2e64431f8c17d5dd9999d2b6a375858712d494d3
morinlab.bib
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| 1 | +@article{katoUnderstandingFunctionstructureFunctionmutation2003, |
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| 2 | + title = {Understanding the Function-Structure and Function-Mutation Relationships of P53 Tumor Suppressor Protein by High-Resolution Missense Mutation Analysis}, |
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| 3 | + author = {Kato, Shunsuke and Han, Shuang-Yin and Liu, Wen and Otsuka, Kazunori and Shibata, Hiroyuki and Kanamaru, Ryunosuke and Ishioka, Chikashi}, |
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| 4 | + date = {2003-07-08}, |
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| 5 | + journaltitle = {Proceedings of the National Academy of Sciences of the United States of America}, |
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| 6 | + shortjournal = {Proc Natl Acad Sci U S A}, |
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| 7 | + volume = {100}, |
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| 8 | + number = {14}, |
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| 9 | + eprint = {12826609}, |
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| 10 | + eprinttype = {pmid}, |
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| 11 | + pages = {8424--8429}, |
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| 12 | + issn = {0027-8424}, |
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| 13 | + doi = {10.1073/pnas.1431692100}, |
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| 14 | + abstract = {Inactivation of the tumor suppressor p53 by missense mutations is the most frequent genetic alteration in human cancers. The common missense mutations in the TP53 gene disrupt the ability of p53 to bind to DNA and consequently to transactivate downstream genes. However, it is still not fully understood how a large number of the remaining mutations affect p53 structure and function. Here, we used a comprehensive site-directed mutagenesis technique and a yeast-based functional assay to construct, express, and evaluate 2,314 p53 mutants representing all possible amino acid substitutions caused by a point mutation throughout the protein (5.9 substitutions per residue), and correlated p53 function with structure- and tumor-derived mutations. This high-resolution mutation analysis allows evaluation of previous predictions and hypotheses through interrelation of function, structure and mutation.}, |
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| 15 | + langid = {english}, |
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| 16 | + pmcid = {PMC166245}, |
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| 17 | + keywords = {Amino Acid Substitution,DNA Repair,Genes p53,Genes Reporter,Humans,Luciferases,Models Molecular,Mutagenesis Site-Directed,Mutation Missense,Point Mutation,Polymerase Chain Reaction,Protein Conformation,Protein Structure Tertiary,Recombinant Fusion Proteins,Saccharomyces cerevisiae,Structure-Activity Relationship,Transcriptional Activation,Tumor Suppressor Protein p53}, |
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| 18 | + file = {/Users/rmorin/Zotero/storage/K7XZZIYN/Kato et al. - 2003 - Understanding the function-structure and function-.pdf} |
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| 19 | +} |
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| 20 | + |
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| 1 | 21 | @article{skalniakRegulatoryFeedbackLoop2009a, |
| 2 | 22 | title = {Regulatory Feedback Loop between {{NF-kappaB}} and {{MCP-1-induced}} Protein 1 {{RNase}}}, |
| 3 | 23 | author = {Skalniak, Lukasz and Mizgalska, Danuta and Zarebski, Adrian and Wyrzykowska, Paulina and Koj, Aleksander and Jura, Jolanta}, |