alpha Karyopherins: Nucleocytoplasmic transport molecules that bind to the NUCLEAR LOCALIZATION SIGNALS of cytoplasmic molecules destined to be imported into the CELL NUCLEUS. Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX. Inside the CELL NUCLEUS alpha karyopherins dissociate from beta karypherins and their cargo. They then form a complex with CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN and RAN GTP-BINDING PROTEIN which is exported to the CYTOPLASM.Karyopherins: A family of proteins involved in NUCLEOCYTOPLASMIC TRANSPORT. Karyopherins are heteromeric molecules composed two major types of components, ALPHA KARYOPHERINS and BETA KARYOPHERINS, that function together to transport molecules through the NUCLEAR PORE COMPLEX. Several other proteins such as RAN GTP BINDING PROTEIN and CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN bind to karyopherins and participate in the transport process.beta Karyopherins: Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.Nuclear Pore: An opening through the NUCLEAR ENVELOPE formed by the nuclear pore complex which transports nuclear proteins or RNA into or out of the CELL NUCLEUS and which, under some conditions, acts as an ion channel.Active Transport, Cell Nucleus: Gated transport mechanisms by which proteins or RNA are moved across the NUCLEAR MEMBRANE.ran GTP-Binding Protein: A monomeric GTP-binding protein involved in nucleocytoplasmic transport of proteins into the nucleus and RNA into the cytoplasm. This enzyme was formerly listed as EC 3.6.1.47.Nuclear Pore Complex Proteins: Proteins that form the structure of the NUCLEAR PORE. They are involved in active, facilitated and passive transport of molecules in and out of the CELL NUCLEUS.Nuclear Localization Signals: Short, predominantly basic amino acid sequences identified as nuclear import signals for some proteins. These sequences are believed to interact with specific receptors at the NUCLEAR PORE.Cell Nucleus: Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Nuclear Proteins: Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Receptors, Cytoplasmic and Nuclear: Intracellular receptors that can be found in the cytoplasm or in the nucleus. They bind to extracellular signaling molecules that migrate through or are transported across the CELL MEMBRANE. Many members of this class of receptors occur in the cytoplasm and are transported to the CELL NUCLEUS upon ligand-binding where they signal via DNA-binding and transcription regulation. Also included in this category are receptors found on INTRACELLULAR MEMBRANES that act via mechanisms similar to CELL SURFACE RECEPTORS.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.Receptors, Adrenergic, alpha: One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.Hypoxia-Inducible Factor 1, alpha Subunit: Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.alpha7 Nicotinic Acetylcholine Receptor: A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric a7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen.Integrin alpha3beta1: Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.Integrin alpha4: An integrin alpha subunit that is unique in that it does not contain an I domain, and its proteolytic cleavage site is near the middle of the extracellular portion of the polypeptide rather than close to the membrane as in other integrin alpha subunits.Integrin alpha6: An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.Integrin alpha5beta1: An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.Integrin alpha4beta1: Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.Interleukin-1alpha: An interleukin-1 subtype that occurs as a membrane-bound pro-protein form that is cleaved by proteases to form a secreted mature form. Unlike INTERLEUKIN-1BETA both membrane-bound and secreted forms of interleukin-1alpha are biologically active.Integrin alpha2beta1: An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.Receptors, Adrenergic, alpha-1: A subclass of alpha-adrenergic receptors that mediate contraction of SMOOTH MUSCLE in a variety of tissues such as ARTERIOLES; VEINS; and the UTERUS. They are usually found on postsynaptic membranes and signal through GQ-G11 G-PROTEINS.Integrin alpha5: This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.Integrin alpha1beta1: Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.

Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. (1/392)

Although many viruses replicate in the nucleus, little is known about the processes involved in the nuclear import of viral genomes. We show here that in vitro generated core particles of human hepatitis B virus bind to nuclear pore complexes (NPCs) in digitonin-permeabilized mammalian cells. This only occurred if the cores contained phosphorylated core proteins. Binding was inhibited by wheat germ agglutinin, by antinuclear pore complex antibodies, and by peptides corresponding either to classical nuclear localization signals (NLS) or to COOH-terminal sequences of the core protein. Binding was dependent on the nuclear transport factors importins (karyopherins) alpha and beta. The results suggested that phosphorylation induces exposure of NLS in the COOH-terminal portion of the core protein that allows core binding to the NPCs by the importin- (karyopherin-) mediated pathway. Thus, phosphorylation of the core protein emerged as an important step in the viral replication cycle necessary for transport of the viral genome to the nucleus.  (+info)

Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R. (2/392)

The erythroid membrane cytoskeletal protein 4.1 is the prototypical member of a genetically and topologically complex family that is generated by combinatorial alternative splicing pathways and is localized at diverse intracellular sites including the nucleus. To explore the molecular determinants for nuclear localization, we transfected COS-7 cells with epitope-tagged versions of natural red cell protein 4.1 (4.1R) isoforms as well as mutagenized and truncated derivatives. Two distant topological sorting signals were required for efficient nuclear import of the 4.1R80 isoform: a basic peptide, KKKRER, encoded by alternative exon 16 and acting as a weak core nuclear localization signal (4.1R NLS), and an acidic peptide, EED, encoded by alternative exon 5. 4.1R80 isoforms lacking either of these two exons showed decreased nuclear import. Fusion of various 4.1R80 constructs to the cytoplasmic reporter protein pyruvate kinase confirmed a requirement for both motifs for full NLS function. 4.1R80 was efficiently imported in the nuclei of digitonin-permeabilized COS-7 cells in the presence of recombinant Rch1 (human importin alpha2), importin beta, and GTPase Ran. Quantitative analysis of protein-protein interactions using a resonant mirror detection technique showed that 4.1R80 bound to Rch1 in vitro with high affinity (KD = 30 nM). The affinity decreased at least 7- and 20-fold, respectively, if the EED motif in exon 5 or if 4.1R NLS in exon 16 was lacking or mutated, confirming that both motifs were required for efficient importin-mediated nuclear import of 4.1R80.  (+info)

Nuclear import of plasmid DNA in digitonin-permeabilized cells requires both cytoplasmic factors and specific DNA sequences. (3/392)

Although much is known about the mechanisms of signal-mediated protein and RNA nuclear import and export, little is understood concerning the nuclear import of plasmid DNA. Plasmids between 4.2 and 14.4 kilobases were specifically labeled using a fluorescein-conjugated peptide nucleic acid clamp. The resulting substrates were capable of gene expression and nuclear localization in microinjected cells in the absence of cell division. To elucidate the requirements for plasmid nuclear import, a digitonin-permeabilized cell system was adapted to follow the nuclear localization of plasmids. Nuclear import of labeled plasmid was time- and energy-dependent, was inhibited by the lectin wheat germ agglutinin, and showed an absolute requirement for cytoplasmic extract. Addition of nuclear extract alone did not support plasmid nuclear import but in combination with cytoplasm stimulated plasmid nuclear localization. Whereas addition of purified importin alpha, importin beta, and RAN was sufficient to support protein nuclear import, plasmid nuclear import also required the addition of nuclear extract. Finally, nuclear import of plasmid DNA was sequence-specific, requiring a region of the SV40 early promoter and enhancer. Taken together, these results confirm and extend our findings in microinjected cells and support a protein-mediated mechanism for plasmid nuclear import.  (+info)

Nuclear import of RPA in Xenopus egg extracts requires a novel protein XRIPalpha but not importin alpha. (4/392)

Replication protein A (RPA) is a eukaryotic single-stranded (ss) DNA-binding protein that is essential for general DNA metabolism. RPA consists of three subunits (70, 33 and 14 kDa). We have identified by two-hybrid screening a novel Xenopus protein called XRIPalpha that interacts with the ssDNA-binding domain of the largest subunit of RPA. XRIPalpha homologues are found in human and in Drosophila but not in yeast. XRIPalpha is complexed with RPA in Xenopus egg extracts together with another 90 kDa protein that was identified as importin beta. We have demonstrated that XRIPalpha, but not importin alpha, is required for nuclear import of RPA. Immunodepletion of XRIPalpha from the egg extracts blocks nuclear import of RPA but not that of nucleoplasmin, a classical import substrate. RPA import can be restored by addition of recombinant XRIPalpha. Conversely, depletion of importin alpha blocks import of nucleoplasmin but not that of RPA. GST-XRIPalpha pull-down assay shows that XRIPalpha interacts directly with recombinant importin beta as well as with RPA in vitro. Finally, RPA import can be reconstituted from the recombinant proteins. We propose that XRIPalpha plays the role of importin alpha in the RPA import scheme: XRIPalpha serves as an adaptor to link RPA to importin beta.  (+info)

The direction of transport through the nuclear pore can be inverted. (5/392)

Transport of macromolecules across the nuclear envelope is an active process that depends on soluble factors including the GTPase Ran. Ran-GTP is predominantly located in the nucleus and has been shown to regulate cargo binding and release of import and export receptors in their respective target compartments. Recently, it was shown that transport of receptor-cargo complexes across the nuclear pore complex (NPC) does not depend on GTP-hydrolysis by Ran; however, the mechanism of translocation is still poorly understood. Here, we show that the direction of transport through the NPC can be inverted in the presence of high concentrations of cytoplasmic Ran-GTP. Under these conditions, two different classes of export cargoes are transported into the nucleus in the absence of GTP hydrolysis. The inverted transport is very rapid and can be blocked by known inhibitors of nuclear protein export. These results suggest that the NPC functions as a facilitated transport channel, allowing the selective translocation of receptor-cargo complexes. We conclude that the directionality of nucleocytoplasmic transport is determined mainly by the compartmentalized distribution of Ran-GTP.  (+info)

Cellular uptake and nuclear delivery of recombinant adenovirus penton base. (6/392)

An Ad2 capsid component, the penton base, expressed as recombinant protein, was found to be capable of affecting the entire entry pathway of adenovirion in HeLa cells, i.e., cell attachment, endocytosis, vesicular escape, intracytoplasmic movement, and translocation through the nuclear pore complex. Data with pentamerization-defective mutants suggested that none of these successive steps depended upon penton base pentamer status, indicating that the peptide domains responsible for these functions were carried by the monomer. Observations performed with wild-type (WT) and an integrin-binding-site double-mutant (K288E340) suggested that the penton base could enter the cell via an alternative, RGD- and LDV-independent, pathway. Of three mutants that were found to be defective in nuclear addressing in insect cells, only one, W165H, was also altered in nuclear transport in HeLa cells. The other two, W119H and RRR547EQQ, showed a WT pattern of nuclear localization in HeLa cells, suggesting that the region including tryptophan-119 and the basic signal at position 547 did not act as a nuclear localization signal in the human cell context. The integrity of cellular structures and the cytoskeleton seemed to be required for the vectorial movement and nuclear import of WT penton base, as suggested by experiments using permeabilized HeLa cells, isolated nuclear membranes, and cytoskeleton-targeted drugs.  (+info)

