Proteostasis stress

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Unknown (1049)
Genomics (262)
Proteomics (243)
Transcriptomics (204)
Other (9)
Models (3)
Metabolomics (2)

Organisms

Allexis (190)
Arabidopsis thaliana (190)
Homo sapiens (190)
Mus musculus (82)
Homo sapiens (78)
Caenorhabditis elegans (26)
Saccharomyces cerevisiae (23)
Drosophila melanogaster (12)
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Arabidopsis thaliana (6)
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Saccharomyces cerevisiae SK1 (2)
Bos taurus (2)
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Fusarium oxysporum f. sp. lycopersici 4287 (1)
Saccharomyces cerevisiae W303 (1)
Saccharomyces cerevisiae BY4741 (1)
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Felis catus (1)
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Zymoseptoria tritici (1)
Gallus gallus (1)
Amphioctopus fangsiao (1)
Human parechovirus strain T82-0169 (1)
Microsporum canis (1)
Zea mays (1)
Botryllus schlosseri (1)
Gasterosteus aculeatus (1)
Mycolicibacterium smegmatis (1)

Organisms

Mus musculus (71)
Homo sapiens (61)
Caenorhabditis elegans (23)
Saccharomyces cerevisiae (19)
Drosophila melanogaster (12)
Rattus norvegicus (4)
Danio rerio (3)
Arabidopsis thaliana (3)
Saccharomyces cerevisiae SK1 (2)
Bos taurus (2)
Fusarium oxysporum f. sp. lycopersici 4287 (1)
Saccharomyces cerevisiae W303 (1)
Cricetulus griseus (1)
Zymoseptoria tritici (1)
Saccharomyces cerevisiae S288C (1)
Listeria monocytogenes (1)
Felis catus (1)
Acinetobacter baumannii (1)
Escherichia coli K-12 (1)
Saccharomyces cerevisiae BY4741 (1)
Gallus gallus (1)
Canis lupus familiaris (1)

Repository

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geo (203)
pride (190)
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biostudies-arrayexpress (31)
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Tissue

Cell culture (74)
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Root (2)
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Blood (1)
Blood cell (1)
Blood plasma (1)
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Cell line cell (1)
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T-lymphocyte (1)

Disease

Cardiovascular system disease (4)
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Disease free (4)
Multiple myeloma (3)
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Huntington Disease (2)
Not Available (1)
Alpha 1-antitrypsin deficiency (1)
Alzheimer's disease (1)
Autism spectrum disorder (1)
Brain cancer (1)
Cardiomyopathy (1)
Heart failure (1)
Hepatocellular carcinoma (1)
Krabbe disease (1)
Liver cancer (1)
Lung cancer (1)
Malignant neoplasm of ovary (1)
Melanoma (1)
Mixed disorder as reaction to stress (1)
Myopathy (1)
Osteosarcoma (1)
Parkinson's disease (1)
Plasmodium falciparum malaria (1)
Polycystic liver disease (1)
Urinary bladder cancer (1)

Technology Type

Mass Spectrometry (190)
Shotgun proteomics (95)
Bottom-up proteomics (54)
Data-dependent acquisition (33)
Gel-based experiment (22)
Data-independent acquisition (19)
Affinity purification coupled with mass spectrometry proteomics (17)
SWATH MS (3)
Top-down proteomics (2)
Mass spectrometry (1)
Affinity proteomics (1)
Chemical cross-linking coupled with mass spectrometry proteomics (1)
DiaPASEF (1)
HDMSE (1)
MSE (1)
Proteogenomics (1)
SRM/MRM (1)

Instrument Platform

Orbitrap Exploris 480 (12)
Q Exactive (6)
Illumina NovaSeq 6000 (4)
Orbitrap Fusion (4)
TripleTOF 5600 (3)
Orbitrap Fusion Lumos (3)
Illumina Genome Analyzer IIx (1)
Illumina HiSeq 2000 (1)
Illumina HiSeq 4000 (1)
Instrument (1)
LTQ Orbitrap (1)
LTQ Orbitrap Elite (1)
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LTQ XL (1)
Orbitrap Astral (1)
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TimsTOF HT (1)
Liquid Chromatography MS - positive - reverse phase (1)
Liquid Chromatography MS - negative - reverse phase (1)

Publication Date

2026 (89)
2025 (80)
2024 (57)
2021 (39)
2022 (38)
2023 (35)
2020 (35)
2018 (21)
2019 (18)
2016 (17)
2017 (10)
2013 (9)
2015 (7)
2012 (6)
2014 (3)
2010 (1)

