Research graph
References from Proteostasis and ageing dissidence. Local targets link to admitted publications; unresolved targets remain external evidence.
Interplay of proteostasis capacity and protein aggregation: implications for cellular function and disease
10.1016/j.jmb.2024.168615 · 2024 · External reference
Adapting proteostasis for disease intervention
10.1126/science.1141448 · 2008 · External reference
The struggle by Caenorhabditis elegans to maintain proteostasis during ageing and disease
10.1186/s13062-016-0161-2 · 2016 · External reference
Proteostasis is differentially modulated by inhibition of translation initiation or elongation
10.7554/elife.76465 · 2023 · External reference
The ubiquitin system, autophagy, and regulated protein degradation
10.1146/annurev-biochem-061516-044859 · 2017 · External reference
Cellular quality control by the ubiquitin-proteasome system and autophagy
10.1126/science.aax3769 · 2019 · External reference
Autophagy in major human diseases
10.15252/embj.2021108863 · 2021 · External reference
Quality control of protein complex assembly by the ubiquitin–proteasome system
10.1016/j.tcb.2022.02.005 · 2022 · External reference
Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly
10.1126/science.2188360 · 1990 · External reference
The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
10.1128/mcb.23.9.3141-3151.2003 · 2003 · External reference
Hsp70 and Hsp90 of E. coli directly interact for collaboration in protein remodeling
10.1016/j.jmb.2015.10.010 · 2015 · External reference
Protein disaggregation mediated by heat-shock protein Hsp104
10.1038/372475a0 · 1994 · External reference
Mechanisms of small heat shock proteins
10.1101/cshperspect.a034025 · 2019 · External reference
Proteasomal and autophagic degradation systems
10.1146/annurev-biochem-061516-044908 · 2017 · External reference
Non-proteolytic ubiquitylation in cellular signaling and human disease
10.1038/s42003-022-03060-1 · 2022 · External reference
Uber eigenartige erkrankung der hirnrinde [On an unusual illness of the cerebral cortex]
1907 · External reference
Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
10.1016/0006-291x(84)91209-9 · 1984 · External reference
A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas
10.1016/0006-291x(86)90708-4 · 1986 · External reference
Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
1987 · External reference
α-Synuclein in Lewy bodies
10.1038/42166 · 1997 · External reference
Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice
10.1038/35022595 · 2000 · External reference
Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)
10.1038/35022604 · 2000 · External reference
Desmin-related cardiomyopathy in transgenic mice: a cardiac amyloidosis
2004 · External reference
Autophagy is an adaptive response in desmin-related cardiomyopathy
2008 · External reference
A hierarchy of ATP-consuming processes in mammalian cells
10.1042/bj3120163 · 1995 · External reference
Conservation of ribosomal fidelity during ageing
10.1016/0047-6374(79)90020-4 · 1979 · External reference
Functional deterioration of mouse liver ribosomes during ageing: translational activity and activity for formation of the 47 S initiation complex
10.1016/0047-6374(84)90097-6 · 1984 · External reference
Inhibition of mRNA translation extends lifespan in Caenorhabditis elegans
10.1111/j.1474-9726.2006.00266.x · 2007 · External reference
Protein translation, 2007
10.1111/j.1474-9726.2007.00341.x · 2007 · External reference
Lifespan extension by conditions that inhibit translation in Caenorhabditis elegans
10.1111/j.1474-9726.2006.00267.x · 2007 · External reference
Increase in the ratio of 18S RNA to 28S RNA in the cytoplasm of mouse tissues during ageing
10.1016/0047-6374(78)90029-5 · 1978 · External reference
Age-dependent decrease in the amount of eukaryotic initiation factor 2 in various rat tissues
10.1042/bj2860263 · 1992 · External reference
Regulation of yeast replicative life span by TOR and Sch9 in response to nutrients
10.1126/science.1115535 · 2005 · External reference
Ribosomal proteins Rpl10 and Rps6 are potent regulators of yeast replicative life span
10.1016/j.exger.2006.11.002 · 2007 · External reference
Yeast life span extension by depletion of 60S ribosomal subunits is mediated by Gcn4
10.1016/j.cell.2008.02.037 · 2008 · External reference
Longevity determined by developmental arrest genes in Caenorhabditis elegans
10.1111/j.1474-9726.2007.00305.x · 2007 · External reference
Lifespan regulation by evolutionarily conserved genes essential for viability
10.1371/journal.pgen.0030056 · 2007 · External reference
eIF4E function in somatic cells modulates ageing in Caenorhabditis elegans
10.1038/nature05603 · 2007 · External reference
Age changes in amino acid incorporation by rat liver microsomes
1969 · External reference
The effect of age on the initiation of protein synthesis in Drosophila melanogaster