The yeast nucleoporin Nup2p is involved in nuclear export of importin alpha/Srp1p. (7/392)

The importin alpha.beta heterodimer mediates nuclear import of proteins containing classical nuclear localization signals. After carrying its cargo into the nucleus, the importin dimer dissociates, and Srp1p (the yeast importin alpha subunit) is recycled to the cytoplasm in a complex with Cse1p and RanGTP. Nup2p is a yeast FXFG nucleoporin that contains a Ran-binding domain. We find that export of Srp1p from the nucleus is impaired in Deltanup2 mutants. Also, Srp1p fusion proteins accumulate at the nuclear rim in wild-type cells but accumulate in the nuclear interior in Deltanup2 cells. A deletion of NUP2 shows genetic interactions with mutants in SRP1 and PRP20, which encodes the Ran nucleotide exchange factor. Srp1p binds directly to an N-terminal domain of Nup2p. This region of Nup2p is sufficient to allow accumulation of an Srp1p fusion protein at the nuclear rim, but the C-terminal Ran-binding domain of Nup2p is required for efficient Srp1p export. Formation of the Srp1p.Cse1p. RanGTP export complex releases Srp1p from its binding site in Nup2p. We propose that Nup2p may act as a scaffold that facilitates formation of the Srp1p export complex.  (+info)

A bipartite nuclear localization signal is required for p53 nuclear import regulated by a carboxyl-terminal domain. (8/392)

Abnormal p53 cellular localization has been considered to be one of the mechanisms that could inactivate p53 function. To understand the regulation of p53 cellular trafficking, we have previously identified two p53 domains involved in its localization. A basic domain, Lys(305)-Arg(306), is required for p53 nuclear import, and a carboxyl-terminal domain, namely the cytoplasmic sequestration domain (CSD) from residues 326-355, could block the nuclear import of Lys(305) or Arg(306) mutated p53. To characterize further the function of these two domains, we demonstrate in this report that the previously described major nuclear localization signal works together with Lys(305)-Arg(306) to form a bipartite and functional nuclear localization sequence (NLS) for p53 nuclear import. The CSD could block the binding of p53 to the NLS receptor, importin alpha, and reduce the efficiency of p53 nuclear import in MCF-7, H1299, and Saos-2 cells. The blocking effect of the CSD is not due to the enhancement of nuclear export or oligomerization of the p53. These results indicate that the CSD can regulate p53 nuclear import by controlling access of the NLS to importin alpha binding.  (+info)

*Importin

"Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha". ... Importin: IPO4, IPO5, IPO7, IPO8, IPO9, IPO11, IPO13 Karyopherin-α: KPNA1, KPNA2, KPNA3, KPNA4, KPNA5, KPNA6 Karyopherin-β: ... Each one of these repeats contains two antiparallel alpha helices linked by a turn, which stack together to form the overall ... Importin-β is the typical structure of a larger superfamily of karyopherins. The basis of their structure is 18-20 tandem ...

*Nuclear localization sequence

"Crystallographic analysis of the recognition of a nuclear localisation signal by the nuclear import factor karyopherin alpha". ... A protein translated with a NLS will bind strongly to importin (aka karyopherin), and, together, the complex will move through ... analysis of the specific yet versatile recognition of distinct nuclear localisation signals by karyopherin alpha". Structure. 8 ... also known as transportin or karyopherin β2), which then translocates the cargo protein into the nucleus. The structural basis ...

*Transportin 1

"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... The classical karyopherin receptor complex, such as the complex that uses Importin-β1 (encoded by gene KPNB1), is a heterodimer ... However, Transportin-1 can directly bind to the cargo proteins and may not need importin alpha subunit to do it. Transportin-1 ... Bonifaci N, Moroianu J, Radu A, Blobel G (Jun 1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". ...

*Karyopherin alpha 1

"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... Importin subunit alpha-1 is a protein that in humans is encoded by the KPNA1 gene. Karyopherin alpha 1 has been shown to ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Percipalle, P; Clarkson W D; Kent H M; Rhodes D; Stewart M (Mar 1997). "Molecular interactions between the importin alpha/beta ...

*Karyopherin alpha 2

"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "Entrez Gene: KPNA2 karyopherin alpha 2 (RAG cohort 1, importin alpha 1)". Lin CY, Huang PH, Liao WL, Cheng HJ, Huang CF, Kuo JC ... KPNA2 also may play a role in V(D)J recombination Karyopherin alpha 2 has been shown to interact with: ARL4A ITK, KPNB1, PLAG1 ... Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML (May 2002). "Identification of a karyopherin alpha 2 ...

*TMCO6

The SRP1 domain is Karyopherin(importin) alpha. This is involved in the exchange of molecules from the nucleus and the ... The SRP1 domain encodes alpha-Karyopherin (importin) and is known for intracellular trafficking and secretion on the membrane. ... The exchange involves the active transport by a carrier protein called karyopherins. A di-leucine motif is also abundant in ...

*KPNA3

"Entrez Gene: KPNA3 karyopherin alpha 3 (importin alpha 4)". Köhler, M; Speck C; Christiansen M; Bischoff F R; Prehn S; Haller H ... The similarities among these proteins suggests that karyopherin alpha-3 may be involved in the nuclear transport system. KPNA3 ... "Isolation and mapping of karyopherin alpha 3 (KPNA3), a human gene that is highly homologous to genes encoding Xenopus importin ... Importin subunit alpha-3 is a protein that in humans is encoded by the KPNA3 gene. The transport of molecules between the ...

*KPNA6

"Entrez Gene: KPNA6 karyopherin alpha 6 (importin alpha 7)". Bukrinsky MI, Haffar OK (2004). "HIV-1 nuclear import: in search of ... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... Importin subunit alpha-7 is a protein that in humans is encoded by the KPNA6 gene. Nucleocytoplasmic transport, a signal- and ... Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. The protein encoded by ...

*KPNA4

"Entrez Gene: KPNA4 karyopherin alpha 4 (importin alpha 3)". Liu L, McBride KM, Reich NC (Jun 2005). "STAT3 nuclear import is ... "Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family ... Importin subunit alpha-4 is a protein that in humans is encoded by the KPNA4 gene. The nuclear import of karyophilic proteins ... Gallay P, Stitt V, Mundy C, Oettinger M, Trono D (Feb 1996). "Role of the karyopherin pathway in human immunodeficiency virus ...

*KPNA5

"Entrez Gene: KPNA5 karyopherin alpha 5 (importin alpha 6)". Bukrinsky MI, Haffar OK (2004). "HIV-1 nuclear import: in search of ... "Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family ... Importin subunit alpha-6 is a protein that in humans is encoded by the KPNA5 gene. The transport of molecules between the ... 1996). "Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import". J. Virol. 70 (2): 1027-32. PMC ...

*ARL4A

... has been shown to interact with Karyopherin alpha 2. GRCh38: Ensembl release 89: ENSG00000122644 - Ensembl, May 2017 ...

*PLAG1

Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML (2002). "Identification of a karyopherin alpha 2 recognition ... PLAG1 has been shown to interact with Karyopherin alpha 2. GRCh38: Ensembl release 89: ENSG00000181690 - Ensembl, May 2017 ... "Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal". J. Biol. ...

*RECQL

... has been shown to interact with KPNA4 and Karyopherin alpha 2. GRCh38: Ensembl release 89: ENSG00000004700 - Ensembl, May ... Seki T, Tada S, Katada T, Enomoto T (1997). "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination ... "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination of Qip1 and Rch1 from hSrp1 by their ability ...

*Nucleoporin 153

"RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the nucleoporin Nup153". Proc. Natl. Acad. ... It also acts as the docking site of an importing karyopherin. On the cytoplasmic side of the NPC, Nup358 fulfills an analogous ... Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin beta3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): ... Brownawell AM, Macara IG (2002). "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding ...

*UBR5

... has been shown to interact with: CIB1, Karyopherin alpha 1, MAPK1, and TOPBP1. GRCh38: Ensembl release 89: ENSG00000104517 ...

*KPNB1

... has been shown to interact with: KPNA3, Karyopherin alpha 1, Karyopherin alpha 2, Mothers against decapentaplegic homolog ... Each of these subunits are part of the karyopherin family of proteins. Importin alpha binds the NLS-containing cargo in the ... Moroianu J, Blobel G, Radu A (September 1997). "RanGTP-mediated nuclear export of karyopherin alpha involves its interaction ... Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta". Proc. ...

*NUP98

Moroianu J, Blobel G, Radu A (September 1997). "RanGTP-mediated nuclear export of karyopherin alpha involves its interaction ... Bonifaci N, Moroianu J, Radu A, Blobel G (May 1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". ... Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin beta3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): ... Bonifaci N, Moroianu J, Radu A, Blobel G (1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". Proc. ...

*ITK (gene)

"Nuclear localization of the tyrosine kinase Itk and interaction of its SH3 domain with karyopherin alpha (Rch1alpha)". Int. ...

*List of MeSH codes (D12.776.157)

... karyopherins MeSH D12.776.157.530.750.500.100 -- alpha karyopherins MeSH D12.776.157.530.750.500.249 -- beta karyopherins MeSH ... gtp-binding protein alpha subunits, g12-g13 MeSH D12.776.157.325.332.100.200 -- gtp-binding protein alpha subunits, gi-go MeSH ... gtp-binding protein alpha subunits, gq-g11 MeSH D12.776.157.325.332.100.400 -- gtp-binding protein alpha subunits, gs MeSH ... alpha subunit MeSH D12.776.157.057.061.500.500 -- stat1 transcription factor MeSH D12.776.157.057.061.500.750 -- stat2 ...

*Importin α

Importin alpha, or karyopherin alpha refers to a class of adaptor proteins that are involved in the import of proteins into the ... Moroianu, J; Blobel, G; Radu, A (1996-06-25). "The binding site of karyopherin alpha for karyopherin beta overlaps with a ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Wang, P.; Palese, P.; O'Neill, R. E. (1997-03-01). "The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus ...