CHEBI ID

CHEBI:24933 (1)
CHEBI:14484 (1)
CHEBI:6074 (1)
CHEBI:24932 (1)
CHEBI:1687 (1)
CHEBI:42317 (1)
CHEBI:1567 (1)
CHEBI:23616 (1)
CHEBI:20097 (1)
CHEBI:13960 (1)
CHEBI:23093 (1)
CHEBI:3593 (1)
CHEBI:57884 (1)
CHEBI:23094 (1)
CHEBI:3588 (1)
CHEBI:1566 (1)
CHEBI:20095 (1)
CHEBI:14734 (1)
CHEBI:25843 (1)
CHEBI:3590 (1)
CHEBI:57802 (1)
CHEBI:13961 (1)
CHEBI:46136 (1)
CHEBI:23096 (1)
CHEBI:872 (1)
CHEBI:28907 (1)
CHEBI:11417 (1)
CHEBI:19325 (1)
CHEBI:19306 (1)
CHEBI:41885 (1)

Metabolite Name

Cerium(3+) trihydride (1)
3-(4-hydroxyphenyl)-1-[2,4,6-trihydroxy-3,5-bis(3-methylbut-2-en-1-yl)phenyl]propan-1-one (1)
N-Acetyl-L-valyl-L-valyl-L-valyl-L-valyl-L-valyl-N-methyl-L-valinamide (1)
N-[(3,5-ditert-butyl-4-hydroxyphenyl)methyl]-2-dimethoxyphosphorylacetamide (1)
?D-?Xylonic acid (1)
3,4,5-trihydroxy-6-({5-hydroxy-11-methoxy-16,18-dioxo-6,8,19-trioxapentacyclo[10.7.0.0?,?.0?,?.0??,??]nonadeca-1(12),2(9),10,13(17)-tetraen-4-yl}oxy)oxane-2-carboxylic acid (1)
PG(20:0/22:4(7Z,10Z,13Z,16Z)) (1)
Benzene, 1,1',1'',1''',1'''',1'''''-(bi-2-cyclopropen-1-yl)-1,1',2,2',3,3'-hexaylhexakis- (1)
PtdIns-(3,4,5)-P3 (1,2-dioctanoyl) (1)
PI(13:0/18:3(6Z,9Z,12Z)) (1)
FD&C Green No. 1 (1)
(2E)-3-phenyl-1-[2,4,6-trihydroxy-3-(4-hydroxy-3-methylbut-2-en-1-yl)-5-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one (1)
1,2,3-Tris(decyloxy)-5-isocyanatobenzene (1)
Lauryl hydroxysultaine (1)
L-Tyrosyl-L-seryl-L-threonyl-L-isoleucyl-L-histidyl-L-prolyl-L-alanyl-L-serine (1)
N-[6-[bis-(4-methylphenyl)sulfonylamino]hexyl]-4-methyl-N-(4-methylphenyl)sulfonylbenzenesulfonamide (1)
Decanoic acid, monoamide with N-(2-aminoethyl)-1,2-ethanediamine (1)
2,5-Bis(8-butoxy-2,6-dimethyloctan-2-yl)benzene-1,4-diol (1)
Germane, acetoxytrimethyl- (1)
L-Prolyl-L-prolyl-L-alanyl-L-alanyl-L-alanylglycylglycyl-L-methionine (1)
AC1NQZVR (1)
Peptide 7194 (1)
L-Lysyl-N~5~-(diaminomethylidene)-L-ornithyl-L-glutaminyl-L-lysyl-L-threonine (1)
4-(3,7-dimethylocta-2,6-dien-1-yl)-5-(6-hydroxy-1-benzofuran-2-yl)benzene-1,3-diol (1)
PG(P-16:0/12:0) (1)
2,6-Dicyclohexyl-1,4-diethyl-1,4-dihydropyridine-3,5-dicarboxylate (1)
L-Serine, L-arginyl-L-leucyl-L-valyl-L-leucylglycyl- (1)
(2S,2'S)-2,2'-[Propane-1,3-diylbis(dodecanoylazanediyl)]dipropanoic acid (non-preferred name) (1)
Beta-Alanine, N-(7-oxo-1,3,5-cycloheptatrien-1-yl)-, 2-(diethylamino)ethyl ester, citrate (1:1) (1)
Piperidine, 1-((4-methyl-1-piperazinyl)acetyl)-2,2,6,6-tetramethyl- (1)

IsPrivate

False (3)

Submitter Keywords

Not Peer Reviewed (1)

First Public Date

2026 (63)
2025 (36)
2024 (28)
2021 (26)
2023 (17)
2022 (16)
2020 (15)
2018 (10)
2019 (8)
2017 (6)
2014 (6)
2016 (4)
2015 (3)
2013 (2)

Classification

bacteria (3)
fungi (1)

Modelling Approach

Differential equation model (1)
Constraint-based model (1)
Ordinary differential equation model (1)

Modification

2x(15)N labeled L-lysine (2)
4 (1)
4x(15)N labeled L-arginine (1)