10.1016/0047-6374(81)90034-8 · 1981 · External reference
Decreased accuracy of protein synthesis in extracts from ageing human diploid fibroblasts
10.1016/0531-5565(89)90022-3 · 1989 · External reference
Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans ageing
2009 · External reference
Multifaceted deregulation of gene expression and protein synthesis with age
2020 · External reference
Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis
10.1038/s41586-021-04295-4 · 2022 · External reference
Altered translation elongation contributes to key hallmarks of ageing in the killifish brain
10.1126/science.adk3079 · 2025 · External reference
Frameshift mutants of β amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
10.1126/science.279.5348.242 · 1998 · External reference
Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
10.1038/nature05096 · 2006 · External reference
Transcription errors induce proteotoxic stress and shorten cellular lifespan
10.1038/ncomms9065 · 2015 · External reference
Translational fidelity and longevity are genetically linked
10.1038/s41467-025-62944-y · 2025 · External reference
Error-prone protein synthesis recapitulates early symptoms of Alzheimer disease in ageing mice
10.1016/j.celrep.2022.111433 · 2022 · External reference
Premature ageing in mice with error-prone protein synthesis
10.1126/sciadv.abl9051 · 2022 · External reference
Translational error in mice increases with ageing in an organ-dependent manner
10.1038/s41467-025-57203-z · 2025 · External reference
Increased fidelity of protein synthesis extends lifespan
10.1016/j.cmet.2021.08.017 · 2021 · External reference
The nascent polypeptide-associated complex is a key regulator of proteostasis
10.1038/emboj.2013.87 · 2013 · External reference
Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
10.1016/j.tibs.2023.10.003 · 2024 · External reference
Dual role of ribosome-binding domain of NAC as a potent suppressor of protein aggregation and ageing-related proteinopathies
10.1016/j.molcel.2019.03.012 · 2019 · External reference
Nascent-polypeptide-associated complex
10.1007/pl00012490 · 2002 · External reference
Chain dynamics of nascent polypeptides emerging from the ribosome
10.1021/cb800059u · 2008 · External reference
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
10.1038/23301 · 1999 · External reference
Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane
10.1016/j.bbamcr.2013.11.007 · 2014 · External reference
Dynamical structures of Hsp70 and Hsp70-Hsp40 complexes
10.1016/j.str.2016.05.011 · 2016 · External reference
Hsp70 chaperones: cellular functions and molecular mechanism
10.1007/s00018-004-4464-6 · 2005 · External reference
Expression of heat shock protein 70 is altered by age and diet at the level of transcription
1993 · External reference
Circulating heat shock protein 70 in health, ageing and disease
10.1186/1471-2172-12-24 · 2011 · External reference
Heat shock proteins and cancer: intracellular chaperones or extracellular signalling ligands?
10.1098/rstb.2016.0524 · 2018 · External reference
The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases
10.1038/sj.emboj.7601930 · 2008 · External reference
Modulating expression of brain heat shock proteins by estrogen in ovariectomized mice model of ageing
10.1016/j.exger.2009.10.006 · 2010 · External reference
Hsp70 basal levels, a tissue marker of the rate of ageing and longevity in mice
10.1016/j.exger.2016.08.013 · 2016 · External reference
Therapeutic effect of exogenous Hsp70 in mouse models of Alzheimer's disease
10.3233/jad-130779 · 2014 · External reference
Serum and lymphocyte levels of heat shock protein 70 in ageing: a study in the normal Chinese population
10.1379/1466-1268(2004)009<0069:salloh>2.0.co;2 · 2004 · External reference
Lysine deacetylases regulate the heat shock response including the age-associated impairment of HSF1
10.1016/j.jmb.2015.02.010 · 2015 · External reference
Age-dependent heat shock hormesis to HSF-1 deficiency suggests a compensatory mechanism mediated by the unfolded protein response and innate immunity in young Caenorhabditis elegans
10.1111/acel.14246 · 2024 · External reference
Age-dependent expression profiles of two adaptogenic systems and thermotolerance in Drosophila melanogaster
10.1007/s12192-020-01074-4 · 2020 · External reference
The heat shock transcription factor Hsf1 is downregulated in DNA damage-associated senescence, contributing to the maintenance of senescence phenotype
10.1111/j.1474-9726.2012.00827.x · 2012 · External reference
Defining the essential function of yeast Hsf1 reveals a compact transcriptional program for maintaining eukaryotic proteostasis
10.1016/j.molcel.2016.05.014 · 2016 · External reference
Multiple functions of Drosophila heat shock transcription factor in vivo
10.1093/emboj/16.9.2452 · 1997 · External reference
HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers
10.1016/j.cell.2012.06.031 · 2012 · External reference
Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis
10.1016/j.cell.2007.07.020 · 2007 · External reference
Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
10.1091/mbc.e03-07-0532 · 2004 · External reference
HSB-1 inhibition and HSF-1 overexpression trigger overlapping transcriptional changes to promote longevity in Caenorhabditis elegans
10.1534/g3.119.400044 · 2019 · External reference
Regulation of aging and age-related disease by DAF-16 and heat-shock factor
10.1126/science.1083701 · 2003 · External reference
Opposing activities protect against age-onset proteotoxicity
10.1126/science.1124646 · 2006 · External reference
Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor
10.1016/s0021-9258(18)48191-4 · 1987 · External reference
The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
10.1016/s0021-9258(19)50533-6 · 1992 · External reference
Heat-shock protein hsp90 governs the activity of pp60v-src kinase
1993 · External reference
Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles
10.1016/j.cell.2014.04.038 · 2014 · External reference
Hop modulates Hsp70/Hsp90 interactions in protein folding
10.1074/jbc.273.6.3679 · 1998 · External reference
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
10.1016/s0960-9822(01)00487-0 · 2001 · External reference
Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery
10.1074/jbc.273.52.35194 · 1998 · External reference
The Hsp70–Hsp90 chaperone cascade in protein folding
10.1016/j.tcb.2018.10.004 · 2019 · External reference
The middle domain of Hsp90 acts as a discriminator between different types of client proteins
10.1128/mcb.02188-05 · 2006 · External reference
Establishing order through disorder by the Hsp90 molecular chaperone
10.1016/j.jmb.2024.168460 · 2024 · External reference
The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions
10.1016/j.molcel.2023.05.021 · 2023 · External reference
Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
10.1074/jbc.270.13.7288 · 1995 · External reference
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
10.1002/j.1460-2075.1996.tb00660.x · 1996 · External reference
Reduced levels of hsp90 compromise steroid receptor action in vivo
10.1038/348166a0 · 1990 · External reference
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
10.1016/s0092-8674(02)01250-3 · 2003 · External reference
The Hsp90 molecular chaperone regulates the transcription factor network controlling chromatin accessibility
10.1016/j.jmb.2019.09.007 · 2019 · External reference
Heat-shock protein 90, a chaperone for folding and regulation
10.1007/pl00012491 · 2002 · External reference
The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
10.1172/jci29715 · 2007 · External reference
The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein α-synuclein
10.1074/jbc.m109.057240 · 2009 · External reference
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
10.1016/j.cell.2014.01.037 · 2014 · External reference
Hsp90 inhibits α-synuclein aggregation by interacting with soluble oligomers
10.1016/j.jmb.2013.08.006 · 2013 · External reference
Imbalances in the Hsp90 chaperone machinery: implications for tauopathies
10.3389/fnins.2017.00724 · 2017 · External reference
Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease
10.1517/14728222.2014.943185 · 2014 · External reference
Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone
10.1016/j.molcel.2011.01.029 · 2011 · External reference
Downregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegans
10.1371/journal.pone.0025485 · 2011 · External reference
Different dietary restriction regimens extend lifespan by both independent and overlapping genetic pathways in C. elegans
10.1111/j.1474-9726.2009.00459.x · 2009 · External reference
Chaperone rings in protein folding and degradation
1999 · External reference
Novel cryo-EM structure of an ADP-bound GroEL–GroES complex
10.1038/s41598-021-97657-x · 2021 · External reference
GroEL-GroES-mediated protein folding requires an intact central cavity
1998 · External reference
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
10.1016/j.cell.2014.10.042 · 2014 · External reference
Pathway of actin folding directed by the eukaryotic chaperonin TRiC
10.1016/j.cell.2018.07.006 · 2018 · External reference
Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT
10.1016/j.cell.2022.11.014 · 2022 · External reference
Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
10.1016/s0092-8674(00)81446-4 · 1998 · External reference
Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
10.1038/nsmb.1515 · 2008 · External reference
The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
10.1038/nsmb.1700 · 2009 · External reference
The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction
10.1038/srep40859 · 2017 · External reference
A chaperome subnetwork safeguards proteostasis in ageing and neurodegenerative disease