*Ebola viral protein 24

2014). "Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of ... KPNA proteins have 10 armadillo repeats each consisting of three alpha helices which determine their binding specificity, the ... Additionally, eVP24 inhibits interferon signaling by competitively binding to karyopherins which blocks phosphorylated STAT1 ... "The Ebola virus VP24 protein prevents hnRNP C1/C2 binding to karyopherin α1 and partially alters its nuclear import". J. Infect ...

*List of MeSH codes (D12.776.543)

... karyopherins MeSH D12.776.543.585.750.500.100 -- alpha karyopherins MeSH D12.776.543.585.750.500.249 -- beta karyopherins MeSH ... gtp-binding protein alpha subunits, g12-g13 MeSH D12.776.543.325.100.200 -- gtp-binding protein alpha subunits, gi-go MeSH ... gtp-binding protein alpha subunits, gq-g11 MeSH D12.776.543.325.100.400 -- gtp-binding protein alpha subunits, gs MeSH D12.776. ... alpha-1 MeSH D12.776.543.750.720.300.300.300.300.200 -- receptors, adrenergic, alpha-2 MeSH D12.776.543.750.720.300.300.300.340 ...

*IRF1

"Differential regulation of karyopherin alpha 2 expression by TGF-beta1 and IFN-gamma in normal human epidermal keratinocytes: ...

*Karyopherin

First, it is binding importin alpha - another type of karyopherin that binds the cargo protein in the cytoplasm - before the ... Most proteins require karyopherins to traverse the nuclear pore. Karyopherins can act as importins (i.e. helping proteins get ... Karyopherins at the US National Library of Medicine Medical Subject Headings (MeSH) Illustrations at berkeley.edu Karyopherin ... Karyopherins are a group of proteins involved in transporting molecules between the cytoplasm and the nucleus of a eukaryotic ...

*IPO5

... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between ... Chook YM, Blobel G (2002). "Karyopherins and nuclear import". Curr. Opin. Struct. Biol. 11 (6): 703-15. doi:10.1016/S0959-440X( ... "Cloning and characterization of human karyopherin beta3". Proc Natl Acad Sci U S A. 94 (9): 4451-6. doi:10.1073/pnas.94.9.4451 ...