Study type

Transcription profiling by array (15)
RNA-seq of coding RNA (11)
ChIP-seq (3)
Other (1)
RNA-seq of coding RNA from single cells (1)

Release Date

2025 (144)
2023 (134)
2022 (111)
2021 (108)
2020 (101)
2024 (94)
2019 (76)
2017 (61)
2016 (58)
2018 (56)
2015 (50)
2026 (26)
2014 (22)
2013 (21)
2012 (11)
2010 (3)
2011 (1)
2009 (1)

Lab affiliation

Molecular Genetics, RPTU Kaiserslautern, Germany (8)
ARC Centre of Excellence in Plant Energy Biology, M316, 35 Stirling Hwy, 6009, WA, Australia Faculty of Science, The University of Western Australia (6)
David H. Koch Institute for Integrative Cancer Research Howard Hughes Medical Institute Massachusetts Institute of Technology Cambridge, MA 02139, USA (6)
Max-Planck-Institute for Biology of Ageing Department of Mitochondrial Proteostasis Joseph-Stelzmann-Str. 9b 50931 Cologne (5)
Max-Planck-Institute for Biology of Ageing Department of Mitochondrial Proteostasis Joseph-Stelzmann-Str. 9b 50931 Cologne Germany (4)
Molecular Genetics, RPTU Kaiserslautern (4)
CEA-Marcoule, ProGenoMIX platform, DRF-Li2D, 30207 Bagnols-sur-Ceze, France (3)
Signalling ISP, Babraham Institute, Cambridge, UK (3)
Applied Microbiology, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44780 Bochum, Germany (2)
CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad - 500007, India (2)
Department of Biochemistry and Molecular Biology; and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, VIC 3010. Australia (2)
Department of Laboratory Medicine, Wiita Lab, University of California, San Francisco, USA (2)
Institute of Biochemistry II, Goethe University, Medical School, Frankfurt, Germany (2)
Institute of Modern Biology, Nanjing University, Nanjing 210008, Jiangsu, China (2)
Max Perutz Labs, Vienna, Austria (2)
Max-Planck-Institute for Biology of Ageing Department of Mitochondrial Proteostasis Joseph-Stelzmann-Str. 9b 50931 Cologne, Germany (2)
ReMedy International Research Agenda Unit, IMol Polish Academy of Sciences, Warsaw, Poland (2)
Assistant Professor Department of Biochemistry Montreal, Quebec H3G 1Y6 (1)
Associate Professor, Institute of Advanced Study in Science and Technology (IASST), Guwahati-110035, Assam, India (1)
Associate Professor, Mayor Lab, Department of Biochemistry and Molecular Biology, Michael Smith Laboratories, University of British Columbia, 2125 East Mall, Vancouver, BC V6T1Z4, Canada (1)
Associate Professor, New York University - Department of Biology, Center for Genomics & Systems Biology (1)
Ben-Gurion University (1)
Bernstein Professor Emeritus in Adult Psychiatry Department of Psychiatry and Behavioral Sciences University of Minnesota Medical School Minneapolis, Minnesota, USA (1)
Biochemistry II, Theodor Boveri-Institute, Biocenter, University of Würzburg, 97074 Würzburg, Germany (1)
Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada (IMRIC). School of Medicine. The Hebrew University of Jerusalem, Israel. (1)
Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany (1)
Boston College, Chemistry (1)
Brain and Mind Research Institute Weill Cornell Medicine 407 E 61st St, New York, NY, 10065 United States (1)
Buchmann Institute of Molecular Life Sciences and Institute of Biophysical Chemistry, Goethe University, Frankfurt am Main, Germany (1)
CECAD Research Center/ Institute for Genetics University of Cologne Joseph-Stelzmann-Str. 26 50931 Cologne (1)

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Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Distinct ER Proteostasis Environments [HEK293DYG]

The unfolded protein response (UPR) maintains endoplasmic reticulum (ER) proteostasis through the activation of transcription factors such as XBP1s and ATF6. The functional consequences of these transcription factors for ER proteostasis remain poorly defined. Here, we describe methodology that enabl...

ORGANISM(S): Homo sapiens

2013-04-23 | E-GEOD-44950 | biostudies-arrayexpress

Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Distinct ER Proteostasis Environments [HEK293DAX]

ORGANISM(S): Homo sapiens

2013-04-23 | E-GEOD-44949 | biostudies-arrayexpress

QUATERNARY AND QUINARY ORGANIZATION OF RESPIRATORY COMPLEX SUBUNITS TO ADAPT PROTEOSTASIS-STRESS

Phase separation and reversible aggregation of proteins is a well-recognized adaptive strategy to survive stress. Here, we show that RCC subunits are engaged into improved super-quaternary organizations inside mitochondria during proteostasis stress. Assembly and oligomeric organizations of Complex ...

ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse)

2024-04-04 | PXD014361 | Pride