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Unknown
(64)
Proteomics
(13)
Transcriptomics
(2)
Genomics
(1)
Organisms
Andropogon gerardi
(13)
Bacteria
(13)
Canis lupus familiaris
(13)
Chromatiales bacterium OalgGamma1
(13)
Clavibacter nebraskensis NCPPB 2581
(13)
Cnidaria
(13)
Ensifer adhaerens
(13)
Fasciola
(13)
Human alphaherpesvirus 1 strain 17
(13)
Human alphaherpesvirus 1 strain KOS
(13)
Human betaherpesvirus 5
(13)
Human herpesvirus 2 strain 186
(13)
Mesocricetus auratus
(13)
Miscanthus x giganteus
(13)
Mus musculus
(13)
Panicum virgatum
(13)
Platyhelminthes
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Pseudomonas aeruginosa PA103
(13)
Rattus norvegicus
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Rattus rattus
(13)
Rhodococcus jostii RHA1
(13)
Rhodopseudomonas palustris
(13)
Shigella
(13)
Sorghastrum nutans
(13)
Spirochaeta sp. ELBA
(13)
Streptococcus dysgalactiae subsp. equisimilis SK1249
(13)
Streptococcus pneumoniae
(13)
Streptomyces coelicolor A3(2)
(13)
Mus musculus
(1)
Homo sapiens
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Homo sapiens
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pride
(13)
biostudies-arrayexpress
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geo
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ENA
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Leaf
(3)
Plant cell
(3)
Cell suspension culture
(2)
HeLa cell
(1)
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(1)
Rosette
(1)
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Mass Spectrometry
(13)
Affinity purification coupled with mass spectrometry proteomics
(5)
Bottom-up proteomics
(4)
Data-dependent acquisition
(3)
Chemical cross-linking coupled with mass spectrometry proteomics
(2)
Shotgun proteomics
(2)
Data-independent acquisition
(1)
SWATH MS
(1)
Publication Date
2019
(3)
2026
(3)
2023
(3)
2025
(2)
2005
(1)
2022
(1)
2020
(1)
2018
(1)
First Public Date
2019
(1)
Study type
Transcription profiling by array
(1)
Release Date
2017
(11)
2025
(5)
2023
(5)
2020
(5)
2015
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2019
(4)
2012
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2021
(3)
2014
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2013
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2007
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2005
(1)
2016
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2006
(1)
Lab affiliation
Center for Functional Protein Assemblies (CPA), Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), Ernst-Otto-Fischer-Stra?e 8, 85748 Garching, Germany
(2)
CNB-CSIC dept. Structure of Macromolecules
(1)
Centro Nacional de Biotecnología (CNB-CSIC), Madrid, España.
(1)
Cornell University, Plant Biology section
(1)
Department of Medical Biology, Health Faculty, UiT - The Arctic University of Norway, Norway.
(1)
IGMM, CNRS, Université de Montpellier, Montpellier, France
(1)
Max-Planck Institute of Biochemistry, Department of Cellular Biochemistry
(1)
Max-Planck-Institute for Biology of Ageing Department of Mitochondrial Proteostasis Joseph-Stelzmann-Str. 9b 50931 Cologne
(1)
Max-Planck-Institute for Biology of Ageing Department of Mitochondrial Proteostasis Joseph-Stelzmann-Str. 9b 50931 Cologne Germany
(1)
Plant Biology Section, School of Integrative Plant Science, Cornell University, Ithaca, New York, United States
(1)
School of Integrative Plant Science Plant Biology Section Cornell University
(1)
Thomas Langer Max-Planck-Institute for Biology of Ageing Department of Mitochondrial Proteostasis Joseph-Stelzmann-Str. 9b 50931 Cologne
(1)
Tags
xref:PubMed:31883965
(1)
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Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control.
Not available
S-EPMC5699869
|
biostudies-literature
Cite
Rubisco Activases: AAA+ Chaperones Adapted to Enzyme Repair.
Not available
S-EPMC5385338
|
biostudies-literature
Cite
New insights into structural and functional relationships between LonA proteases and ClpB chaperones.
Not available
S-EPMC6722904
|
biostudies-literature
Cite
Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules.
Not available
S-EPMC9035409
|
biostudies-literature
Cite
AAA+ Machines of Protein Destruction in Mycobacteria.
Not available
S-EPMC5515868
|
biostudies-literature
Cite
Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.
Not available
S-EPMC3413357
|
biostudies-literature
Cite
Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone.
Not available
S-EPMC6917787
|
biostudies-literature
Cite
Dodecamer assembly of a metazoan AAA
+
chaperone couples substrate extraction to refolding.
Not available
S-EPMC10171807
|
biostudies-literature
Cite
Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions.
Not available
S-EPMC3430535
|
biostudies-literature
Cite
Hsp78 (78 kDa Heat Shock Protein), a Representative AAA Family Member Found in the Mitochondrial Matrix of
Saccharomyces cerevisiae
.
Not available
S-EPMC5572323
|
biostudies-literature
Cite
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