*MicroRNA

Zuo Y, Qiang L, Farmer SR (March 2006). "Activation of CCAAT/enhancer-binding protein (C/EBP) alpha expression by C/EBP beta ... a member of the karyopherin family, recognizes a two-nucleotide overhang left by the RNase III enzyme Drosha at the 3' end of ... such as TNF alpha or GM-CSF. It has been demonstrated that given complete complementarity between the miRNA and target mRNA ... adipogenesis requires a peroxisome proliferator-activated receptor-gamma-associated repression of HDAC1 at the C/ebp alpha gene ...
The translocation of macromolecules into the nucleus is a fundamental eukaryotic process, regulating gene expression, cell division and differentiation, but which is impaired in a range of significant diseases including cancer and viral infection. The import of proteins into the nucleus is generally initiated by a specific, high affinity interaction between nuclear localisation signals (NLSs) and nuclear import receptors in the cytoplasm, and terminated through the disassembly of these complexes in the nucleus. For classical NLSs (cNLSs), this import is mediated by the importin-alpha (IMP alpha) adaptor protein, which in turn binds to IMP beta to mediate translocation of nuclear cargo across the nuclear envelope. The interaction and disassembly of import receptor: cargo complexes is reliant on the differential localisation of nucleotide bound Ran across the envelope, maintained in its low affinity, GDP-bound form in the cytoplasm, and its high affinity, GTP-bound form in the nucleus. This in ...
1.I.1 The Eukaryotic Nuclear Pore Complex (E-NPC) Family [formerly 1.A.75]. Numerous NPC proteins, called nucleoporins, have been identified and characterized from vertebrates and yeast (Brohawn et al., 2009). Thirty such proteins are recognized constituents of the yeast NPC, and at least 50 nucleopore proteins have been characterized from vertebrates. Many of these proteins have been tabulated for (1) S. cerevisiae and (2) vertebrates by Stoffler et al. (1999) and Tran and Wente (2006). How they function in transport is poorly defined. It is known, however, that nuclear proteins contain short sequences called nuclear localization sequences (NLS) that target them for nuclear import. A nuclear localization sequence receptor and several cytosolic factors appear to play roles in nuclear import of NLS-bearing proteins. Nuclear export signals (NESs) have also been identified. Several different forms of each type of targeting signal have been identified that lack homology to each other and may be ...
KPNA4 (karyopherin alpha 4), also known as importin alpha 3, is a member of the importin alpha family of proteins which includes KPNA1 (importin alpha…
The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in cell division regulation. The active transport of proteins between the nucleus and the cytoplasm is mediated by the transport receptors of the β-karyopherin family. In this work we characterized the terminal phenotype of a mutant strain in β-karyopherin Kap95, a component of the classical nuclear import pathway. When KAP95 was inactivated, most cells arrested at the G2/M phase of the cell cycle, which is in agreement with the results observed in mutants in the other components of this pathway. However, a number of cells accumulate at G1, suggesting a novel role of Kap95 and the classical import pathway at Start. We investigated the localization of Start transcription factors. It is known that Swi6 contains a classical NLS that interacts with importin α. Here we show that the in vivo nuclear import of Swi6 depends on Kap95. For Swi4, we identified a functional NLS between amino acids 371 and 376
Importin alpha 5/KPNA1/SRP1 products available through Novus Biologicals. Browse our Importin alpha 5/KPNA1/SRP1 product catalog backed by our Guarantee+.
importin-alpha-P1, importin alpha 1, IPOA1, karyopherin alpha 2 (RAG cohort 1, importin alpha 1), Karyopherin subunit alpha-2, pendulin, QIP2importin alpha 2, RAG cohort 1, RAG cohort protein 1, RCH1importin subunit alpha-2, SRP1, SRP1alpha, SRP1- ...
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Specialized trafficking systems in eukaryotic cells serve a critical role in partitioning intracellular proteins between the nucleus and cytoplasm. Cytoplasmic proteins (including chromatin remodeling enzymes and transcription factors) must gain access to the nucleus to exert their functions to properly program fundamental cellular events ranging from cell cycle progression to gene transcription. Knowing that nuclear import mediated by members of the karyopherin α family of transport receptors plays a critical role in regulating development and differentiation, we wanted to determine the identity of proteins that are trafficked by this karyopherin α pathway. To this end, we performed a GST pull-down assay using porcine orthologs of karyopherin α1 (KPNA1) and karyopherin α7 (KPNA7) and prey protein derived from porcine fibroblast cells and used a liquid chromatography and tandem mass spectrometry (LC-MS/MS) approach to determine the identity of KPNA1 and KPNA7 interacting proteins. Our screen
The importin-alpha/beta complex and the GTPase Ran mediate nuclear import of proteins with a classical nuclear localization sigl. The protein encoded…
KPNA6 - KPNA6 (untagged)-Human karyopherin alpha 6 (importin alpha 7) (KPNA6) available for purchase from OriGene - Your Gene Company.
Elevated expression of members of the nuclear transport protein family has been reported in multiple cancers and presents as novel anticancer therapeutic targets. Using a cervical cancer model system, we have previously shown that inhibition of the nuclear import receptor, KpnB1 by siRNA and a novel small molecule, Inhibitor of Nuclear Import (INI-43) resulted in cancer cell death via apoptosis. In this study, we investigated the cancer cell killing effects of KpnB1 inhibition in combination with Cisplatin (CDDP), a first-line chemotherapeutic agent used in the treatment of many cancers. KpnB1 siRNA and INI-43 treatment at sub-lethal concentrations enhanced cancer cells sensitivity to CDDP. Our data shows that the combination treatment of INI-43 and CDDP significantly decreases CDDP IC50 compared to CDDP treatment alone. Increased PARP-cleavage was observed in combination treated cells and this correlated with increased γH2A.X, indicating increased apoptosis and DNA damage. Furthermore, INI-43 ...
Karyopherin (importin) beta 3 RNAi available through Novus Biologicals. Browse our Karyopherin (importin) beta 3 RNAi catalog backed by our Guarantee+.
A nuclear receptor likely involved in nuclear protein import is described. Purified ATP-depleted yeast nuclei show saturable high-affinity binding of the yeast nuclear protein Mcm1. The dissociation constant for the binding is 0.5 microM, and the number of binding sites is approximately 3,500 per nucleus, equivalent to 10-30 binding sites per nuclear pore. Mcm1 competes with other yeast nuclear proteins Ste12 and Swi5, but not with Rap1 or Nop1, indicating that there may be different types of import receptors. Bound Mcm1 is resistant to extraction by nucleases, salt, and non-ionic detergent, but can be released by 5 M urea, suggesting that Mcm1 binds to a yeast equivalent of the nuclear pore complex-lamina fraction of higher eukaryotes ...
KPNA3 antibody, C-term (karyopherin alpha 3 (importin alpha 4)) for ICC/IF, IHC-P, IP, WB. Anti-KPNA3 pAb (GTX26038) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
I am currently working on a computer user interface for specifying (not designing) mutational protein libraries. In addition to a online forms interface I would like to be able to directly import protein sequence data and multiple sequence alignments from a file. I was wondering whether any researchers would like to comment on what types of programs and data formats are popular. In paticular, I am considering an function to directly import Excel spreadsheet files (ala GoCore, etc.). Any comments would be greatly appreciated. Rick Colman UC Irvine ...
KPNA6 - KPNA6 - Human, 4 unique 29mer shRNA constructs in retroviral RFP vector shRNA available for purchase from OriGene - Your Gene Company.
购买KPNA6兔多克隆抗体(ab105350),KPNA6抗体经WB,ICC/IF验证,可与人,小鼠,大鼠样本反应。产品出库一年都在质保范围内。中国现货速达。
Complete information for KPNA5 gene (Protein Coding), Karyopherin Subunit Alpha 5, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
KPNA2兔多克隆抗体(ab82313)可与人样本反应并经WB, ELISA实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
(A) Effect of RCC1 depletion on Rch1 recycling. tsBN2 cells were injected with Rch133-529 into the cytoplasm followed by incubation at 33.5°C (a and b) or
Satellite cells are stem cells with an essential role in skeletal muscle repair. Precise regulation of gene expression is critical for proper satellite cell quiescence, proliferation, differentiation and self-renewal. Nuclear proteins required for gene expression are dependent on the nucleocytoplasmic transport machinery to access to nucleus, however little is known about regulation of nuclear transport in satellite cells. The best characterized nuclear import pathway is classical nuclear import which depends on a classical nuclear localization signal (cNLS) in a cargo protein and the heterodimeric import receptors, karyopherin alpha (KPNA) and beta (KPNB). Multiple KPNA1 paralogs exist and can differ in importing specific cNLS proteins required for cell differentiation and function. We show that transcripts for six Kpna paralogs underwent distinct changes in mouse satellite cells during muscle regeneration accompanied by changes in cNLS proteins in nuclei. Depletion of KPNA1, the most ...
Importin is a type of karyopherin that transports protein molecules into the nucleus by binding to specific recognition sequences, called nuclear localization sequences (NLS). Importin has two subunits, importin α and importin β. Members of the importin-β family can bind and transport cargo by themselves, or can form heterodimers with importin-α. As part of a heterodimer, importin-β mediates interactions with the pore complex, while importin-α acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo. The NLS-Importin α-Importin β trimer dissociates after binding to Ran GTP inside the nucleus, with the two importin proteins being recycled to the cytoplasm for further use. Importin can exist as either a heterodimer of importin-α/β or as a monomer of Importin-β. Importin-α was first isolated in 1994 by a group including Enno Hartmann, based at the Max Delbrück Center for Molecular Medicine. The process of nuclear protein import had already been ...
View Notes - Lecture 6 10 from BICD 110 at UCSD. Lecture 6 10/10/07 Nuclear Import/Export Nuclear Import Receptors Importins Helps cargo get into nucleus does this by binding to cargo (protein with
Our results define a bipartite NLS that is integrated within the DNA-recognition region of IRF3. We mapped the NLS of IRF3 to aa 64-130, partially overlapping with the DBD. Basic amino acids KR77/78 and RK86/87 are required for efficient nuclear import of IRF3. Significantly, we demonstrate that the NLS of IRF3 also plays an important role in the DNA-binding activity.. The IRF family contains nine mammalian members (IRF1, IRF2, IRF3, IRF4, IRF5, IRF6, IRF7, IRF8, and IRF9), which are most conserved in their DBD. IRF1 and IRF2, which are closely related to each other, contain a conserved NLS located immediately C-terminal to the DBD, involving aa 120-138 (33). IRF4, IRF8, and IRF9 are highly conserved with each other and use the homologous NLS (aa 66-85) to direct their accumulation in the nucleus (34). Interestingly, IRF5 contains two monopartite consensus NLSs, a N-terminal NLS and a C-terminal NLS (35). Our study, together with previous reports, demonstrated that the NLSs of IRFs are generally ...
We have characterized the nuclear localization signal (NLS) of XRCC1 structurally using X-ray crystallography and functionally using fluorescence imaging. Crystallography and binding studies confirm the bipartite nature of the XRCC1 NLS interaction with Importin α (Impα) in which the major and minor binding motifs are separated by ,20 residues, and resolve previous inconsistent determinations. Binding studies of peptides corresponding to the bipartite NLS, as well as its major and minor binding motifs, to both wild-type and mutated forms of Impα reveal pronounced cooperative binding behavior that is generated by the proximity effect of the tethered major and minor motifs of the NLS. The cooperativity stems from the increased local concentration of the second motif near its cognate binding site that is a consequence of the stepwise binding behavior of the bipartite NLS. We predict that the stepwise dissociation of the NLS from Impα facilitates unloading by providing a partially complexed ...
Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus ...
Das 26S Proteasom führt die letzen Schritte des essentiellen, Ubiquitin abhängigen Proteinabbaus durch, indem es ubiquitinierte und fehlgefaltete Proteine erkennt und eliminiert. Da es in S. cerevisiae während allen Stadien der Zellteilung vornehmlich im Zellkern lokalisiert ist, ist der Importweg dieses 2,5 MDa umfassenden proteolytischen Komplexes in den Zellkern von besonderem Interesse. Das 26S Proteasom unterteilt sich in das katalytisch aktive 20S Proteasom sowie den 19S Regulatorkomplex. Für 20S Proteasomen konnten Lehmann und Mitarbeitende (2002, JMB, 317, 401) zeigen, dass Vorläuferkomplexe über den Karyopherin alpha/beta abhängigen Importweg in den Zellkern gelangen und dort zu 20S Proteasomen heranreifen. In dieser Arbeit wird gezeigt, dass die nukleäre Lokalisation der 19S Regulatorkomplexe ebenfalls von Karyopherin alpha/beta abhängt. Die Untersuchung der potentiellen klassischen Kernlokalisationssequenzen (cNLS) in den Untereinheiten des 19S Base Subkomplex ergab, dass ...
... , Authors: Maria Giubettini, Pauline van der Watt, Annalisa Verrico, Valeria de Turris, Virna Leaner, Patrizia Lavia. Published in: Atlas Genet Cytogenet Oncol Haematol.
1EE5: Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha.
Baycrest is pleased to share our Quality Improvement Plan (QIP) with our clients, family members and broader community. The QIP is a requirement under the Excellent Care For All Act, 2010 and was approved by the Baycrest Board of Directors.. This plan describes the key actions we are committed to taking to make improvements to the care and services you receive. As in previous years, these improvement priorities are rooted in our strategic goal to deliver exceptional quality of care and quality of life for our patients and residents.. Our QIP was developed with extensive feedback from clients, staff and physicians and reflects what they told us matters most to deliver safe, high quality care. Along with a review of our improvement achievements and challenges over the past year, required standards, legislation, and best practices, our QIP reflects consistent themes across our organization while at the same time, making sure these priorities reflect the specific needs of our long term care ...
Importin and nucleoplasmin complex, molecular model. Nucleoplasmin tags proteins for entry to the cell nucleus, while importin transports the protein across the nuclear membrane. - Stock Image C025/1566
is a type of protein that moves other protein molecules into the nucleus by binding to a specific recognition sequence, called the nuclear localization signal (NLS). Importin is classified as a karyopherin.…
Yanxiao Gong, Shengli Zhang, Ping Xu, Zhenda Xie and Shining Zhu. Realization of a hybrid squeeze operator via a single chi(2) nonlinear photonic crystal and its applications in quantum information ...
4BA3: Crystal Structure of Rice Importin-Alpha and Structural Basis of its Interaction with Plant-Specific Nuclear Localization Signals.
Buy our Human KPNA4 peptide. Ab23144 is a blocking peptide for ab6039 and has been validated in BL. Abcam provides free protocols, tips and expert support for…
Buy our Recombinant Human KPNA2 protein. Ab123205 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE. Abcam provides free…
The B2 and B3 elements constitute an extended bipartite NLS sufficient for nuclear import of a heterologous protein. NIH 3T3 cells were transfected with the PK
beta Karyopherins: Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.
Definition of karyopherins in the Definitions.net dictionary. Meaning of karyopherins. What does karyopherins mean? Information and translations of karyopherins in the most comprehensive dictionary definitions resource on the web.
IMB1_HUMAN] Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal ...
Predicted to have nuclear import signal receptor activity and nuclear localization sequence binding activity. Involved in negative regulation of muscle cell differentiation and protein import into nucleus. Predicted to localize to the cytoplasm and nucleus. Orthologous to human TNPO2 (transportin 2 ...
