Nucleophosmin C-terminal leukemia-associated domain interacts with G-rich quadruplex forming DNA.
about
Molecules that target nucleophosmin for cancer treatment: an updateStructure of Nucleophosmin DNA-binding Domain and Analysis of Its Complex with a G-quadruplex Sequence from the c-MYC PromoterStructural polymorphism in the N-terminal oligomerization domain of NPM1Synergic role of nucleophosmin three-helix bundle and a flanking unstructured tail in the interaction with G-quadruplex DNA.G4-DNA formation in the HRAS promoter and rational design of decoy oligonucleotides for cancer therapy.Nucleophosmin mutations alter its nucleolar localization by impairing G-quadruplex binding at ribosomal DNARecognition of intermolecular G-quadruplexes by full length nucleophosmin. Effect of a leukaemia-associated mutation.A redox mechanism underlying nucleolar stress sensing by nucleophosminIdentification of inhibitors of biological interactions involving intrinsically disordered proteins.Leukemia-Associated Mutations in Nucleophosmin Alter Recognition by CRM1: Molecular Basis of Aberrant TransportMAZ-binding G4-decoy with locked nucleic acid and twisted intercalating nucleic acid modifications suppresses KRAS in pancreatic cancer cells and delays tumor growth in mice.Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association.FUsed in sarcoma is a novel regulator of manganese superoxide dismutase gene transcription.Nucleophosmin mutations in acute myeloid leukemia: a tale of protein unfolding and mislocalization.The function of DNA binding protein nucleophosmin in AAV replicationHRAS is silenced by two neighboring G-quadruplexes and activated by MAZ, a zinc-finger transcription factor with DNA unfolding property.Wild-type p53 binds to MYC promoter G-quadruplex.Structural investigation of nucleophosmin interaction with the tumor suppressor Fbw7γ.Chromosomal passenger complex hydrodynamics suggests chaperoning of the inactive state by nucleoplasmin/nucleophosmin.AML cells carrying NPM1 mutation are resistant to nucleophosmin displacement from nucleoli caused by the G-quadruplex ligand TmPyP4.Conformational stabilization as a strategy to prevent nucleophosmin mislocalization in leukemia.DNA G-quadruplexes show strong interaction with DNA methyltransferases in vitro.Self-interaction of NPM1 modulates multiple mechanisms of liquid-liquid phase separation.
P2860
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P2860
Nucleophosmin C-terminal leukemia-associated domain interacts with G-rich quadruplex forming DNA.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Nucleophosmin C-terminal leuke ...... G-rich quadruplex forming DNA.
@en
type
label
Nucleophosmin C-terminal leuke ...... G-rich quadruplex forming DNA.
@en
prefLabel
Nucleophosmin C-terminal leuke ...... G-rich quadruplex forming DNA.
@en
P2093
P2860
P50
P356
P1476
Nucleophosmin C-terminal leuke ...... G-rich quadruplex forming DNA.
@en
P2093
Bruno Giardina
Carlo Lo Sterzo
Flavio Scaloni
Giovanni L Scaglione
Luca Federici
P2860
P304
37138-37149
P356
10.1074/JBC.M110.166736
P407
P577
2010-09-20T00:00:00Z