Results 121 to 130 of about 21,607 (213)

Importin-11 keeps PTEN safe from harm [PDF]

open access: yes, 2017
In this issue, Chen et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201604025) show that Importin-11 traffics the tumor suppressor PTEN into the nucleus and in so doing protects it from cytoplasmic proteins that cause PTEN degradation.
Nick R. Leslie   +1 more
core   +1 more source

Arginine methylation as a regulatory ratchet in cancer: From substrate selection to malignant‐state stabilization

open access: yesMolecular Oncology, Volume 20, Issue 10, Page 2466-2489, October 2026.
Arginine methylation can be viewed as a persistence‐prone post‐translational modification regulated by a network of PRMTs. Competitive and compensatory interactions among PRMTs can redistribute methylation across substrate pools shaped by sequence, structural, spatial, and environmental layers, reinforcing RNA‐processing, chromatin, and signaling ...
So Hyun Kwon, Ji Min Lee
wiley   +1 more source

Importin beta regulates mitosis via distinct molecular mechanisms [PDF]

open access: yes, 2018
Importin beta is the major vector for protein import in interphase nuclei and acts as an effector of the GTPase RAN. After nuclear envelope breakdown, when nuclear transport ceases, Importin beta acts in control of mitosis. Importin beta is overexpressed
VERRICO, ANNALISA
core  

Importin beta validates human importin beta as a cell cycle negative regulator-4

open access: yes, 2011
In beta with 94% identities (828/876, black boxes) and 97% positives (857/876 gray and black boxes). The amino acid composition, along with the length of the protein, is well conserved between and human importin beta. Three of the conservative amino acid
Rene C Chan (63112)   +2 more
core   +1 more source

Export of Importin α from the Nucleus Is Mediated by a Specific Nuclear Transport Factor [PDF]

open access: yes, 1997
NLS proteins are transported into the nucleus by the importin α/β heterodimer. Importin α binds the NLS, while importin β mediates translocation through the nuclear pore complex.
Kutay, Ulrike   +11 more
core   +1 more source

Lactate metabolism and protein lactylation in programmed cell death: From novel mechanism to therapeutic strategies in human diseases

open access: yesClinical and Translational Medicine, Volume 16, Issue 10, October 2026.
This review highlights protein lactylation as a metabolic‐epigenetic regulator linking lactate reprogramming to programmed cell death. By modulating histone and non‐histone targets, lactylation reshapes cell fate decisions and represents a promising biomarker and therapeutic target in human diseases.
Yue Chen   +8 more
wiley   +1 more source

Global Proteomic Analysis of Sperm and Seminal Plasma From Tropically‐Adapted Rams With Contrasting Parameters of Frozen‐Thawed Semen

open access: yesMolecular Reproduction and Development, Volume 93, Issue 10, October 2026.
ABSTRACT The aim of this study was to characterize the proteome of sperm and seminal plasma (SP) from rams with high semen freezability (HF) and low semen freezability (LF). Eleven ejaculates were collected from 12 rams, at 3‐day intervals, and cryopreserved (132 semen samples).
Wallisson Bruno de Morais Pacheco   +14 more
wiley   +1 more source

Regulation of nuclear localization signal-importin α interaction by Ca2+/S100A6 [PDF]

open access: yes, 2010
Although the precise intracellular roles of S100 proteins are not fully understood, these proteins are thought to be involved in Ca2+-dependent diverse signal transduction pathways.
Tokuda, Masaaki   +11 more
core   +1 more source

Extensive cargo identification reveals distinct biological roles of the 12 importin pathways

open access: yeseLife, 2017
Vast numbers of proteins are transported into and out of the nuclei by approximately 20 species of importin-β family nucleocytoplasmic transport receptors.
Makoto Kimura   +5 more
semanticscholar   +1 more source

Binding of NP to importin α.

open access: yes, 2013
(A) Purification of mRFP-Flag-tagged WT and mutant NP110aas from COS-7 cells and GST-tagged importin α isoforms, Rch1, Qip1 and NPI-1 from Escherichia coli.
Yutaka Sasaki (286423)   +5 more
core   +1 more source

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