The Genetics Society of America (GSA), founded in 1931, is the professional membership organization for scientific researchers and educators in the field of genetics. Our members work to advance knowledge in the basic mechanisms of inheritance, from the molecular to the population level.. Online ISSN: 1943-2631. ...
Hand Therapy Group has been recognised for the quality and safety of their service with the award of accreditation by Quality Innovation Performance (QIP) at our Macquarie, Pacific and Hills Norwest practices. QIP is Australias most comprehensive not-for-profit accreditation organisation, dedicated to delivering accreditation and support services to a diverse…. ...
Video: Senior author Dr. Michael Fainzilber and lead author Rotem Ben-Tov Perry describe the new Neuron study in a video abstract.. Finding this evidence was far from simple: Importins are so crucial in the cells nucleus that even the smallest embryo could not survive without them. But Rotem Ben-Tov Perry, a research student at the Weizmann Institute who was lead author of the new study, found a way to distinguish the importin beta1 in the cell body from that in the axon: The axonal protein was apparently made from a longer version of messenger RNA, the cells working recipe for building a protein. To see if they could selectively affect just the axonal version of the protein, the Weizmann researchers worked with Drexels Twiss to take advantage of high precision knock-out technology. Rather than knocking a whole gene out of the system, they managed to remove one little piece of the messenger RNAs recipe for manufacturing importins- just the longer bit that sends the RNA to the axon.. Now they ...
I am looking for NLS for lac-Z gene. I believe the NLS is now available commercially, but I have looked up some common suppliers with no success. I would appreciate if anyone can help me out with this. Or if knows of any source where I can get hold of NLS-LacZ plasmid. Thanks Obaid Khan ...
313175.1 Except import which takes way too long. I took a full export of WE8ISO8859p1 Database and now importing it in AL32UTF8. It is always difficult to prove where the slowness is coming from; but I think it has to do something with NLS_LENGTH_SEMANTICS. On the same server; if new database was in WE8ISO8859P1, a 5 million row table import took 2 hours; but in Al32UTF8 with NLS_LENGTH_SEMANTICS it is taking 1 day!!! Any idea how to improve the performance of import. ...
This is the primary hub for reporting Import Errors on our companion site. Please note that IMPORTS ARE A WORK IN PROGRESS. We are only accepting specif... Tokotna Import Information Error Reports
Correct targeting of nuclear proteins is mediated by nuclear localization sequences (NLS) which permit specific binding to the nucleus and subsequent translocation across the nuclear envelope via the nuclear pore complex. It is proposed that nuclear import is facilitated by NLS-receptors which reside in the cytoplasm and at the nuclear pore. These NLS-receptors could facilitate an early step of nuclear protein import, i.e. targeting and binding of nuclear proteins at the nuclear pore. We have generated anti-idiotype antibodies against the SV40 T-antigen nuclear localization sequence that allowed us to study NLS-binding proteins in a variety of different organisms. Proteins of similar size are recognized by these antibodies in yeast, Drosophila, rat and human cells. Cytological analysis indicates that the NLS-binding proteins reside in part at nuclear pores. One of the proteins recognized by anti-idiotype antibodies is identical to a previously identified NLS-binding protein. Using isolated yeast ...
Several lines of evidence presented in this paper indicate that Vpr plays a critical role in the regulation of HIV‐1 nuclear import. First, inactivating mutations in the vpr gene resulted in a greatly diminished nuclear translocation of the HIV‐1 PIC in our in vitro system. Secondly, added‐back recombinant Vpr rescued nuclear import of a Vpr‐defective HIV‐1 and stimulated import of an artificial weak karyophile. Thirdly, Vpr associated with karyopherin α, and this binding increased the affinity of interaction between karyopherin α and NLS‐containing proteins. Our data suggest that Vpr regulates the nuclear import of HIV‐1 PIC by binding to karyopherin α and increasing its affinity for viral NLSs, including the NLS of MA. This binding interaction may allow the PIC to compete efficiently for karyopherin α/β heterodimers in the cytosol and thus may facilitate docking and movement of the PIC across the NPC. Without Vpr, the nuclear import of such complexes is greatly impaired ...
This entry represents the N-terminal domain of importin-beta (also known as karyopherins-beta) that is important for the binding of the Ran GTPase protein [(PUBMED:10367892)].. Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins [(PUBMED:12372823), (PUBMED:17161424)], which is important for importin-beta mediated transport.. Ran GTPase helps to control the unidirectional transfer of cargo. The cytoplasm contains primarily RanGDP and the nucleus RanGTP through the actions of RanGAP and RanGEF, ...
In a comparison of the nuclear import of model small and large protein cargos by the importin α/β and transportin pathways, we have made the striking observation that the large cargos require both Ran and hydrolyzable GTP for nuclear import. This contrasts with the import requirements for small cargos that were observed previously and also that were noted in this study: Transportin-mediated import requires neither Ran nor GTP (Englmeier et al., 1999; Ribbeck et al., 1999; Fig. 1), and importin α/β-mediated import requires Ran and a GTP analogue but not GTP hydrolysis (Schwoebel et al., 1998; Fig. 1). We determined that RanGTP is required for the large cargos to traverse the central channel of the NPC, but is not required for association with the cytoplasmic side of the NPC. Furthermore, our data indicate that RanGTP acts to promote large cargo import by directly binding to importin β and transportin, at least in part. These findings are most easily explained by a model in which RanGTP ...
CTMI (2004) 285: Springer-Verlag 2004 Nuclear Import in Viral Infections U. F. Greber 1 ()) M. Fornerod 2 1 Zoologisches Institut der Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland
SPE Part: 8B-S016-RCH Strata® Screen-C (55 µm, 70 Å), 300 mg / 6 mL, Tubes , 30/Pk Phase: Mixed Mode C8 and SCX Sorbent Type: Silica-based Format: Tube Target Analytes: Basic drugs from biological matrices
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
Type:Other Operation System:Other Place of Origin:Guangdong, China (Mainland) Brand Name:TQ Model Number:TQ-518D 8d iris-nls Category: iris-nls 8d iris-nls Type:Biochemical Analysis System 8d iris-nls Co...
IMPORT TUNER (UK) i Tidningsarkivet. Ett digitalt arkiv för svenska tidningar och tidskrifter. Här finns bland annat omslag och innehållstexter för IMPORT TUNER (UK).
One of Italys most popular cuts, penne rigate has a wider tube than the original penne (quills), but rigate (with ridges) on the outside.
Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran
Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:10811608). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling (PubMed:16222336). Interacts with regulatory proteins of cell cycle progression including CDKN1B (PubMed:10891500, PubMed:10811608). This interaction is required for correct intracellular transport and degradation of CDKN1B (PubMed:10811608).
Riverside Health Care is putting patients first by improving the quality and accountability of the services we provide through compliance with the Excellent Care for All Act, which came into effect in June 2010. The intention of the act is to improve the quality and value of the patient experience through the application of evidence-based health care. Quality improvement is an ongoing priority that helps Riverside Health Care continually find new and improved ways of doing things so that we can enhance care for clients/residents/patients, increase satisfaction and achieve even better clinical outcomes.. Our Quality Improvement Plan or QIP is one tool that we are using to help us document and review our current performance in a variety of areas. With this plan, we will be able to very clearly see our targeted areas for improvement and chart our progress.. Documentation. ...
Combining with a nuclear export signal (NES) to mediate transport of the NES-containing protein through the nuclear pore to the cytoplasm.
1. A compound according to the general formula Ia or Ib: ##STR00368## wherein in each R1 means H, C1-C6 alkyl, cycloalkyl, or C1-C4 alkylcycloalkyl, R2 means H, C1-C14 alkyl, C2-C14 alkenyl, aryl, C1-C4 alkylaryl, heteroaryl, C1-C4 alkylheteroaryl, C2-C4 alkenylheteroaryl, cycloalkyl, C1-C4 alkylcycloalkyl, heterocycloalkyl, C1-C4 alkylheterocycloalkyl, CmH2m+o-pYp(with m=1 to 6, for o=1, p=1, to 2m+o; for m=2 to 6, o=-1, p=1 to 2m+o; for m=4 to 6, o=-2, p=1 to 2m+o; Y=independently selected from the group consisting of halogen, OH, OR21, NH2, NHR21, NR21R22, and SH, SR21), (CH2)rCH2NHCOR21, (CH2)rCH2OCOR21, (CH2)rCH2NHCSR21, (CH2)rCH2S(O)nR21, with n=0, 1, 2, (CH2)rCH2SCOR21, (CH2)rCH2OSO2--R21, (CH2)rCHO, (CH2)rCH═NOH, (CH2)rCH(OH)R21, --(CH2)rCH═NOR21, (CH2)rCH═NOCOR21, (CH2)rCH═NOCH2CONR21R22, (CH2)rCH═NOCH(CH3)CONR21R22, (CH2)rCH═NOC(CH3)2CONR21R22, (CH2)rCH═N--NHCO--R23, (CH2)rCH═N--NHC(O)NH--R23, (CH2)rCH═N--NHC(S)NH--R23, (CH2)rCH═N--NHC(NH)NH--R23, ...
DI-fusion, le Dépôt institutionnel numérique de lULB, est loutil de référencementde la production scientifique de lULB.Linterface de recherche DI-fusion permet de consulter les publications des chercheurs de lULB et les thèses qui y ont été défendues.
Free import and export records for East End Ny Import Inc.. Discover trends and information about East End Ny Import Inc. from U.S. bill of lading records in 2012 and 2014
obtain the fitted object fm1 ,- nls(demand ~ SSasympOrig(Time, A, lrc), data = BOD) # get the profile for the fitted model: default level is too extreme pr1 ,- profile(fm1, alpha = 0.05) # profiled values for the two parameters pr1$A pr1$lrc # see also example(plot.profile.nls ...
Hair follicle cycling is an exquisitely regulated and dynamic process consisting of phases of growth, regression and quiescence. The transitions between the phases are governed by a growing number of regulatory proteins, including transcription factors. The hairless (hr) gene encodes a putative transcription factor that is highly expressed in the skin, where it appears to be an essential regulator during the regression of the catagen hair follicle. In hairless mice, as well as humans with congenital atrichia, the absence of hr gene function initiates a premature and abnormal catagen due to a dysregulation of apoptosis and cell adhesion, and defects in the signaling required for hair follicle remodeling. Here, we report structure-function studies of the hairless gene product, in which we identify a novel bipartite nuclear localization signal (NLS) of the form KRA(X13) PKR. Deletion analysis of the mouse hr gene mapped the NLS to amino acid residues 409-427. Indirect immunofluorescence microscopy ...
Transportin-1 (or Importin-β 2) is a protein that in humans is encoded by the TNPO1 gene. This protein is a karyopherin which interacts with nuclear localization sequence to target nuclear proteins to the nucleus. The classical karyopherin receptor complex, such as the complex that uses Importin-β1 (encoded by gene KPNB1), is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a beta subunit which docks the complex at nucleoporins. However, Transportin-1 can directly bind to the cargo proteins and may not need importin alpha subunit to do it. Transportin-1 is thought to use the same principal mechanism to carry out nuclear transport as other Importins. It mediates docking to the nuclear pore complex through binding to nucleoporin and is subsequently translocated through the pore by an energy requiring mechanism. Then, in the nucleus Ran binds to Transportin-1, it dissociates from cargo, and Transportin-1 is re-exported from the nucleus to the cytoplasm where ...
Shop Nuclear transport factor ELISA Kit, Recombinant Protein and Nuclear transport factor Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
PTEN levels are under tight control to balance growth restriction and survival. The Ub system has emerged as the prime regulator of PTEN levels, which need to be rapidly lowered upon insults that threaten cell survival, like ischemia or wounding (Naguib and Trotman, 2013). In spite of a wealth of data that link loss of PTEN protein to tumorigenesis, it has remained unclear which genetic alterations could indirectly and efficiently suppress PTEN (Leslie and Foti, 2011). Our results introduce the IPO11 nuclear import receptor as the Achilles heel of the checks and balances in the PTEN ubiquitination system (Fig. 4 E). Tissues, which rely on strong nuclear PTEN import, like lung, could be especially vulnerable to IPO11 failure. On top of maintaining PTEN levels, IPO11 could be equally important in supporting nuclear-specific PTEN functions that were previously reported (Song et al., 2012) or remain to be discovered. It is not clear at present how ubiquitinated PTEN interacts with Importin-11. The ...
G-protein-coupled receptors are usually located at the plasma membrane from where they trigger their intracellular signaling cascade. However, CysLT1R has a bipartite nuclear localization sequence that also enables it to be located at the nuclear membrane ( 39). Despite the lack of a nuclear localization sequence domain in CysLT2R, we made the novel finding that CysLT2R is also expressed at the nuclear membrane. This conclusion is based on findings from both microscopic analyses and analyses of nuclei preparations by Western blot. Indeed, CysLT2R seems to be even more concentrated at the nuclear membrane than CysLT1R, and in contrast to CysLT1R, agonist stimulation leads to an increased accumulation of CysLT2R at the plasma membrane. Although lacking a nuclear localization sequence domain, CysLT2R does possess an IFN regulatory factor 7 (IRF7) site. The presence of this site could indicate that CysLT2R is a downstream target for IFNα and possibly also an interacting partner to IRF7. If there is ...
Many pathways activate NF‐κB by transducing signals to a core activation module consisting of the IKK complex, IκB, ubiquitylation machinery, proteasome, rel homo‐ or heterodimer and nuclear import factors. Pathway‐specific molecules function in the link between stimulus recognition and IKK complex activation in an interplay that must elicit an appropriate response to the stimulus, in part through the coordinate regulation of other transcription factor systems. In an effort to better understand the disparate mechanisms for NF‐κB activation, we have explored an expression cloning approach with the hope of finding new players, new mechanistic insights and, potentially, new pathways. To probe components used for lymphocyte signaling to NF‐κB, we screened a mouse thymus expression library and cloned the murine CARD11 cDNA.. Our data indicate that CARD11 functions in the activation of NF‐κB by TCR ligation and CD28 co‐stimulation. Expression of a CARD‐deleted CARD11 in Jurkat T ...
Type:Biochemical Analysis System Brand Name:TQ Model Number:TQ-518D Place of Origin:Guangdong, China (Mainland) Function:Detecting Body Health Warranty:One Year Certificate:CE OS:Win xp,Win 7,Win 8... C...
Imports of (bop) - Basic Chemicals and Industrial in Canada increased to 2133.80 CAD Million in January from 2090.80 CAD Million in December of 2016. Imports of (bop) - Basic Chemicals and Industrial in Canada averaged 1155.24 CAD Million from 1988 until 2017, reaching an all time high of 2447 CAD Million in October of 2013 and a record low of 362.50 CAD Million in July of 1988. This page includes a chart with historical data for Canada Imports of (bop) - Basic Chemicals And Industrial.
Feed Import is a module that allows you to import content into entities from various file types (like XML, HTML, CSV). In this page we will find how to import taxonomy terms.
import getopt import sys import csv from itertools import izip_longest from itertools import izip from memoized import memoized # sudo easy_install mpmath import mpmath #mpmath.mp.dps = 20 # decimal digits of precision @memoized def mpmathcdf(g,df,dps=10): mpmath.mp.dps = dps x,k = mpmath.mpf(g), mpmath.mpf(df) cdf = mpmath.gammainc(k/2, 0, x/2, regularized=True) # floating point precision insufficient, use more precision if cdf == 1.0: if dps > 4000: return cdf # give up after a certain point else: cdf = mpmathcdf(g,df,dps*2) return cdf def GtoP(g,df): assert g >= 0, g return float(1-mpmathcdf(g,df)) import math @memoized def flnf(f): return f*math.log(f) if f>0.5 else 0 @memoized def gtest(a,b,c,d): row1 = a+b row2 = c+d col1 = a+c col2 = b+d total = flnf(a+b+c+d) celltotals = flnf(a)+flnf(b)+flnf(c)+flnf(d) rowtotals = flnf(row1)+flnf(row2) coltotals = flnf(col1)+flnf(col2) # abs is necessary to account for float precision errors when doing the subtraction return abs(2*((celltotals + ...
