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Genomics
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Andropogon gerardi
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Chromatiales bacterium OalgGamma1
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Clavibacter nebraskensis NCPPB 2581
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(13)
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Illumina NovaSeq 6000
(2)
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2025
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Transcription profiling by array
(5)
ChIP-seq
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(16)
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Lab affiliation
The Sir Peter MacCallum Department of Oncology, The University of Melbourne, Victoria, Australia
(2)
1Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany 2Division of Cell Biology, Biomedical Center, Faculty of Medicine, University of Munich, Großhaderner Str. 9, 82152 Martinsried, Germany
(1)
Australian Regenerative Medicine Institute, Monash University, Wellington Road, Clayton, VIC 3800, Australia
(1)
CRG/UPF Proteomics Unit, Center for Genomics Regulation, Universitat Pompeu Fabra, 08003 Barcelona, Spain.
(1)
Cedars-Sinai Medical Center
(1)
Institute for Genetics, CECAD Research Center, University of Cologne
(1)
Institute of Genetics and Molecular Medicine, University of Edinburgh, EH4 2XR Edinburgh, Scotland, United Kingdom
(1)
Laboratory of Protein Metabolism, International Institute of Molecular and Cell Biology in Warsaw, 4 Ks. Trojdena Street, 02-109 Warsaw, Poland
(1)
Lehrstuhl fuer Organische Chemie II Department Chemie TU Muenchen
(1)
Max Planck Institute for Multidisciplinary Sciences, Bioanalytical Mass Spectrometry Group, Am Fassberg 11, 37077 Göttingen, Germany University Medical Center Goettingen, Institute for Clinical Chemistry, Bioanalytics, Robert-Koch-Strasse 40, 37075 Göttingen, Germany
(1)
Munich Cluster for Systems Neurology (SyNergy) Ludwig-Maximilians-University Munich, Germany
(1)
Proteomics Unit. Macromolecular Structures Department. Spanish National Biotechnology Centre.
(1)
Tags
xref:PubMed:29522205
(2)
xref:PubMed:34380014
(1)
xref:PubMed:39844192
(1)
xref:PubMed:41289019
(1)
xref:PubMed:29463595
(1)
xref:PubMed:39977267
(1)
xref:PubMed:39128917
(1)
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Structural Basis for Chaperone-Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP.
Not available
S-EPMC9303552
|
biostudies-literature
Cite
Chaperone-Independent Peripheral Quality Control of CFTR by RFFL E3 Ligase.
Not available
S-EPMC6447300
|
biostudies-literature
Cite
Conserved and Unique Roles of Chaperone-Dependent E3 Ubiquitin Ligase CHIP in Plants.
Not available
S-EPMC8299108
|
biostudies-literature
Cite
The chaperone-assisted E3 ligase C terminus of Hsc70-interacting protein (CHIP) targets PTEN for proteasomal degradation.
Not available
S-EPMC3346122
|
biostudies-literature
Cite
Heat Shock Protein 90 Chaperone Regulates the E3 Ubiquitin-Ligase Hakai Protein Stability.
Not available
S-EPMC7017148
|
biostudies-literature
Cite
Chaperone-mediated autophagy controls the turnover of E3 ubiquitin ligase MARCHF5 and regulates mitochondrial dynamics.
Not available
S-EPMC8526038
|
biostudies-literature
Cite
Chaperone-assisted E3 ligase CHIP: A double agent in cancer.
Not available
S-EPMC9485218
|
biostudies-literature
Cite
Chaperone-assisted E3 ligase-engineered mesenchymal stem cells target hyperglycemia-induced p53 for ubiquitination and proteasomal degradation ameliorates self-renewal.
Not available
S-EPMC12020092
|
biostudies-literature
Cite
A conserved RAD6-MDM2 ubiquitin ligase machinery targets histone chaperone ASF1A in tumorigenesis.
Not available
S-EPMC4745749
|
biostudies-literature
Cite
GRAIL1 Stabilizes Misfolded Mutant p53 through a Ubiquitin Ligase-Independent, Chaperone Regulatory Function.
Not available
S-EPMC11530312
|
biostudies-literature
Cite
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