10.1016/j.celrep.2014.09.042 · 2014 · External reference
Role of the chaperonin TCP-1 ring complex in protein aggregation and neurodegeneration
10.3389/fnmol.2025.1617771 · 2025 · External reference
Protein disaggregation machineries in the human cytosol
10.1016/j.sbi.2023.102735 · 2023 · External reference
Spiraling in control: structures and mechanisms of the Hsp104 disaggregase
10.1101/cshperspect.a034033 · 2019 · External reference
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
10.1016/s0092-8674(00)81223-4 · 1998 · External reference
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation
10.1038/nsmb.3277 · 2016 · External reference
Nuclear Hsp104 safeguards the dormant translation machinery during quiescence
10.1038/s41467-023-44538-8 · 2024 · External reference
Hsp110 is a nucleotide-activated exchange factor for Hsp70
10.1074/jbc.m710063200 · 2008 · External reference
Coordinated Hsp110 and Hsp104 activities power protein disaggregation in Saccharomyces cerevisiae
10.1128/mcb.00027-17 · 2017 · External reference
Cellular handling of protein aggregates by disaggregation machines
10.1016/j.molcel.2018.01.004 · 2018 · External reference
The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70
10.1038/s41598-021-96518-x · 2021 · External reference
Small heat shock proteins are molecular chaperones
10.1016/s0021-9258(18)53882-5 · 1993 · External reference
HSF1 physically neutralizes amyloid oligomers to empower overgrowth and bestow neuroprotection
10.1126/sciadv.abc6871 · 2020 · External reference
Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation
2010 · External reference
Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
10.1038/ncb2838 · 2013 · External reference
Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation
10.1371/journal.pgen.1011194 · 2024 · External reference
Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
10.1146/annurev.neuro.26.010302.081142 · 2003 · External reference
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
10.1038/nm1782 · 2008 · External reference
The most infectious prion protein particles
10.1038/nature03989 · 2005 · External reference
The inhibition of IGF-1 signaling promotes proteostasis by enhancing protein aggregation and deposition
10.1096/fj.15-281675 · 2016 · External reference
Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin
2014 · External reference
Restricted access: spatial sequestration of damaged proteins during stress and aging
10.15252/embr.201643458 · 2017 · External reference
Decline in protease activities with age in the nematode Caenorhabditis elegans
10.1016/0047-6374(88)90001-2 · 1988 · External reference
Altered proteasome structure, function, and oxidation in aged muscle
10.1096/fj.04-2578fje · 2005 · External reference
Mechanisms and regulation of substrate degradation by the 26S proteasome
10.1038/s41580-024-00778-0 · 2025 · External reference
Repair or destruction—an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis
10.1002/1873-3468.12750 · 2017 · External reference
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
10.1126/science.2538923 · 1989 · External reference
STING signalling is terminated through ESCRT-dependent microautophagy of vesicles originating from recycling endosomes
10.1038/s41556-023-01098-9 · 2023 · External reference
Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
10.1074/jbc.271.18.10946 · 1996 · External reference
Degradation-mediated protein quality control in the nucleus
10.1016/j.cell.2005.01.016 · 2005 · External reference
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
10.1038/35050618 · 2001 · External reference
The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism
10.1038/s41598-019-41060-0 · 2019 · External reference
Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
10.1128/mcb.19.6.4535 · 1999 · External reference
10.1093/embo-reports/kve246 · 2001 · Admitted local publication
Defective ribosomal products challenge nuclear function by impairing nuclear condensate dynamics and immobilizing ubiquitin
10.15252/embj.2018101341 · 2019 · External reference
Age-associated decrease in proteasome content and activities in human dermal fibroblasts: restoration of normal level of proteasome subunits reduces ageing markers in fibroblasts from elderly persons
10.1093/gerona/62.5.490 · 2007 · External reference
Proteasome augmentation mitigates age-related cognitive decline in mice
10.1111/acel.14492 · 2025 · External reference
Inhibition of the ubiquitin-proteasome system in Alzheimer's disease
2000 · External reference
Proteasomal function is impaired in substantia nigra in Parkinson's disease
10.1016/s0304-3940(00)01701-8 · 2001 · External reference
Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation
10.1074/jbc.m301048200 · 2003 · External reference
Protein oxidation and degradation during postmitotic senescence
10.1016/j.freeradbiomed.2005.06.009 · 2005 · External reference