Tozando Online Shopping is a premier Budo equipment supplier. Tozando carries all items of Kendo, Iaito, Japanese Swords, Iaido, Aikido, Kyudo and many others for all your needs.
Information and assistance for import, cargo and shipping sectors. Cargo Online Lodgement System (COLS). Biosecurity Import Conditions (BICON) database.
usr/bin/env python import numpy import scipy from scipy import optimize wt_CD = scipy.array([-46.396, -46.43 , -46.082, -46.159, -46.169, -45.949, -45.896, -45.78 , -45.7 , -45.434, -45.19 , -45.084, -44.374, -43.963, -43.265, -42.12 , -40.694, -38.897, -36.468, -33.651, -30.485, -26.564, -23.369, -21.652, -20.149, -18.564, -17.223, -15.661, -14.473, -13.155, -12.688, -11.335, -11.297, -10.525, -10.013, -9.199, -8.816, -8.388, -8.499, -7.707, -7.329, -7.355, -6.688, -6.782, -6.789, -6.37 , -5.944, -5.817, -5.719, -5.545, -5.651, -5.692, -4.971, -5.184]) wt_m0 = scipy.array([ 0. , 0.3, 0.6, 0.9, 1.2, 1.5, 1.8, 2. , 2.2, 2.4, 2.6, 2.8, 3. , 3.2, 3.4, 3.6, 3.8, 4. , 4.2, 4.4, 4.6, 4.8, 5. , 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6. , 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7. , 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8. , 8.1]) def denmeltfit(CDsignal, m0): import numpy import scipy from scipy import optimize # define equation for denaturant melt fit # m0 = denaturant ...
According to Economy Watch, the island nation of Japan imports commodities primarily, with the largest import being that of petroleum. Japan is known as a processing nation, importing raw materials...
Former military president General Ibrahim Babangida has said the prevailing security challenges require the collective efforts of all Nigerians.
To the best of our knowledge, this is the first study in which the relationships between expression of KPNA2 and the most clinically relevant features of UTUCs were evaluated. We demonstrated that KPNA2 was significantly upregulated in UTUC specimens. Moreover, high nuclear KPNA2 immunoreactivity was identified as a novel predictor of bladder recurrence and poor DFS and OS of UTUC patients after RNU, and its predictive ability was independent of the conventional predictive factors such as sex, tumor location, tumor size, and tumor multiplicity. Additionally, KPNA2 knockdown resulted in decreased cell proliferation and migration and increased apoptosis in urothelial carcinoma cells.. The karyopherins are an evolutionarily conserved family of transport factors that mediate the nucleocytoplasmic transport of large complexes (,40 kDa) [23]. The karyopherin family comprises both importins (import factors) and exportins (export factors). To date, approximately 22 importin β proteins and 6 importin α ...
Human papillomaviruses (HPVs) are small DNA tumor viruses that replicate and assemble exclusively inthe nucleus. Thus their proteins, including E6, must carry nuclear localization signals (NLSs) to enter the nucleus.To analyze and to predict the nuclear localization signals and several post translational modifications bybioinformatics analysis, we obtained 91 E6 protein sequences from available databases. To investigate thelocalization of these sequences, we used Hum-Ploc software. Homology and alignment of sequences wereperformed by Blast software and Multalin server respectively. Prediction of N-glycosylation and serine, threonineand tyrosine phosphorylation sites of HPV E6 protein sequences was accomplished with NetNGlyc and NetPhossoftware. Out of 91 types, the NLSs of 29 types were predicted by signal-3L and signal-CF software. We tried topredict the NLSs of remaining HPV E6 proteins according to the homology of the already predicted NLSs.However, because of considerable variation between E6
Exposure of mammalian cells to agents that induce apoptosis results in a rapid and substantial inhibition of protein synthesis. In MCF-7 breast cancer cells, tumor necrosis factor alpha (TNFalpha) and TNF-related apoptosis-inducing ligand inhibit overall translation by a mechanism that requires caspase (but not necessarily caspase-3) activity. This inhibition is associated with the increased phosphorylation of eukaryotic initiation factor (eIF2) alpha, increased association of eIF4E with the inhibitory eIF4E-binding protein (4E-BP1), and specific cleavages of eIF4B and eIF2alpha. All of these changes require caspase activity. The cleavage of eIF4GI, which specifically needs caspase-3 activity, is dispensable for the inhibition of translation in MCF-7 cells. Similar experiments with embryonic fibroblasts from control mice and animals defective for expression of the double-stranded RNA-regulated protein kinase (PKR) reveal requirements for both caspase activity and PKR for inhibition of protein ...
BACKGROUND: We examined the association of dialysis facility characteristics with payment reductions and change in clinical performance measures during the first year of the United States Centers for Medicare & Medicaid Services (CMS) End Stage Renal Disease Quality Incentive Plan (ESRD QIP) to determine its potential impact on quality and disparities in dialysis care. METHODS: We linked the 2012 ESRD QIP Facility Performance File to the 2007-2011 American Community Survey by zip code and dichotomized the QIP total performance scores-derived from percent of patients with urea reduction rate , 65, hemoglobin , 10 g/dL, and hemoglobin , 12 g/dL-as any versus no payment reduction ...
Paciorkowski AR, Weisenberg J, Kelley JB, Spencer A, Tuttle E, Ghoneim D, Thio LL, Christian SL, Dobyns WB, Paschal BM; European Journal of Human Genetics 22(5) pp 589-593
Long-lasting activity-dependent changes in synaptic efficacy require new transcription and thus involve the transport of signals from synapse to nucleus. While electrochemical signaling allows neurons to rapidly communicate between compartments, soluble signaling molecules have also been shown to translocate from synapse to nucleus to trigger changes in gene expression (Otis et al., 2006; Cohen and Greenberg, 2008). We, and others, have described a role for importin nuclear transporters in relaying signals from distal processes to the nucleus (Hanz et al., 2003; Thompson et al., 2004; Dieterich et al., 2008; Lai et al., 2008; Jordan and Kreutz, 2009). In this study, we present data showing that importin α binds to a bipartite NLS in the NR1-1a subunit of the NMDA receptor. Our findings are consistent with this interaction serving to tether importin α at the PSD in an activity-dependent manner. Specifically, our results suggest that NMDA receptor stimulation activates PKC, which phosphorylates ...
Meiotic silencing by unpaired DNA is an RNAi-mediated pathway that functions to silence unpaired genes during the sexual phase of Neurospora crassa. The presence of a gene insertion or deletion causes an unpairing event during the homolog pairing stage. My dissertations aim was to further characterize this new RNAi pathway. First, I was involved in adapting the in vivo protein interaction technique Bimolecular Fluorescence Complementation (BiFC) to N. crassa to investigate SAD-1/SAD-2 interaction. SAD-1 and SAD-2 interact in the perinuclear region, suggesting that SAD-2 functions to bring SAD-1 to its proper location. Next, I was involved in identifying components of quelling that also function in meiotic silencing. dcl-1 and qip were found to be important for sexual development and meiotic silencing. DCL-1 and QIP also localize in the perinuclear region, implicating these genes in meiotic silencing. Finally, I tested the mating type locus for immunity to meiotic silencing. Unpaired reporter ...
Ordered staples for version 3 origami design edited by Castro. The templated had now been decreased to the smaller 7202 template strand. Will be leaving for Puerto Rico while waiting for staples to come in, will be back on the 23rd. Corresponded with Dr. James Adair at PennU and Dr. Robert Bob Lee of OSU pharma. Literature Review: In general, some better indications that the origami can be functionalized with cationic peptides to facilitate transport across the nuclear pore complex. Roseneckers lab synthesized a tetramer of the PKKKRKV NLSV404 peptide sequnece spaced by glycine residues. (may want to consider finding a lab that has a Applied Biosystems Automatic Synthesizer) [4]. A strong paper, with luciferase transfection assay, in situ flourescent hybridization to detect plasmid dna, and a nuclear import assay with labelled BSA-BODIPY to be transported by the peptide. The SV40 NLS sequence they used is the minimal sequence observed on the T-antigen of SV40 necessary. HeLa cells showed ...
Hanif Charania, RBC Royal Bank Regional Vice-president (left), and Keith Richmond, RBC Royal Bank Vice-president, Commercial Financial Services (far right), present a cheque for $20,000 to Adrienne Bakker, Royal Columbian Hospital (RCH) Foundation President and CEO, and David Worthington, RCH Foundation Board Vice-chair. RBCs generous donation will fund a Glidescope Endoscope for RCHs Emergency Department. The Glidescope provides a consistently clear view of a critically injured patients trachea (windpipe), enabling quick intubation to assist with breathing ...
View Notes - BIO 320 Lecture10slides_2009 from BIO 50160 at University of Texas. BIO320 - Lecture 10 02/19/2009 NUCLEAR TRANSPORT Optional Reading on Blackboard Science (2006) 314: 766-767 The
Quoth Leazen: , Im having some trouble understanding how __import__ works. , From the docs I read that from spam.ham import eggs results in , __import__(spam.ham, globals(), locals(), [eggs]) rendering the , later function call eggs, what ever that is, but I actually get ham! Ive just read the blurb on __import__ in section 2.1 of the Library Reference, and I dont see anything to indicate that it returns the things named in the last argument. On the contrary: When the name variable is of the form package.module, normally, the top-level package (the name up till the first dot) is returned, not the module named by name. However, when a non-empty fromlist argument is given, the module named by name is returned. The last sentence indicates that __import__(spam.ham, globals(), locals(), [eggs]) will return the module named spam.ham, as you have found. , [...] So I wonder what the last argument is for since it seams rather , useless. [...] Some implementations of __import__ might ...
package com.company.my; import java.io.IOException; import java.util.Collections; import org.eclipse.emf.common.util.URI; import org.eclipse.emf.ecore.EAttribute; import org.eclipse.emf.ecore.EClass; import org.eclipse.emf.ecore.EClassifier; import org.eclipse.emf.ecore.EPackage; import org.eclipse.emf.ecore.EReference; import org.eclipse.emf.ecore.EcoreFactory; import org.eclipse.emf.ecore.EcorePackage; import org.eclipse.emf.ecore.resource.Resource; import org.eclipse.emf.ecore.resource.ResourceSet; import org.eclipse.emf.ecore.resource.impl.ResourceSetImpl; import org.eclipse.emf.ecore.xmi.impl.EcoreResourceFactoryImpl; public class MyEMFGenerator { public void generate(final String pathToDDLEcore, final String pathToOutputFile) throws IOException { // it is very important that we do everything through ResourceSets ResourceSet resourceSet = new ResourceSetImpl(); Resource ddlResource = createAndLoadDDLResource(resourceSet, pathToDDLEcore); // of course, in production code we would fail here ...
package com.company.my; import java.io.IOException; import java.util.Collections; import org.eclipse.emf.common.util.URI; import org.eclipse.emf.ecore.EAttribute; import org.eclipse.emf.ecore.EClass; import org.eclipse.emf.ecore.EClassifier; import org.eclipse.emf.ecore.EPackage; import org.eclipse.emf.ecore.EReference; import org.eclipse.emf.ecore.EcoreFactory; import org.eclipse.emf.ecore.EcorePackage; import org.eclipse.emf.ecore.resource.Resource; import org.eclipse.emf.ecore.resource.ResourceSet; import org.eclipse.emf.ecore.resource.impl.ResourceSetImpl; import org.eclipse.emf.ecore.xmi.impl.EcoreResourceFactoryImpl; public class MyEMFGenerator { public void generate(final String pathToDDLEcore, final String pathToOutputFile) throws IOException { // it is very important that we do everything through ResourceSets ResourceSet resourceSet = new ResourceSetImpl(); Resource ddlResource = createAndLoadDDLResource(resourceSet, pathToDDLEcore); // of course, in production code we would fail here ...
Jonathan Baughs research seeks to develop physical devices that will enable quantum information processing (QIP). His experimental program focuses on electron and nuclear spin qubits, especially their realization in semiconductor nanostructures, and the development of quantum control techniques.
STAFF REPORT ISB: The imports of mobile phones into Pakistan remained up by 6.15 per cent to $282.87 million during first five months (July-Nov) of fiscal year 2014-15 as compared to the imports of $266.47 million during the same period of last year. The data of Pakistan Bureau of Statistics (PBS) shows that on month basis the mobile phone imports during the month of November 2014 also increased by 19.17 per cent and decreased by 0.54pc when compared to the imports in November 2013 and…Read More. ...
Imports of Chemicals in Japan decreased to 562956 JPY Million in February from 626202.34 JPY Million in January of 2017. Imports of Chemicals in Japan averaged 305680.08 JPY Million from 1983 until 2017, reaching an all time high of 728733.83 JPY Million in July of 2015 and a record low of 120548.40 JPY Million in August of 1986. This page includes a chart with historical data for Japan Imports of Chemicals.
Imports of Feeding Stuff For Animals in Australia decreased to 64 AUD Million in June from 87 AUD Million in May of 2016. Imports of Feeding Stuff For...
China wants to import more to solve its trade imbalances instead of parking windfall revenues in U.S. and euro zone government bonds, the chairman of Chinas largest lender said on Thursday.
Endometrial cancer is the most frequently occurring malignancy of the female genital tract in Western countries. Although in many cases surgically curable, about 30% of the tumours represent an aggressive and untreatable disease. In an attempt to establish a reliable prognostic marker for endometrial carcinomas disregarding their histological diversity, we investigated the expression of KPNA2, a mediator of nucleocytoplasmic transport, and other cell proliferation-associated proteins and their correlation with cancer progression. We analysed patient tissue microarrays (TMAs) assembled from 527 endometrial cancer tissue specimens and uterus samples from a Trp53 knockout mouse model of endometrial cancer. Our data show that KPNA2 expression was significantly up-regulated in human endometrial carcinomas and associated with higher tumour grade (p = 0.026), higher FIGO stage (p = 0.027), p53 overexpression (p , 0.001), activation of the PI3K/AKT pathway, and epithelial-mesenchymal transition. ...
Transport of macromolecules into and out of the nucleus is generally effected by targeting signals that are recognized by specific members of the importin/exportin transport receptor family. The latter mediate passage through the nuclear envelope-embedded nuclear pore complexes (NPCs) by conferring interaction with NPC constituents, as well as with other components of the nuclear transport machinery, including the guanine nucleotide-binding protein Ran. Importantly, nuclear transport is regulated at multiple levels via a diverse range of mechanisms, such as the modulation of the accessibility and affinity of target signal recognition by importins/exportins, with phosphorylation/dephosphorylation as a major mechanism. Alteration of the level of the expression of components of the nuclear transport machinery also appears to be a key determinant of transport efficiency, having central importance in development, differentiation and transformation ...
In this study, we used multiple functional assays to characterize NXT1, a protein that we identified based on its sequence relatedness to NTF2. The similarities of NXT1 and NTF2 include their amino acid identity (26% within a species), low molecular sizes (NTF2, 127 amino acids; NXT1, 140 amino acids), acidic isoelectric points (NTF2, 5.1; NXT1, 5.0), steady-state nuclear localization (45), interaction with the NPC (6, 31, 36), and direct binding to Ran (31, 34). However, NXT1 and NTF2 also have distinct properties that provide insights into their respective functions. NTF2 binds to Ran-GDP and mediates its import into the nucleus (38, 43,45), thereby functioning as a nuclear import factor. In contrast, NXT1 binds to Ran-GTP. The precise function of this interaction is unknown, but it clearly suggests a role in nuclear export. Indeed, using a permeabilized cell assay (16), we have shown here that NXT1 stimulates nuclear export of PKI. The logical interpretation of this result is that NXT1 ...

