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

Karyopherin alpha 1

NPI-1, Importin alpha, importin alpha5, NPII, KPNA1
Recombination activating proteins RAG1 and RAG2 regulate and mediate V(D)J recombination, the process by which genes for immunoglobulins and T-cell receptors are generated. Several other ubiquitously expressed proteins are thought to be recruited in the recombination process. Among these are the genes affected in severe combined immune deficiency and genes involved in ds-DNA break repair. The protein encoded by this gene interacts with RAG1 and may play a role in V(D)J recombination. Two transcript variants, one protein-coding and the other not, have been found for this gene. [provided by RefSeq, Jan 2009] (from NCBI)
Top mentioned proteins: Arginine Vasopressin, importin, Neuropilin-1, ACID, CAN
Papers on NPI-1
KPNA3-knockdown eliminates the second heat shock protein peak associated with the heat shock response of male silkworm pupae (Bombyx mori) by reducing heat shock factor transport into the nucleus.
Liu et al., Hefei, China. In Gene, Feb 2016
Three predicted karyopherin alphas (KPNA1, KPNA2 and KPNA3) have been identified from the silkworm Bombyx mori.
Changing expression and subcellular distribution of karyopherins during murine oogenesis.
Holt et al., Newcastle, Australia. In Reproduction, Dec 2015
Of the KPNAs examined (Kpna1, Kpna2, Kpna3, Kpna4, Kpna6, Kpna7, Kpnb1, Ipo5 and Xpo1), all were expressed in the embryonic ovary with up-regulation of protein levels concomitant with meiotic entry for KPNA2, accompanied by the redistribution of the cellular localisation of KPNA2 and XPO1.
AVP-NPII gene mutations and clinical characteristics of the patients with autosomal dominant familial central diabetes insipidus.
Mergen et al., Antalya, Turkey. In Pituitary, Dec 2015
BACKGROUND: Familial central diabetes insipidus (DI), usually an autosomal dominant disorder, is caused by mutations in arginine vasopressin-neurophysin II (AVP-NPII) gene that leads to aberrant preprohormone processing and gradual destruction of AVP-secreting cells.
Identification of a Novel Deletion in AVP-NPII Gene in a Patient with Central Diabetes Insipidus.
Mergen et al., Ankara, Turkey. In Ann Clin Lab Sci, Sep 2015
Our objective was to present the results of the molecular analyses of AVP-neurophysin II (AVP-NPII) gene in a large familial neurohypophyseal (central) DI pedigree.
A novel AVP gene mutation in a Turkish family with neurohypophyseal diabetes insipidus.
Tasan et al., İstanbul, Turkey. In J Endocrinol Invest, Aug 2015
Mutation analysis was performed by sequencing the whole coding region of AVP-NPII gene using DNA isolated from peripheral blood samples.
Identification of an AVP-NPII mutation within the AVP moiety in a family with neurohypophyseal diabetes insipidus: review of the literature.
Skordis et al., Cyprus. In Hormones (athens), Jul 2015
The disorder is caused by mutations affecting the AVP-NPII gene, resulting in absent or deficient secretion of the antidiuretic hormone arginine vasopressin (AVP) by the neurohypophysis.
Early-onset central diabetes insipidus is associated with de novo arginine vasopressin-neurophysin II or Wolfram syndrome 1 gene mutations.
Maghnie et al., Napoli, Italy. In Eur J Endocrinol, Apr 2015
OBJECTIVE: Idiopathic early-onset central diabetes insipidus (CDI) might be due to mutations of arginine vasopressin-neurophysin II (AVP-NPII (AVP)) or wolframin (WFS1) genes.
Autosomal dominant familial neurohypophyseal diabetes insipidus caused by a mutation in the arginine-vasopressin II gene in four generations of a Korean family.
Yoo et al., Pusan, South Korea. In Ann Pediatr Endocrinol Metab, 2014
Autosomal dominant neurohypophyseal diabetes insipidus is a rare form of central diabetes insipidus that is caused by mutations in the vasopressin-neurophysin II (AVP-NPII) gene.