Inverse correlation of protein oxidation and proteasome activity in liver and lung
10.1016/j.mad.2009.09.004 · 2009 · External reference
Differential regulation of proteasome functionality in reproductive vs. somatic tissues of Drosophila during ageing or oxidative stress
10.1096/fj.12-221408 · 2013 · External reference
Genetic and pharmacologic proteasome augmentation ameliorates Alzheimer's-like pathology in mouse and fly APP overexpression models
10.1126/sciadv.abk2252 · 2022 · External reference
Reduced proteasome activity in the ageing brain results in ribosome stoichiometry loss and aggregation
2020 · External reference
Ageing perturbs 26S proteasome assembly in Drosophila melanogaster
10.1096/fj.06-6751com · 2007 · External reference
Hyperactivation of the proteasome in Caenorhabditis elegans protects against proteotoxic stress and extends lifespan
10.1016/j.jbc.2022.102415 · 2022 · External reference
Identification and functional clustering of global gene expression differences between human age-related cataract and clear lenses and aged human lenses
2003 · External reference
Gene expression profiling in human age-related nuclear cataract
2003 · External reference
Ageing and cellular maturation cause changes in ubiquitin-eye lens protein conjugates
10.1016/0003-9861(90)90006-k · 1990 · External reference
EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan
10.1038/emboj.2011.195 · 2011 · External reference
Mutation in E1, the ubiquitin activating enzyme, reduces Drosophila lifespan and results in motor impairment
10.1371/journal.pone.0032835 · 2013 · External reference
Parkin overexpression during ageing reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespan
2013 · External reference
Synaptic proteasome is inhibited in Alzheimer's disease models and associates with memory impairment in mice
10.1038/s42003-023-05511-9 · 2023 · External reference
Cytoplasmic TDP-43 impairs the activity of the ubiquitin-proteasome system
10.1016/j.expneurol.2021.113833 · 2021 · External reference
The ubiquitin-conjugating enzyme UBE2D maintains a youthful proteome and ensures protein quality control during ageing by sustaining proteasome activity
10.1371/journal.pbio.3002998 · 2025 · External reference
SUMO modification of Huntingtin and Huntington's disease pathology
10.1126/science.1092194 · 2004 · External reference
IKK phosphorylates huntingtin and targets it for degradation by the proteasome and lysosome
10.1083/jcb.200909067 · 2009 · External reference
The age-related accumulation of protein carbonyl in rat liver correlates with the age-related decline in liver proteolytic activities
10.1093/gerona/54.8.b318 · 1999 · External reference
Age-related decline in chaperone-mediated autophagy
10.1074/jbc.m002102200 · 2000 · External reference
Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study
10.1093/jnen/64.2.113 · 2005 · External reference
Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase
10.1038/ng1884 · 2006 · External reference
Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease
10.1523/jneurosci.0800-08.2008 · 2008 · External reference
Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice
10.1371/journal.pgen.1000838 · 2010 · External reference
The role of autophagy during the early neonatal starvation period
10.1038/nature03029 · 2004 · External reference
Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice
10.1083/jcb.200412022 · 2005 · External reference
Loss of autophagy in the central nervous system causes neurodegeneration in mice
10.1038/nature04723 · 2006 · External reference
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
10.1038/nature04724 · 2006 · External reference
Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
10.4161/auto.5269 · 2008 · External reference
Macroautophagy deficiency mediates age-dependent neurodegeneration through a phospho-tau pathway
10.1186/1750-1326-7-48 · 2012 · External reference
Overexpression of Atg5 in mice activates autophagy and extends lifespan
10.1038/ncomms3300 · 2013 · External reference
Distinct roles for motor neuron autophagy early and late in the SOD1G93A mouse model of ALS
2017 · External reference
Lysosome biology in autophagy
10.1038/s41421-020-0141-7 · 2020 · External reference
Activation of autophagy depends on Atg1/Ulk1-mediated phosphorylation and inhibition of the Hsp90 chaperone machinery
10.1016/j.celrep.2023.112807 · 2023 · External reference
The coming of age of chaperone-mediated autophagy
10.1038/s41580-018-0001-6 · 2018 · External reference
The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
10.1128/mcb.02070-07 · 2008 · External reference
Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome
10.1016/j.cell.2021.03.048 · 2021 · External reference
Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy
10.1126/science.1101738 · 2004 · External reference
Dopamine-modified α-synuclein blocks chaperone-mediated autophagy
2008 · External reference