beta Karyopherins
      - Importin-beta
     Summary Report | CureHunterbeta Karyopherins - Importin-beta Summary Report | CureHunter

Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. ... Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules ... Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN ... GTP-BINDING PROTEIN causes release of karyopherin beta. ... formation by tethering karyopherin alpha 2 and karyopherin beta ...
more infohttp://www.curehunter.com/public/keywordSummaryD028961-beta-Karyopherins-Importin-beta.do

Karyopherin alpha 1 - WikipediaKaryopherin alpha 1 - Wikipedia

"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... Importin subunit alpha-1 is a protein that in humans is encoded by the KPNA1 gene. Karyopherin alpha 1 has been shown to ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Percipalle, P; Clarkson W D; Kent H M; Rhodes D; Stewart M (Mar 1997). "Molecular interactions between the importin alpha/beta ...
more infohttps://en.wikipedia.org/wiki/Karyopherin_alpha_1

Karyopherin alpha 2 - WikipediaKaryopherin alpha 2 - Wikipedia

"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "Entrez Gene: KPNA2 karyopherin alpha 2 (RAG cohort 1, importin alpha 1)". Lin CY, Huang PH, Liao WL, Cheng HJ, Huang CF, Kuo JC ... KPNA2 also may play a role in V(D)J recombination Karyopherin alpha 2 has been shown to interact with: ARL4A ITK, KPNB1, PLAG1 ... Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML (May 2002). "Identification of a karyopherin alpha 2 ...
more infohttps://en.wikipedia.org/wiki/Karyopherin_alpha_2

RCSB PDB 









- 1BK6: KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS Methods Report PageRCSB PDB - 1BK6: KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS Methods Report Page

Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. ...
more infohttp://www.rcsb.org/pdb/explore/materialsAndMethods.do?structureId=1BK6

WikiGenes - KPNA4 - karyopherin alpha 4 (importin alpha 3)WikiGenes - KPNA4 - karyopherin alpha 4 (importin alpha 3)

Synonyms: IPOA3, Importin alpha Q1, Importin subunit alpha-3, Karyopherin subunit alpha-4, MGC12217, ... ... Assignment of KPNA4 and KPNB1 encoding karyopherin alpha 4 and beta 1 to human chromosome bands 11q22 and 17q21 respectively, ... Assignment of KPNA4 and KPNB1 encoding karyopherin alpha 4 and beta 1 to human chromosome bands 11q22 and 17q21 respectively, ... Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination of Qip1 and Rch1 from hSrp1 by their ability ...
more infohttps://www.wikigenes.org/e/gene/e/3840.html

3D View 









- 1BK6: KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS 3D View Report Page3D View - 1BK6: KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS 3D View Report Page

Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. ...
more infohttp://www.rcsb.org/pdb/explore/jmol.do?structureId=1BK6&bionumber=1

Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5 -...Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5 -...

Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5 ... Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5 X. ...
more infohttps://pubs.rsc.org/en/Content/ArticleLanding/OB/2017/C7OB00012J

Targeting Nuclear Import Shuttles, Importins/Karyopherins Alpha by a Peptide Mimicking the NFκB1/p50 Nuclear Localization...Targeting Nuclear Import Shuttles, Importins/Karyopherins Alpha by a Peptide Mimicking the NFκB1/p50 Nuclear Localization...

