Results 31 to 40 of about 10,614 (241)

RAM function is dependent on Kapβ2-mediated nuclear entry [PDF]

, 2014
Eukaryotic gene expression is dependent on the modification of the first transcribed nucleotide of pre-mRNA by the addition of the 7-methylguanosine cap.
Aregger, Buratowski, Cansizoglu, Chook, Chu, Cowling, Cowling, Dormann, Fridell, Glover-Cutter, Gonatopoulos-Pournatzis, Lee, Li, Perales, Rebane, Shafer, Shatkin, Shuman, Suzuki, Süel, Thomas Gonatopoulos-Pournatzis, Topisirovic, Van Dusen, Victoria H. Cowling, Xu   +24 more
core   +4 more sources

Adjunct Duties for Karyopherins: Regulating Septin Sumoylation [PDF]

Developmental Cell, 2007
Karyopherins are shuttling transport receptors regulated by the small GTPase Ran, which move cargo between the nucleus and cytoplasm by passing through the nuclear pore complexes. A recent paper in Journal of Cell Biology (Makhnevych et al., 2007) highlights an additional role for karyopherins during mitosis, in regulating the sumoylation status of the
Panse, Vikram Govind, Hurt, Ed
openaire   +2 more sources

KPNA2 is a potential diagnostic serum biomarker for epithelial ovarian cancer and correlates with poor prognosis

Tumor Biology, 2017
This study aimed to determine whether serum karyopherin alpha 2 levels can be used as a diagnostic biomarker for epithelial ovarian carcinoma. Karyopherin alpha 2 protein was detected by enzyme-linked immunosorbent assay in serum samples from 162 ...
Long Huang, Yun Zhou, Xin-Ping Cao, Jia-Xin Lin, Lan Zhang, Shu-Ting Huang, Min Zheng   +6 more
doaj   +1 more source

Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through NUP62, inhibiting host nucleocytoplasmic transport pathways [PDF]

, 2012
The herpes simplex virus ICP27 protein is important for the expression and nuclear export of viral mRNAs. Although several binding sites have been mapped along the ICP27 sequence for various RNA and protein partners including the transport receptor TAP ...
Arnold, Aubert, Bachi, Bonifaci, Braun, Bryant, Chen, Chen, Copeland, Cullen, Darshan, Ellison, Ellison, Escudero-Paunetto, Faria, Fischer, Flach, Fontaine-Rodriguez, Fontoura, Fornerod, Fridell, Gerace, Gruffat, Grüter, Gustin, Gustin, Gustin, Han, Hardwicke, Hernandez, Hiriart, Hofemeister, Hutten, Johnson, Kambach, Koffa, Larralde, Lengyel, Lengyel, Li, Lilley, Long, Macaulay, Malik, Malik, McCarthy, Mears, Mears, Mears, Meyer, Michael, Nelson, Park, Pasdeloup, Pasquinelli, Pearson, Pellet, Petersen, Phelan, Piñol-Roma, Pollard, Pritchard, Rice, Rice, Rice, Rice, Rojas, Saavedra, Sandri-Goldin, Satterly, Schmitt, Sekulovich, Siomi, Smith, Soliman, Soliman, Souki, Strambio-De-Castillia, Strässer, Tsuji, Wagstaff, Wente, Zhi, Zhi   +83 more
core   +3 more sources

The Wolbachia cytoplasmic incompatibility enzyme CidB targets nuclear import and protamine-histone exchange factors

eLife, 2019
Intracellular Wolbachia bacteria manipulate arthropod reproduction to promote their own inheritance. The most prevalent mechanism, cytoplasmic incompatibility (CI), traces to a Wolbachia deubiquitylase, CidB, and CidA.
John Frederick Beckmann, Gagan Deep Sharma, Luis Mendez, Hongli Chen, Mark Hochstrasser   +4 more
doaj   +1 more source

Intermolecular disulfide bonds among nucleoporins regulate karyopherin-dependent nuclear transport [PDF]

Journal of Cell Science, 2013
Disulfide (S-S) bonds play important roles in the regulation of protein function and cellular stress responses. In this study, we demonstrate that distinct sets of nucleoporins (Nups), components of the nuclear pore complex (NPC), form S-S bonds and regulate nuclear transport through the NPC.
Shige H. Yoshimura, Shotaro Otsuka, Masahiro Kumeta, Mariko Taga, Kunio Takeyasu   +4 more
openalex   +4 more sources

Cloning and characterization of human karyopherin β3 [PDF]

Proceedings of the National Academy of Sciences, 1997
Nuclear import of classical nuclear localization sequence-bearing proteins is mediated by karyopherin α/β1 heterodimers. A second nuclear import pathway, mediated by karyopherin β2 (transportin), recently was described for mRNA-binding proteins. Here we report the cloning and characterization of human karyopherin β3, which may be involved in a third ...
N R, Yaseen, G, Blobel
openaire   +2 more sources

Exploring the role of mononuclear phagocytes in the epididymis

Asian Journal of Andrology, 2015
The onslaught of foreign antigens carried by spermatozoa into the epididymis, an organ that has not demonstrated immune privilege, a decade or more after the establishment of central immune tolerance presents a unique biological challenge.
Nicolas Da Silva, Tegan B Smith
doaj   +1 more source

An agent-based model for mRNA export through the nuclear pore complex. [PDF]

, 2014
mRNA export from the nucleus is an essential step in the expression of every protein- coding gene in eukaryotes, but many aspects of this process remain poorly understood.
Azimi, Mohammad, Bulat, Evgeny, Mofrad, Mohammad RK, Weis, Karsten   +3 more
core   +2 more sources

The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence. [PDF]

Proceedings of the National Academy of Sciences, 1996
By using proteolysis, recombinant mutant proteins, or synthetic peptides and by testing these reagents in liquid phase binding or nuclear import assays, we have mapped binding regions of karyopherin alpha. We found that the C-terminal region of karyopherin alpha recognizes the nuclear localization sequence (NLS), whereas its N-terminal region binds ...
J, Moroianu, G, Blobel, A, Radu
openaire   +2 more sources