Results 81 to 90 of about 29,175 (219)

Ibetazol, a novel inhibitor of importin β1-mediated nuclear import

open access: yesCommunications Biology
Nucleocytoplasmatic transport plays an essential role in eukaryotic cell homeostasis and is mediated by karyopherins. Importin β1 (KPNB1) and its adaptor protein importin α1 (KPNA2) are the best-characterized karyopherins that effect nuclear import. Here,
Thomas Vercruysse   +11 more
doaj   +1 more source

KPNB1 (karyopherin (importin) beta 1) [PDF]

open access: yesAtlas of Genetics and Cytogenetics in Oncology and Haematology, 2013
Review on KPNB1 (karyopherin (importin) beta 1), with data on DNA, on the protein encoded, and where the gene is implicated.
Maria Giubettini   +5 more
openaire   +3 more sources

Holistic bone developing microenvironment engineered apoptotic extracellular vesicles recapitulate multidimensional developmental signatures in adult and senile bone repair

open access: yesInterdisciplinary Medicine, EarlyView.
The developing bone was identified as an M2a‐like macrophage driven immune microenvironment with multidimensional developmental signatures. hME‐ApoEVs were successfully fabricated via stimulating the M2a‐like developing microenvironment in vitro and confirmed its recapitulation of developmental features.
Xiaoran Yu   +11 more
wiley   +1 more source

C9orf72 arginine-rich dipeptide repeat proteins disrupt karyopherin-mediated nuclear import

open access: yeseLife, 2020
Disruption of nucleocytoplasmic transport is increasingly implicated in the pathogenesis of neurodegenerative diseases, including ALS caused by a C9orf72 hexanucleotide repeat expansion. However, the mechanism(s) remain unclear.
Lindsey R Hayes   +4 more
doaj   +1 more source

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry [PDF]

open access: yes, 2012
Protein phosphorylation is a common post-translational modification in eukaryotic cells and has a wide range of functional effects. Here, we used mass spectrometry to search for phosphorylated residues in all the proteins of influenza A and B viruses ...
Denham, Eleanor M.   +8 more
core   +3 more sources

Missense Variants in the A Isoform of FGF13 as a Novel Cause of Paroxysmal Dyskinesia

open access: yesMovement Disorders, EarlyView.
Abstract Background Pathogenic variants within the unique N‐terminal inactivation particle of FGF13 isoform A (FGF13A) have so far been associated only with an X‐linked dominant epileptic encephalopathy (DEE). Objective The aim was to expand the clinical and molecular spectrum of FGF13A‐related disorder.
Cyril Mignot   +22 more
wiley   +1 more source

Thioredoxin-related transmembrane protein 2 (TMX2) regulates the Ran protein gradient and importin-β-dependent nuclear cargo transport

open access: yesScientific Reports, 2019
TMX2 is a thioredoxin family protein, but its functions have not been clarified. To elucidate the function of TMX2, we explored TMX2-interacting proteins by LC-MS. As a result, importin-β, Ran GTPase (Ran), RanGAP, and RanBP2 were identified.
Ami Oguro, Susumu Imaoka
doaj   +1 more source

Sweet silver: A formaldehyde-free silver staining using aldoses as developing agents, with enhanced compatibility with mass spectrometry [PDF]

open access: yes, 2008
Protein detection methods after electrophoresis have to be sensitive, homogeneous, and not to impair downstream analysis of proteins by MS. Speed, low cost, and user friendliness are also favored features. Silver staining combines many of these features,
Berggren   +26 more
core   +4 more sources

Importins/Karyopherins Meet Nucleoporins [PDF]

open access: yesCell, 1996
I thank Gunter Blobel, Valerie Doye, Dirk Gorlich, Iain Mattaj, Ulf Nehrbass, and Uli Scheer for helpful comments on the manuscript.
openaire   +1 more source

The Importin β Binding Domain Modulates the Avidity of Importin β for the Nuclear Pore Complex [PDF]

open access: yesJournal of Biological Chemistry, 2010
Importin beta mediates active passage of cellular substrates through the nuclear pore complex (NPC). Adaptors such as importin alpha and snurportin associate with importin beta via an importin beta binding (IBB) domain. The intrinsic structural flexibility of importin beta allows its concerted interactions with IBB domains, phenylalanine-glycine ...
Kaylen, Lott   +4 more
openaire   +2 more sources

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