References
- Fletcher S and Hamilton AD (2007) Protein-protein interaction inhibitors: small molecules from screening techniques. Curr Top Med Chem 7, 922-927 https://doi.org/10.2174/156802607780906735
- Gonzalez MW and Kann MG (2012) Chapter 4: Protein interactions and disease. PLoS Comput Biol 8, e1002819 https://doi.org/10.1371/journal.pcbi.1002819
- Wells JA and McClendon CL (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009 https://doi.org/10.1038/nature06526
- Scott DE, Bayly AR, Abell C and Skidmore J (2016) Small molecules, big targets: drug discovery faces the protein-protein interaction challenge. Nat Rev Drug Discov 15, 533-550 https://doi.org/10.1038/nrd.2016.29
- Jares-Erijman EA and Jovin TM (2003) FRET imaging. Nat Biotechnol 21, 1387-1395 https://doi.org/10.1038/nbt896
- Kerppola TK (2008) Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu Rev Biophys 37, 465-487 https://doi.org/10.1146/annurev.biophys.37.032807.125842
- Lee KB, Hwang JM, Choi IS et al (2011) Direct monitoring of the inhibition of protein-protein interactions in cells by translocation of PKCdelta fusion proteins. Angew Chem Int Ed Engl 50, 1314-1317 https://doi.org/10.1002/anie.201005333
- Lee KH, Lee S, Lee WY, Yang HW and Heo WD (2010) Visualizing dynamic interaction between calmodulin and calmodulin-related kinases via a monitoring method in live mammalian cells. Proc Natl Acad Sci U S A 107, 3412-3417 https://doi.org/10.1073/pnas.0911262107
- Lee S, Ha JS, Lee SG and Kim TK (2012) Inducible biosynthetic nanoscaffolds as recruitment platforms for detecting molecular target interactions inside living cells. J Am Chem Soc 134, 11346-11349 https://doi.org/10.1021/ja303518d
- Aizer A, Brody Y, Ler LW, Sonenberg N, Singer RH and Shav-Tal Y (2008) The dynamics of mammalian P body transport, assembly, and disassembly in vivo. Mol Biol Cell 19, 4154-4166 https://doi.org/10.1091/mbc.e08-05-0513
- Kedersha N, Stoecklin G, Ayodele M et al (2005) Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol 169, 871-884 https://doi.org/10.1083/jcb.200502088
- Marchi S, Patergnani S and Pinton P (2014) The endoplasmic reticulum-mitochondria connection: one touch, multiple functions. Biochim Biophys Acta 1837, 461-469 https://doi.org/10.1016/j.bbabio.2013.10.015
- Smith JJ and Aitchison JD (2013) Peroxisomes take shape. Nat Rev Mol Cell Biol 14, 803-817 https://doi.org/10.1038/nrm3700
- Zheng D, Ezzeddine N, Chen CY, Zhu W, He X and Shyu AB (2008) Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. J Cell Biol 182, 89-101 https://doi.org/10.1083/jcb.200801196
- Franks TM and Lykke-Andersen J (2008) The control of mRNA decapping and P-body formation. Mol Cell 32, 605-615 https://doi.org/10.1016/j.molcel.2008.11.001
- DeRose R, Miyamoto T and Inoue T (2013) Manipulating signaling at will: chemically-inducible dimerization (CID) techniques resolve problems in cell biology. Pflugers Arch 465, 409-417 https://doi.org/10.1007/s00424-012-1208-6
- Robida AM and Kerppola TK (2009) Bimolecular fluorescence complementation analysis of inducible protein interactions: effects of factors affecting protein folding on fluorescent protein fragment association. J Mol Biol 394, 391-409 https://doi.org/10.1016/j.jmb.2009.08.069
- Iwakuma T and Lozano G (2003) MDM2, an introduction. Mol Cancer Res 1, 993-1000
- Shangary S and Wang S (2008) Targeting the MDM2-p53 interaction for cancer therapy. Clin Cancer Res 14, 5318-5324 https://doi.org/10.1158/1078-0432.CCR-07-5136
- Burgess A, Chia KM, Haupt S, Thomas D, Haupt Y and Lim E (2016) Clinical Overview of MDM2/X-Targeted Therapies. Front Oncol 6, 7
- Kulikov R, Winter M and Blattner C (2006) Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation. J Biol Chem 281, 28575-28583 https://doi.org/10.1074/jbc.M513311200
- Fry DC, Wartchow C, Graves B et al (2013) Deconstruction of a nutlin: dissecting the binding determinants of a potent protein-protein interaction inhibitor. ACS Med Chem Lett 4, 660-665 https://doi.org/10.1021/ml400062c
- Jung S, Choi M, Choi K et al (2017) Inactivation of human DGAT2 by oxidative stress on cysteine residues. PLoS One 12, e0181076 https://doi.org/10.1371/journal.pone.0181076
Cited by
- Splicing Modifier Rescues the Disease Phenotypes in an In Vitro Human Spinal Muscular Atrophy Model pp.1557-8534, 2019, https://doi.org/10.1089/scd.2018.0181