308
SubjectTerms Age
Aging
Animals
Autophagy
Cell death
Cell growth
Cell survival
Cellular Senescence
Chaperones
Cooperativity
Degeneration
Disease
Endoplasmic reticulum
Fibroblasts
Heat shock proteins
Homeostasis
Humans
Kinases
Life cycles
Models, Biological
molecular chaperones
Molecular Chaperones - metabolism
Nematodes
Oxidative stress
Phagocytosis
Polypeptides
Proteasomes
Protein biosynthesis
Protein synthesis
Protein transport
Proteolysis
Proteostasis
Review
Senescence
Stress response
Ubiquitin
ubiquitin-proteasomal system
SummonAdditionalLinks – databaseName: ProQuest Central
  dbid: BENPR
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Na9wwEB3ShEIvpd91mwYF2lMx8VojyXsqSUgIhQ0hNJBDwejL7UKw0_XmkH_fGdvr7pY2F4OtMR5LI3meJL8H8DGnoIiVIWwS0acoXUiZEiUlOKSmmc-z0EknzM712RV-vVbXw4RbO2yrXI2J3UAdGs9z5AeMPDSyPsmX218pq0bx6uogofEIdmgILijCd45Ozi8ux1kWlpWgDKLf8S4J3x_wfHjLpFSSFSXXvkUdZf-_8sy_t0uufX9On8HTIXEUh31LP4etWL-Ax72U5P1L-D5b6dwK_qUgLpiDX9g6iAtmYmhu7uk-Meu2TjK3cSsuexX62BvMa8GK6Q0li-28FXR6yPJF4phf5BVcnZ58Oz5LB-WE1KMplmkVlEbmEtXRq1i5idaU21QhKqvC1DmJaF0xVdZoHwmmTlVEy_pjwWiXBylfw3ZNfr4FEZRxWFV0sDkGgy4rrPWU9ahJKLzHBD6v6rD0A604q1vclAQvuMbL9RpP4NNofdvTafzH7oibY7RhEuzuQrP4UQ59qgyVihadyZ01iD5ziIHQmESdYRWzkMDuqjHLoWe25Z84SmB_LKY-xY-3dWzuehumtMwmCbzp2370RPJKsdQ6AbMRFRuubpbU858dbzfhGEon8d3Dbr2HJzlj-kylOe7C9nJxFz9Q4rN0e0N0_waliAXY
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Journals: Open Access
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1ba9RAFD6USsEXUeslWssU6pNEZ5MzM9kHkbZYSmFFxIU-CGFu0YUlq5stuP_ec3JZulrf-hJI5oTMNfN9k8n3ARxn1CliZYibRPQp5i6kLImSEh1SY-kzGVrrhMknfTHFyyt1tQOD22hfgc2t1I79pKbL-dvfv9YfaMC_Z8ZJlP0dL3E3rDOV81-_92hOMmziMOmBfvtOLgjZSNXtfP_npq05qZXuvw1v_r1t8sY8dP4QHvQAUpx0Lf4IdmL9GPY6S8n1PnybDH63gn8tiEvW4he2DuIzKzIs5mu6T0zaLZSscdyIL50bfewCZrVg5_QFgcZm1gg6PWEbI3HGBXkC0_OPX88u0t5BIfVoilVaBaWRNUV19CpWbqQ1YZwqRGVVGDuXI1pXjJU12keiq2MV0bIPWTDaZSHPn8JuTfl8DiIo47Cq6GAzDAadLKz1hH7UKBTeYwJvhjosfS8vzi4X85JoBtd4ebPGE3i9if7ZyWr8J-6Um2MTw2LY7YXF8nvZj60yVCpadCZz1iB66RADsbIctcQqypDAwdCY5dDBSmayGtnvJoGjTTKNLX68rePiuothaUs5SuBZ1_abnOT8xTjXOgGz1Su2srqdUs9-tPrdxGcIVuKLuyjbS7if8QqAVGmGB7C7Wl7HVwSTVu6wHQF_AFxKFHc
  priority: 102
  providerName: Scholars Portal
Title Molecular Chaperones and Proteolytic Machineries Regulate Protein Homeostasis in Aging Cells
URI https://www.ncbi.nlm.nih.gov/pubmed/32456366
https://www.proquest.com/docview/2407649618
https://www.proquest.com/docview/2407313201
https://pubmed.ncbi.nlm.nih.gov/PMC7291254
https://doaj.org/article/df5ea4b72ba744c0b44d66634604fe0d
Volume 9
