ArticleBiochemistry2009
Preparation of recombinant peptides with site- and degree-specific lysine (13)C-methylation.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- An autoinhibited state of 53BP1 revealed by small molecule antagonists and protein engineering.Nature communications · 2023Article
- TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs.Molecular cell · 2021Article
- Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of 53BP1 Chromatin Recruitment by RNF168/169 and RAD18.Molecular cell · 2017Article
- Article
- Identification of a fragment-like small molecule ligand for the methyl-lysine binding protein, 53BP1.ACS chemical biology · 2015Article
- Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1.Structure (London, England : 1993) · 2015Article
- Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination.Nature structural & molecular biology · 2013Article
- PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53.Nature structural & molecular biology · 2012Article
- RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites.The EMBO journal · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Lysine methylation is an important post-translational modification that affects protein function; for example, the transcriptional activity of the p53 tumor suppressor protein. To facilitate structural characterization of complexes involving proteins and methylated targets by nuclear magnetic resonance spectroscopy, we devised a simple method for preparing recombinant (15)N/(13)C-enriched peptides with a (13)C-methyl-labeled methylated lysine analogue. The method, which relies on the synthesis of (13)C-enriched alkylating agents, was applied to the production of 15-residue p53 peptides variously methylated at lysine analogue 370. The peptides were used to probe the methylation state-dependent interactions of mono, di, and trimethylated p53 with three different proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.