... with endogenous human importins/karyopherins to determine the mechanism of NTM modulation of importin alpha-mediated nuclear ... Targeting Nuclear Import Shuttles, Importins/Karyopherins Alpha by a Peptide Mimicking the NFκB1/p50 Nuclear Localization ... with endogenous human importins/karyopherins to determine the mechanism of NTM modulation of importin alpha-mediated nuclear ...
more infohttps://www.moleculardevices.com/resources/publications/targeting-nuclear-import-shuttles-importins-karyopherins-alpha-by-a-peptide-mimicking-the-nuclear-localization-sequence

Die nukleäre Expression von Karyopherin alpha 2: ein prädiktiver Faktor für das Überleben von Patientinnen mit...Die nukleäre Expression von Karyopherin alpha 2: ein prädiktiver Faktor für das Überleben von Patientinnen mit...

Meiler, Robert Paul (2010) Die nukleäre Expression von Karyopherin alpha 2: ein prädiktiver Faktor für das Überleben von ... Die nukleäre Expression von Karyopherin alpha 2: ein prädiktiver Faktor für das Überleben von Patientinnen mit ... Karyopherin a2 (KPNA2) has been reported as a important factor of tumorgenesis and progression of breast cancer. The aim of ... Karyopherin α2 (KPNA2) stellte sich als ein wichtiger Faktor bezüglich Tumorentstehung und Fortschreiten des Mammakarzinoms dar ...
more infohttps://epub.uni-regensburg.de/17823/

LOC365232 (similar to karyopherin (importin) alpha 4) - Rat Genome DatabaseLOC365232 (similar to karyopherin (importin) alpha 4) - Rat Genome Database

similar to karyopherin (importin) alpha 4 LOC365232 similar to karyopherin (importin) alpha 4 (predicted) predicted is ... similar to karyopherin (importin) alpha 4 (predicted) Symbol and Name status set to provisional. 70820. PROVISIONAL. ...
more infohttps://rgd.mcw.edu/rgdweb/report/gene/main.html?id=1583798

Structure Cluster 









- 1EE5: YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A NUCLEOPLASMIN NLS PEPTIDE 3D...Structure Cluster - 1EE5: YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A NUCLEOPLASMIN NLS PEPTIDE 3D...

Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin ... Description: KARYOPHERIN ALPHA protein , Length: 424 No structure alignment results are available for 1EE5.A explicitly.. It is ... YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A NUCLEOPLASMIN NLS PEPTIDE. ...
more infohttps://www.rcsb.org/pdb/explore/structureCluster.do?structureId=1EE5

Karyopherin alpha 2 is a novel prognostic marker and a potential therapeutic target for colon cancer | Journal of Experimental ...Karyopherin alpha 2 is a novel prognostic marker and a potential therapeutic target for colon cancer | Journal of Experimental ...

... a member of the karyopherin family, plays a vital role in carcinogenesis. Yet its role in colon cancer is poorly characterized ... Karyopherin alpha 2 (KPNA2), a member of the karyopherin family, plays a vital role in carcinogenesis. Yet its role in colon ... Karyopherin alpha 2 is a novel prognostic marker and a potential therapeutic target for colon cancer. *Yu Zhang1. , ... Hu ZY, Yuan SX, Yang Y, Zhou WP, Jiang H. Pleomorphic adenoma gene 1 mediates the role of karyopherin alpha 2 and has ...
more infohttps://jeccr.biomedcentral.com/articles/10.1186/s13046-015-0261-3

Pleomorphic adenoma gene 1 mediates the role of karyopherin alpha 2 and has prognostic significance in hepatocellular carcinoma...Pleomorphic adenoma gene 1 mediates the role of karyopherin alpha 2 and has prognostic significance in hepatocellular carcinoma...

Karyopherin alpha 2 (KPNA2) promotes tumor growth in hepatocellular carcinoma (HCC). We aimed to determine the content and ... Karyopherin alpha 2 (KPNA2) is one of karyopherin a family, and could form heterodimer with Karyopherin 1 to promote nucleus ... Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML: Identification of a karyopherin alpha 2 recognition site in ... Karyopherin alpha 2 (KPNA2) promotes tumor growth in hepatocellular carcinoma (HCC). We aimed to determine the content and ...
more infohttps://jeccr.biomedcentral.com/articles/10.1186/s13046-014-0061-1

KPNA6 Gene - GeneCards | IMA7 Protein | IMA7 AntibodyKPNA6 Gene - GeneCards | IMA7 Protein | IMA7 Antibody

Karyopherin Subunit Alpha 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... KPNA6 (Karyopherin Subunit Alpha 6) is a Protein Coding gene. Diseases associated with KPNA6 include Lennox-Gastaut Syndrome. ... Acetylation of importin-alpha nuclear import factors by CBP/p300. (PMID: 10801418) Bannister AJ … Kouzarides T (Current biology ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=KPNA6&keywords=GH01G033035&prefilter=genomic_location

US7101995B2 - Compositions and processes using siRNA, amphipathic compounds and polycations 
        - Google PatentsUS7101995B2 - Compositions and processes using siRNA, amphipathic compounds and polycations - Google Patents

108010077099 alpha Karyopherins Proteins 0 description 2 * 102000009899 alpha Karyopherins Human genes 0 description 2 ...
more infohttps://patents.google.com/patent/US7101995B2/en

Karyopherins: potential biological elements involved in the delayed graft function in renal transplant recipients | BMC Medical...Karyopherins: potential biological elements involved in the delayed graft function in renal transplant recipients | BMC Medical...

Signal transducers and activators of transcription (STAT) utilize karyopherins-alpha (KPNA) for their passage from cytoplasm ... of karyopherin-mediated nuclear transport in the onset and development of DGF. Additionally, it reveals that karyopherins could ... which includes genes encoding for several subtypes of karyopherins, a group of proteins involved in nucleocytoplasmic transport ... Karyopherin-alpha (also known as importin-alpha) is an adaptor protein that recognizes the first discovered or classical NLS, ...
more infohttps://bmcmedgenomics.biomedcentral.com/articles/10.1186/1755-8794-7-14

Structure Gallery | Max Planck Institute of BiochemistryStructure Gallery | Max Planck Institute of Biochemistry

Karyopherin Alpha from Saccharomyces Cerevisiae bound to NLS. Conti E et al. Cell. 1998 ...
more infohttps://www.biochem.mpg.de/conti/structures

Nucleus-specific importin alpha proteins and nucleoporins regulate protein import and nuclear division in the binucleate...Nucleus-specific importin alpha proteins and nucleoporins regulate protein import and nuclear division in the binucleate...

thermophila encodes a large, karyopherin alpha-like protein family. The diagram in panel A depicts the conserved domains of ... Localization studies of 13 putative importin (imp) alpha- and 11 imp beta-like proteins revealed that imp alpha-like proteins ... These data suggest that micronucleus-specific proteins are transported by specific imp alpha adapters. The different imp alpha ... Nucleus-specific importin alpha proteins and nucleoporins regulate protein import and nuclear division in the binucleate ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed?term=18676955

KPNA2 - Importin subunit alpha-1 - Homo sapiens (Human) - KPNA2 gene & proteinKPNA2 - Importin subunit alpha-1 - Homo sapiens (Human) - KPNA2 gene & protein

At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta ... "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ...
more infohttps://www.uniprot.org/uniprot/P52292

AAGCCAT MIR135A MIR135BAAGCCAT MIR135A MIR135B

karyopherin alpha 3 (importi.... Kua. LCP1. 3936. LCP1. lymphocyte cytosolic protein.... LDLRAD2. 401944. LDLRAD2. low density ...
more infohttp://software.broadinstitute.org/gsea/msigdb/cards/AAGCCAT_MIR135A_MIR135B.html

Integrated mutation, copy number and expression profiling in resectable non-small cell lung cancer | BMC Cancer | Full TextIntegrated mutation, copy number and expression profiling in resectable non-small cell lung cancer | BMC Cancer | Full Text

Barbieri C, Barton C, Pietenpol J: Delta Np63 alpha expression is regulated by the phosphoinositide 3-kinase pathway. The ... Karyopherin alpha 5 (importin alpha 6). 6q22.2. -0.66. 8.7 E-3 LMO4 ...
more infohttps://bmccancer.biomedcentral.com/articles/10.1186/1471-2407-11-93

SCHLOSSER MYC TARGETS REPRESSED BY SERUMSCHLOSSER MYC TARGETS REPRESSED BY SERUM

karyopherin alpha 2 (RAG cohort.... 40417_at. 22948. CCT5. chaperonin containing TCP1, sub.... ...
more infohttp://software.broadinstitute.org/gsea/msigdb/cards/SCHLOSSER_MYC_TARGETS_REPRESSED_BY_SERUM.html

Anti-KPNA5 antibody (ab125529) | AbcamAnti-KPNA5 antibody (ab125529) | Abcam

Karyopherin alpha 5 importin alpha 6 antibody. *Karyopherin subunit alpha 5 antibody ... At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta ... Belongs to the importin alpha family.. Contains 10 ARM repeats.. Contains 1 IBB domain. ...
more infohttp://www.abcam.com/kpna5-antibody-ab125529.html

anti-SRP1 antibody, N-term  | GeneTexanti-SRP1 antibody, N-term | GeneTex

... importin alpha 5)) for WB. Anti-SRP1 pAb (GTX26035) is tested in Human samples. 100% Ab-Assurance. ... importin-alpha-S1, karyopherin alpha 1 (importin alpha 5), NPI-1, IPOA5, karyopherin alpha1 (importin alpha5), NPI 1, importin ... karyopherin alpha 1, importin alpha 5, importin alpha5, KPNA1 / Importin alpha5, karyopherin alpha1, recombination activating ... karyopherin alpha 1 (importin alpha 5). Background. Recombination activating proteins RAG1 and RAG2 regulate and mediate V(D)J ...
more infohttp://www.genetex.com/KPNA1-Importin-alpha-5-antibody-N-term-GTX26035.html
  • The different imp alpha proteins exhibit substantial sequence divergence and do not appear to be simply redundant in function. (nih.gov)
  • Disruption of the IMA10 gene encoding an imp alpha-like protein that accumulates in dividing micronuclei results in nuclear division defects and lethality. (nih.gov)
  • Additionally, it reveals that karyopherins could be good candidates as potential DGF predictive clinical biomarkers and targets for pharmacological interventions in renal transplantation. (biomedcentral.com)