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Na9wwEB1KSqGX0jb9cJMGBdpTMdHaI8l7TEJCKGwIoYEcCkZfpgvBG-LNIf8-M5Z38ZaWXHIx2BpjWRpZ79nyewDfCkqK2BjiJhF9jqULOUui5ESH1FT6QobeOmF2rs-u8Oe1uh5ZffGasCQPnBruIDQqWnSmcNYgeukQA0HuErXEJsrAT1-a80Zkqn8GV4RkpEor3Uvi9Qf8HrxjMaqSnSRHc1Av1f8vfPn3MsnRvHP6Ft4MgFEcpoq-gxexfQ-vkoXkwzb8nq38bQX_ShDvWHtf2DaIC1ZgWNw80Hli1i-ZZE3jTlwm9_mYAuatYKf0BYHEbt4J2j1k2yJxzDfyAa5OT34dn-WDY0Lu0VTLvAlKI2uI6uhVbNxEa8I0TYjKqjB1rkS0rpoqa7SPRE-nKqJl37FgtCtCWX6ErZbq-RlEUMZh09DGFhgMOllZ6wntqEmovMcMfqzasPaDnDi7WtzURCu4xetxi2fwfR19m2Q0_hN3xN2xjmHx6_4ApUQ9pET9VEpksLvqzHoYkV3NzFUj-9tksL8uprHEl7dtXNynGJaylJMMPqW-X9ek5C_EpdYZmI2s2KjqZkk7_9PrdRN_IRiJX57j3nbgdcGMX6q8wF3YWt7dx68Ei5ZuD14enZxfXO71I4G2M6weAXEQD8Q
linkProvider Directory of Open Access Journals
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEB5VqRBcEO8aCl0kekJWHXt2nRwQ6lMpbaKqaqUekMy-DJEqp8SpUP4Uv5EZP0KCgFsvluwdy-Pd2d2Z2d3vA3gXk1H4PKXYxKMNMTEuZEiUkMIh2Y9sHLmKOmE4UoNL_HQlr9bgZ3sWhrdVtmNiNVC7ieUc-Q5HHgqZn-TjzfeQWaN4dbWl0KjN4sTPf1DIVn44PqD23Y7jo8OL_UHYsAqEFtPeLMydVMg4m8pb6XPTVYrm_dx5qaXrG5MgatPrS50q6ymE60uPmrm5XKpM7DgBSkP-OibkKnRgfe9wdHa-yOowjQV5LPUO-yTpRzucfy8ZBCthBsulua-iCPibX_vn9syl-e7oETxsHFWxW1vWY1jzxRO4V1NXzp_C52HLqyv4CIOfMua_0IUTZ4z8MLme03tiWG3VZCzlUpzXrPe-FhgXghnaJ-ScluNS0O0u0yWJff6RZ3B5J3X6HDoF6bkBwsnUYJ7TRcfoUjRRT2tLXpbsup61GMD7tg4z28CYM5vGdUbhDNd4tlzjAWwvpG9q-I5_yO1xcyxkGHS7ejCZfs2aPpy5XHqNJo2NThFtZBAdRX8JqghzH7kANtvGzJqRoMx-220AbxfF1If587rwk9tahiE0o24AL-q2X2iS8Mp0olQA6YpVrKi6WlKMv1U44RQ3kfuKL_-v1hbcH1wMT7PT49HJK3gQcz4hkmGMm9CZTW_9a3K6ZuZNY-kCvtx15_oFnEdCoQ
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEB5VrUBcEO8aCiwSPSErjj27Tg4I9RW1lERRRaUekMy-XCJVTolTofw1fh0zfoQEAbdeLNk7lte7s7szs7PfB_A2JqXweUq-iUcbYmJcyJAoIblDsh_ZOHIVdcJwpI7P8eOFvNiAn-1ZGE6rbOfEaqJ2U8sx8g57HgqZn6STN2kR48PBh-vvITNI8U5rS6dRq8ipX_wg9618f3JIfb0bx4OjzwfHYcMwEFpMe_Mwd1IhY24qb6XPTVcpsgFy56WWrm9MgqhNry91qqwnd64vPWrm6XKpMrHjYChN_1spHx_dhK39o9H4bBnhYUoLsl7qbPsk6UcdjsWXDIiVMJvlyjpY0QX8zcb9M1VzZe0bPID7jdEq9motewgbvngEd2oay8Vj-DJsOXYFH2fwM8b_F7pwYswoENOrBb0nhlXaJuMql-LMXzJtmK8FJoVgtvYpGarlpBR0u8fUSeKAf-QJnN9Kmz6FzYLquQ3CydRgntNFx-hSNFFPa0sWl-y6nrUYwLu2DTPbQJozs8ZVRq4Nt3i22uIB7C6lr2soj3_I7XN3LGUYgLt6MJ1dZs14zlwuvUaTxkaniDYyiI48wQRVhLmPXAA7bWdmzaxQZr91OIA3y2Iaz_x5XfjpTS3DcJpRN4Bndd8va5LwLnWiVADpmlasVXW9pJh8qzDDyYciUxaf_79ar-EuDars08no9AXcizm0EMkwxh3YnM9u_Euyv-bmVaPoAr7e9tj6BXm_Rt8
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Molecular+Chaperones+and+Proteolytic+Machineries+Regulate+Protein+Homeostasis+in+Aging+Cells&rft.jtitle=Cells+%28Basel%2C+Switzerland%29&rft.au=Boris+Margulis&rft.au=Anna+Tsimokha&rft.au=Svetlana+Zubova&rft.au=Irina+Guzhova&rft.date=2020-05-24&rft.pub=MDPI+AG&rft.eissn=2073-4409&rft.volume=9&rft.issue=5&rft.spage=1308&rft_id=info:doi/10.3390%2Fcells9051308&rft.externalDBID=DOA&rft.externalDocID=oai_doaj_org_article_df5ea4b72ba744c0b44d66634604fe0d
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2073-4409&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2073-4409&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2073-4409&client=summon