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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Zinc finger protein 638

The protein encoded by this gene is a nucleoplasmic protein. It binds cytidine-rich sequences in double-stranded DNA. This protein has three types of domains: MH1, MH2 (repeated three times) and MH3. It is associated with packaging, transferring, or processing transcripts. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: p21, CAN, Ciz1, HAD, ACID
Papers on NP220
A multicenter phase II randomized study of Cremophor-free polymeric nanoparticle formulation of paclitaxel in women with locally advanced and/or metastatic breast cancer after failure of anthracycline.
Mohapatra et al., Pune, India. In Asia Pac J Clin Oncol, 2013
METHOD: Patients were randomized to receive either nanoparticle paclitaxel (NP) 300 mg/m(2) , (NP300) or NP220 mg/m(2) or Cremophor paclitaxel 175 mg/m(2) (CP 175).
Regulation of adipocyte differentiation by the zinc finger protein ZNF638.
Mueller et al., Bethesda, United States. In J Biol Chem, 2011
ZNF638 is a novel and early regulator of adipogenesis that works as a transcription cofactor of C/EBPs.
Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus DNA sequence ARYSR(0-2)YYAC.
Keherly et al., Galveston, United States. In J Biomed Sci, 2003
Matrin 3 and NP220 share RNA-binding domains, and NP220 has been shown to recognize and bind to the DNA sequence, CCCCC (G/C).
Mapping of human DNA-binding nuclear protein (NP220) to chromosome band 2p13.1-p13.2 and its relation to matrin 3.
Kitagawa et al., Japan. In Biosci Biotechnol Biochem, 1998
Human NP220 (hNP220) is a novel DNA-binding nuclear protein, which has an arginine/serine-rich motif and polypyrimidine tract-binding motif, and NP220s and matrin 3 are thought to form a novel family of nuclear proteins.
Zinc finger-like motif conserved in a family of RNA binding proteins.
Kitagawa et al., Nagoya, Japan. In Biosci Biotechnol Biochem, 1997
Correction of this sequence showed that the NP220 family has a fourth homologous motif with the characteristics of a Cys2-His2 zinc finger-like motif.
A family of novel DNA-binding nuclear proteins having polypyrimidine tract-binding motif and arginine/serine-rich motif.
Kitagawa et al., Nagoya, Japan. In Biochem Biophys Res Commun, 1996
NP220 is a DNA-binding nuclear protein originally cloned from human cell lines.
A large DNA-binding nuclear protein with RNA recognition motif and serine/arginine-rich domain.
Kitagawa et al., Nagoya, Japan. In J Biol Chem, 1996
cDNA species encoding a large DNA-binding protein (NP220) of 1978 amino acids was isolated from human cDNA libraries.
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