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Total Chemical Synthesis of SUMO and SUMO‐Based Probes for Profiling the Activity of SUMO‐Specific Proteases.
- Published in:
- Angewandte Chemie, 2018, v. 130, n. 29, p. 9096, doi. 10.1002/ange.201803483
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- Article
Divergent Molecular and Cellular Responses to Low and High-Dose Ionizing Radiation.
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- Cells (2073-4409), 2022, v. 11, n. 23, p. 3794, doi. 10.3390/cells11233794
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- Article
SENP6 regulates localization and nuclear condensation of DNA damage response proteins by group deSUMOylation.
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- Nature Communications, 2023, v. 41, n. 1, p. 1, doi. 10.1038/s41467-023-41623-w
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- Article
Author Correction: Exploration of nuclear body-enhanced sumoylation reveals that PML represses 2-cell features of embryonic stem cells.
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- 2023
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- Correction Notice
The lncRNA LETS1 promotes TGF-β–induced EMT and cancer cell migration by transcriptionally activating a TβR1-stabilizing mechanism.
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- Science Signaling, 2023, v. 16, n. 790, p. 1, doi. 10.1126/scisignal.adf1947
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- Article
SUMO targets the APC/C to regulate transition from metaphase to anaphase.
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- Nature Communications, 2018, v. 9, n. 1, p. 1, doi. 10.1038/s41467-018-03486-4
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- Article
System-wide identification of wild-type SUMO-2 conjugation sites.
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- Nature Communications, 2015, v. 6, n. 6, p. 7289, doi. 10.1038/ncomms8289
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- Article
Probing ubiquitin and SUMO conjugation and deconjugation.
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- Biochemical Society Transactions, 2018, v. 46, n. 2, p. 423, doi. 10.1042/BST20170086
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- Article
I?Ba is a target for the mitogen-activated 90 kDa ribosomal S6 kinase.
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- EMBO Journal, 1997, v. 16, n. 11, p. 3133, doi. 10.1093/emboj/16.11.3133
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- Article
In‐Plate Chemical Synthesis of Isopeptide‐Linked SUMOylated Peptide Fluorescence Polarization Reagents for High‐Throughput Screening of SENP Preferences.
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- ChemBioChem, 2023, v. 24, n. 2, p. 1, doi. 10.1002/cbic.202200601
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- Article
Total Chemical Synthesis of SUMO and SUMO‐Based Probes for Profiling the Activity of SUMO‐Specific Proteases.
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- Angewandte Chemie International Edition, 2018, v. 57, n. 29, p. 8958, doi. 10.1002/anie.201803483
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- Article
Uncovering global SUMOylation signaling networks in a site-specific manner.
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- Nature Structural & Molecular Biology, 2014, v. 21, n. 10, p. 927, doi. 10.1038/nsmb.2890
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- Article
Splicing factors control triple-negative breast cancer cell mitosis through SUN2 interaction and sororin intron retention.
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- Journal of Experimental & Clinical Cancer Research (17569966), 2021, v. 40, n. 1, p. 1, doi. 10.1186/s13046-021-01863-4
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- Article
A CSB-PAF1C axis restores processive transcription elongation after DNA damage repair.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-21520-w
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- Article
CHD7 and 53BP1 regulate distinct pathways for the re-ligation of DNA double-strand breaks.
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- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-19502-5
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- Article
Publisher Correction: The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II.
- Published in:
- 2020
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- Correction Notice
Deciphering non-canonical ubiquitin signaling: biology and methodology.
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- Frontiers in Molecular Biosciences, 2024, p. 1, doi. 10.3389/fmolb.2023.1332872
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- Article
Exploration of nuclear body-enhanced sumoylation reveals that PML represses 2-cell features of embryonic stem cells.
- Published in:
- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-33147-6
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- Publication type:
- Article
Exploration of nuclear body-enhanced sumoylation reveals that PML represses 2-cell features of embryonic stem cells.
- Published in:
- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-33147-6
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- Publication type:
- Article
XPC–PARP complexes engage the chromatin remodeler ALC1 to catalyze global genome DNA damage repair.
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- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-31820-4
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- Article
Deubiquitinating enzymes and the proteasome regulate preferential sets of ubiquitin substrates.
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- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-30376-7
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- Article
Identification of proximal SUMO-dependent interactors using SUMO-ID.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-26807-6
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- Article
Zinc finger protein ZNF384 is an adaptor of Ku to DNA during classical non-homologous end-joining.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-26691-0
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- Article
THO complex deficiency impairs DNA double-strand break repair via the RNA surveillance kinase SMG-1.
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- Nucleic Acids Research, 2022, v. 50, n. 11, p. 6235, doi. 10.1093/nar/gkac472
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- Article
Transcription-coupled nucleotide excision repair is coordinated by ubiquitin and SUMO in response to ultraviolet irradiation.
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- Nucleic Acids Research, 2020, v. 48, n. 1, p. 231, doi. 10.1093/nar/gkz977
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- Article
The small CRL4<sup>CSA</sup> ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics.
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- Nature Communications, 2024, v. 15, n. 1, p. 1, doi. 10.1038/s41467-024-50584-7
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- Article
BRCA1/BARD1 ubiquitinates PCNA in unperturbed conditions to promote continuous DNA synthesis.
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- Nature Communications, 2024, v. 15, n. 1, p. 1, doi. 10.1038/s41467-024-48427-6
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- Article
BioE3 identifies specific substrates of ubiquitin E3 ligases.
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- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-43326-8
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- Article
RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2α.
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- Nucleic Acids Research, 2010, v. 38, n. 6, p. 1922, doi. 10.1093/nar/gkp1157
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- Article
The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II.
- Published in:
- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-19643-7
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- Publication type:
- Article
The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation.
- Published in:
- Nature Communications, 2019, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41467-019-11773-x
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- Article
SUMOylation Is Associated with Aggressive Behavior in Chondrosarcoma of Bone.
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- Cancers, 2021, v. 13, n. 15, p. 3823, doi. 10.3390/cancers13153823
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- Article
A proteomics study identifying interactors of the FSHD2 gene product SMCHD1 reveals RUVBL1-dependent DUX4 repression.
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- Scientific Reports, 2021, v. 11, n. 1, p. 1, doi. 10.1038/s41598-021-03030-3
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- Article
Physical interactions between specifically regulated subpopulations of the MCM and RNR complexes prevent genetic instability.
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- PLoS Genetics, 2024, v. 20, n. 5, p. 1, doi. 10.1371/journal.pgen.1011148
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- Article