article Open AccessTop 1% cited
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners
BMC Genomics · 2008 · Vol. 9(S1) · pp. S1–S1
Christopher J. Oldfield✉(Indiana University – Purdue University Indianapolis)Jingwei Meng(Indiana University – Purdue University Indianapolis)Jack Yang(Indiana University – Purdue University Indianapolis)Mary Qu Yang(Indiana University – Purdue University Indianapolis)Vladimir N. Uversky(Institute for Biological Instrumentation)A. Keith Dunker(Indiana University – Purdue University Indianapolis)
Abstract
These data support the conjecture that hub proteins often utilize intrinsic disorder to bind to multiple partners and provide detailed information about induced fit in structured regions.
14-3-3 protein interactionsMicrotubule and mitosis dynamicsBioinformatics and Genomic NetworksIntrinsically disordered proteinsFlexibility (engineering)BiologyComputational biologyStructural plasticityFunctional diversityProtein–protein interactionDiversity (politics)GeneticsBiophysics
MeSH terms
Models, MolecularProtein BindingProtein ConformationSignal TransductionTumor Suppressor Protein p5314-3-3 Proteins
Funding
- National Institutes of Health
- Russian Academy of Sciences
Citations
588
FWCI
14.21
field-weighted impact
References
163
Percentile
99%
vs. same field & year
Citations per year
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Biochemistry · 2002 · 1,727 citations
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Nature · 1998 · 42,581 citations
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