Results 31 to 40 of about 333,594 (257)

Nuclear Import and Export Signals of Human Cohesins SA1/STAG1 and SA2/STAG2 Expressed in Saccharomyces cerevisiae [PDF]

open access: yes, 2012
Background: Human SA/STAG proteins, homologues of the yeast Irr1/Scc3 cohesin, are the least studied constituents of the sister chromatid cohesion complex crucial for proper chromosome segregation.
Jurek, Marta   +27 more
core   +1 more source

A conserved C-terminal domain of the Aspergillus fumigatus developmental regulator MedA is required for nuclear localization, adhesion and virulence. [PDF]

open access: yesPLoS ONE, 2012
MedA is a developmental regulator that is conserved in the genome of most filamentous fungi. In the pathogenic fungus Aspergillus fumigatus MedA regulates conidiogenesis, adherence to host cells, and pathogenicity.
Qusai Al Abdallah   +6 more
doaj   +1 more source

Nuclear transport signals control cellular localization and function of androgen receptor cofactor p44/WDR77.

open access: yesPLoS ONE, 2011
The androgen receptor (AR) cofactor p44/WDR77, which regulates expression of a set of androgen target genes, is required for differentiation of prostate epithelium.
Zhongping Gu   +3 more
doaj   +1 more source

Identification of a novel nuclear localization signal sequence in Chlamydia trachomatis-secreted hypothetical protein CT311. [PDF]

open access: yesPLoS ONE, 2013
We previously reported that Chlamydia trachomatis hypothetical protein CT311 was secreted out of chlamydial inclusion and into host cell cytosol. We now found that CT311 further entered host cell nucleus at the late stage of infection and continued to ...
Lei Lei   +3 more
doaj   +1 more source

Nuclear localization signal peptides (NLS) and their role in viral pathogenicity

open access: yesAnnals of Mechnikov's Institute, 2020
The review provides data about nuclear localization signal peptides (NLS) and their function in the cell, incl. with a viral infection process. The binding, penetration, assembly, and budding of viruses are currently being intensively studied in many ...
Tatiana Nikolaevna Nosalskaya   +2 more
doaj   +3 more sources

Specific nuclear envelope transmembrane proteins can promote the location of chromosomes to and from the nuclear periphery [PDF]

open access: yes, 2013
BACKGROUND: Different cell types have distinctive patterns of chromosome positioning in the nucleus. Although ectopic affinity-tethering of specific loci can be used to relocate chromosomes to the nuclear periphery, endogenous nuclear envelope proteins ...
Vassiliki Lazou   +23 more
core   +1 more source

Nucleolar localization of influenza A NS1: striking differences between mammalian and avian cells [PDF]

open access: yes, 2010
In mammalian cells, nucleolar localization of influenza A NS1 requires the presence of a C-terminal nucleolar localization signal. This nucleolar localization signal is present only in certain strains of influenza A viruses.
Soubies, S.M.   +18 more
core   +1 more source

Functional domains of SP110 that modulate its transcriptional regulatory function and cellular translocation

open access: yesJournal of Biomedical Science, 2018
Background SP110, an interferon-induced nuclear protein, belongs to the SP100/SP140 protein family. Very recently, we showed that SP110b, an SP110 isoform, controls host innate immunity to Mycobacterium tuberculosis infection by regulating nuclear factor-
Jia-Shiun Leu   +4 more
doaj   +1 more source

Coordinate nuclear targeting of the FANCD2 and FANCI proteins via a FANCD2 nuclear localization signal. [PDF]

open access: yesPLoS ONE, 2013
Fanconi anemia (FA) is a rare recessive disease, characterized by congenital defects, bone marrow failure, and increased cancer susceptibility. FA is caused by biallelic mutation of any one of sixteen genes.
Rebecca A Boisvert   +4 more
doaj   +1 more source

Structural Limitations of the Ad5 E1A 12S Nuclear Localization Signal [PDF]

open access: yes, 1996
The Ad5 E1A 12S gene encodes an oncoprotein with the ability to immortalize and cooperate with other viral or cellular oncoproteins to transform primary epithelial cells.
QUINLAN, MARGARET P., DOUGLAS, JANET L.
core   +1 more source

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