BIG3 Inhibits the Estrogen-Dependent Nuclear Translocation of PHB2 via Multiple Karyopherin-Alpha Proteins in Breast Cancer Cells.
Katagiri et al., Tokushima, Japan. In Plos One, 2014
We found that overexpressed PHB2 interacted with KPNA1, KPNA5, and KPNA6, thereby leading to the E2-dependent translocation of PHB2 into the nuclei of breast cancer cells.
[Identification of prototype foamy virus Bel1 nuclear localization signal and its corresponding importins].
Qiao et al., In Bing Du Xue Bao, 2014
The results of the GST-pulldown showed that the Bel1 fragment with residues 215-223, which bears the NLS, interacts with KPNA1, KPNA6, and KPNA7.
Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnα1 and Kpnβ1.
Wiedlocha et al., Oslo, Norway. In Traffic, 2012
LRRC59 facilitates transport of cytosolic FGF1 through nuclear pores by interaction with Kpns and movement of LRRC59 along the ER and NE membranes
Regulation of karyopherin α1 and nuclear import by mammalian target of rapamycin.
Kristof et al., Montréal, Canada. In J Biol Chem, 2012
mTOR and protein phosphatase 2A catalytically control the constitutive nuclear import of latent STAT1 by KPNA1, which are key modulators of STAT1 expression and apoptosis.
Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin α5.
Cingolani et al., Philadelphia, United States. In J Biol Chem, 2012
Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin alpha5.
The Ebola virus VP24 protein prevents hnRNP C1/C2 binding to karyopherin α1 and partially alters its nuclear import.
Basler et al., New York City, United States. In J Infect Dis, 2011
The ability of hnRNP C1/C2 to bind KPNA1 is diminished in the presence of VP24, and cells transiently expressing VP24 redistribute hnRNP C1/C2 from the nucleus to the cytoplasm.
Nuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 Vpr.
Aida et al., Wako, Japan. In Plos One, 2010
the requirement for and the regulation of CAS in the functioning of the Vpr-Impalpha complex
Mechanisms underlying progressive polyuria in familial neurohypophysial diabetes insipidus.
Oiso et al., Nagoya, Japan. In J Neuroendocrinol, 2010
Familial neurohypophysial diabetes insipidus (FNDI), an autosomal dominant disorder, is mostly caused by mutations in the gene of neurophysin II (NPII), the carrier protein of arginine vasopressin (AVP).
The roles of the RAG1 and RAG2 "non-core" regions in V(D)J recombination and lymphocyte development.
Simkus et al., Washington, D.C., United States. In Arch Immunol Ther Exp (warsz), 2009
Work from multiple laboratories has shed light on activities resident within these domains, including ubiquitin ligase activity and KPNA1 binding by the RING finger domain of RAG1 and the recognition of specific chromatin modifications as well as phosphoinositide binding by the PHD module of RAG2.
Nuclear import and export of proteins: the molecular basis for intracellular signaling.
Yoneda et al., Suita, Japan. In Cytokine Growth Factor Rev, 1998
Recent advances in nuclear protein import have shown that the extracellular signal-dependent nuclear import of Stat1 is mediated via complex formation with NPI-1 (a member of the alpha subunit family) and the beta subunit of the nuclear pore-targeting complex, and a small GTPase, Ran.
Elucidation of neurophysin/bioligand interactions from molecular modeling.
Ciarkowski et al., Gdańsk, Poland. In Acta Biochim Pol, 1996
Neurophysins I and II (NPI and NPII) serve in the neurosecretory granules of the posterior pituitary as carrier proteins for the neurophyseal hormones oxytocin (OT) and vasopressin (VP), respectively, until the latter are released into blood.
Recent gene conversion involving bovine vasopressin and oxytocin precursor genes suggested by nucleotide sequence.
Schütz et al., In Nature, 1984
The organization of these precursors has been established by sequence determination of cloned bovine cDNAs encoding prepro-arginine vasopressin-neurophysin II (prepro-AVP-NPII) and prepro-oxytocin-neurophysin I (prepro-OT-NPI).
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