[10]. Lambert J M R,Gorzov P, Veprintsev D B, et al. PRIMA-1 reactivates mutant p53 by covalentbinding to the core domain[J]. Cancer cell, 2009, 15(5): 376-388.[11]. https://clinicaltrials.gov/ct2/show/NCT03745716?term=APR-246&phase=2&draw=2&rank=1 ...
Soln structure p53 core domainFersht, A R
别名Mutant type p53(N235K N239Y); Chain A, Human P53 Core Domain Mutant N239y; Human P53 Core Domain Mutant N235K, N239Y. 规格价格50ul/880元 购买 100ul/1580元 购买 200ul/2480元 购买 大包装/询价 说明书50ul 100ul 200ul 研究领域 ...
Jovin, Scanning force microscopy of the complexes of p53 core domain with supercoiled DNA, J. Mol. Biol. 299 (2000) 585-592.Jett SD,Cherny DI,Subramaniam V,et al.Scanning forcemicroscopy of the complexes of p53 core domain with super-coiled DNA〔J〕. Journal of Molecular Biology . 2000...
别名p53 responsive gene 5; p53 responsive gene 5 protein; p53-responsive gene 5; p53-responsive gene 5 protein; PRG5; Protease inhibitor WAP1; Putative protease inhibitor WAP1; WAP four disulfide core domain 5; WAP1; WFDC5_HUMAN.
(2001). A subset of tumor-derived mutant forms of p53 down-regulate p63 and p73 through a direct interaction with the p53 core domain. Mol Cell Biol 21: 1874–1887. Article CAS PubMed PubMed Central Google Scholar Gan L, Xiang M, Zhou L, Wagner DS, Klein WH, Nathans J . (1996)...
A Subset of Tumor-Derived Mutant Forms of p53 Down-Regulate p63 and p73 through a Direct Interaction with the p53 Core Domain The p53 protein is related by sequence homology and function to the products of two other genes, p63 and p73, that each encode several isoforms. We and oth... C...
Figure 1: Molecular visualizations of the p53 core domain. (a,b) All residues of the p53 core domain (1TSR-B33) within 10 Å of Cys124 are shown in a surface representation coloured by atom type: cyan, C; blue, N; red, O; yellow, S. (a) Cys124 is initially occluded in the...
Hot-spot mutants of p53 core domain evince characteristic local structural changes Proc. Natl. Acad. Sci. U S A, 96 (1999), pp. 8438-8442 View in ScopusGoogle Scholar Yan et al., 2014 W. Yan, Y.S. Jung, Y. Zhang, X. Chen Arsenic trioxide reactivates proteasome-dependent degradation...
The residues are found in the more stable paralogs p63 and p73 and stabilise the wild-type p53 core domain. We solved the structure of the HM core domain by X-ray crystallography at 1.75 Ã resolution. It has minimal structural changes from QM that affect the packing of hydrophobic ...