New monoclonal antibodies recognizing p53 protein phosphorylated by casein kinase II at serine 392
Folia biologica.
2001 ;
47 (4) :
148-51.
Language English Country Czech Republic Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
Persistent link
https://www.medvik.cz/link/pmid11508859
PubMed
11508859
Knihovny.cz E-resources
- MeSH
- Protein Denaturation MeSH
- Enzyme-Linked Immunosorbent Assay MeSH
- Phosphorylation MeSH
- Phosphoserine chemistry immunology MeSH
- Hybridomas immunology MeSH
- Immunoblotting MeSH
- Casein Kinase II MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Antibodies, Monoclonal immunology isolation & purification MeSH
- Mice, Inbred BALB C MeSH
- Mice MeSH
- Neoplasm Proteins analysis MeSH
- Tumor Suppressor Protein p53 chemistry immunology metabolism MeSH
- Ovarian Neoplasms chemistry MeSH
- Protein Processing, Post-Translational * MeSH
- Protein Serine-Threonine Kinases metabolism MeSH
- Recombinant Fusion Proteins chemistry immunology MeSH
- Amino Acid Sequence MeSH
- Antibody Specificity MeSH
- Blotting, Western MeSH
- Cross Reactions MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Phosphoserine MeSH
- Casein Kinase II MeSH
- Antibodies, Monoclonal MeSH
- Neoplasm Proteins MeSH
- Tumor Suppressor Protein p53 MeSH
- Protein Serine-Threonine Kinases MeSH
- Recombinant Fusion Proteins MeSH
Evidence for allosteric effects on p53 oligomerization induced by phosphorylation
Protein science.
2018 Feb ;
27 (2) :
523-530.
[epub] 20171208
The Biochemical journal.
2004 Mar 15 ;
378 (Pt 3) :
939-47.
