Results 121 to 130 of about 21,607 (213)
Importin-11 keeps PTEN safe from harm [PDF]
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 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]
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
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]
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
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
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]
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
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
(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

