Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
Christopher L. Warren(Albert Einstein College of Medicine), David Shechter(Albert Einstein College of Medicine), David Cowburn(Rockefeller University), Sean M. Cahill(Rockefeller University), Jerome M. Karp(Albert Einstein College of Medicine), Takashi Onikubo(Rockefeller University), Tsutomu Matsui(SLAC National Accelerator Laboratory), Mark E. Girvin(Albert Einstein College of Medicine), Michael Brenowitz(Duke University)
Cited by 28
Related Papers
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
|Nature|1992|689
MODULAR PEPTIDE RECOGNITION DOMAINS IN EUKARYOTIC SIGNALING
|Annual Review of Biophysics and Biomolecular Structure|1997|554
Solution Structure of the Proapoptotic Molecule BID
|Cell|1999|391
A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV‐1 Nef protein.
|The EMBO Journal|1995|256
Identification of the Binding Site for Acidic Phospholipids on the PH Domain of Dynamin: Implications for Stimulation of GTPase Activity
|Journal of Molecular Biology|1996|251