Results 121 to 130 of about 441,552 (301)

Multiple SecA protein isoforms in Escherichia coli [PDF]

open access: yesJournal of Bacteriology, 1987
To define the anti-SecA-LacZ antiserum, immunoprecipitates produced with either whole anti-SecA-LacZ rabbit antiserum or affinity-purified antibodies were used to analyze nondenatured lysates of Escherichia coli. The antiserum contains antibodies that recognize different proteins.
openaire   +2 more sources

Hyperosmotic stress‐induced redistribution of pre‐mRNA cleavage factor I subunits is associated with shifts in alternative polyadenylation

open access: yesFEBS Open Bio, EarlyView.
Hyperosmotic stress triggers the relocation of the CFIm complex from the nucleus to the cytoplasm. This shift creates a nuclear ‘stoichiometric bottleneck’, limiting CFIm availability for mRNA processing. Consequently, specific mRNAs like NUDT21 and DICER1 undergo targeted 3′UTR shortening, demonstrating how spatial protein dynamics drive rapid ...
Hitomi Soumiya   +2 more
wiley   +1 more source

IsoSel: Protein Isoform Selector for phylogenetic reconstructions

open access: yesPLOS ONE, 2017
The reliability of molecular phylogenies is strongly dependent on the quality of the assembled datasets. In the case of eukaryotes, the selection of only one protein isoform per genomic locus is mandatory to avoid biases linked to redundancy. Here, we present IsoSel, a tool devoted to the selection of alternative isoforms in the context of phylogenetic
Héloïse Philippon   +3 more
openaire   +4 more sources

Effects of IGFBP4 deficiency on human preadipocyte proliferation and differentiation through the IGF1R/AKT pathway

open access: yesFEBS Open Bio, EarlyView.
IGFBP4 knockdown (KD) impairs preadipocyte proliferation and is associated with IGF1R protein downregulation and attenuated AKT phosphorylation. The mechanisms by which IGFBP4 KD influences the IGF1R/AKT signaling pathway involve newly synthesized proteins and lysosomal degradation pathways. Created in BioRender.
Yujia Guo   +6 more
wiley   +1 more source

Alterations in mRNA 3′ UTR Isoform Abundance Accompany Gene Expression Changes in Human Huntington’s Disease Brains

open access: yesCell Reports, 2017
The huntingtin gene has two mRNA isoforms that differ in their 3′ UTR length. The relationship of these isoforms with Huntington’s disease is not established.
Lindsay Romo   +3 more
doaj   +1 more source

Voltage-dependent anion channels: different isoforms for different functions

open access: yes, 2009
The Voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane (OMM) and mediates the flow of ions and metabolites between the cytoplasm and the mitochondrial network.
DE STEFANI, Diego, De Stefani, D.
core  

Differential activation of JNK1 isoforms by TRAIL receptors modulate apoptosis of colon cancer cell lines

open access: yes, 2009
Tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) induces apoptosis on binding to its receptors, death receptor 4 and 5 (DR4, DR5).
M Keane   +11 more
core   +1 more source

Regional and developmental brain expression patterns of SNAP25 splice variants [PDF]

open access: yes, 2011
SNAP25 is an essential SNARE protein for regulated exocytosis in neuronal cells. Differential splicing of the SNAP25 gene results in the expression of two transcripts, SNAP25a and SNAP25b.
Chamberlain, Luke H.   +7 more
core   +1 more source

Mutant NPM1 in Acute Myeloid Leukemia Initiation and Maintenance

open access: yesAging and Cancer, EarlyView.
NPM1 mutations drive acute myeloid leukemia by acting as neomorphic transcriptional regulators that cooperate with Menin–MLL and XPO1 to sustain HOX/MEIS1 expression and block differentiation. Targeting these mutant‐specific transcriptional dependencies provides a rational therapeutic strategy for NPM1‐mutated AML.
Yanan Jiang   +3 more
wiley   +1 more source

Characterization of isoforms of protein 4.1 present in the nucleus [PDF]

open access: yesBiochemical Journal, 1991
Although protein 4.1 was originally identified as an element of the erythrocyte membrane skeleton, its presence in most mammalian cell types is now well described. Antibodies raised against erythrocyte protein 4.1 or synthetic peptides corresponding to the spectrin-actin-binding domain of protein 4.1 react with plasma membranes and, unexpectedly ...
openaire   +2 more sources

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