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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1997 4
1998 7
1999 6
2000 10
2001 8
2002 4
2003 10
2004 11
2005 10
2006 20
2007 15
2008 15
2009 30
2010 17
2011 19
2012 25
2013 18
2014 18
2015 23
2016 18
2017 20
2018 7
2019 2
2020 0
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281 results
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Page 1
Phosphorylation of Gli2 by protein kinase A is required for Gli2 processing and degradation and the Sonic Hedgehog-regulated mouse development.
Pan Y, et al. Dev Biol 2009. PMID 19056373 Free PMC article.
To address these questions, we mutated these PKA sites in the mouse Gli2 locus to create the Gli2(P1-4) allele. Gli2(P1-4) homozygous embryos die in utero and exhibit exencephaly, defects in neural tube closure, enlarged craniofacial structures, and an extra anterior digit. ...Furthermore, Gli2(P1-4) expression prevents massive cell death and promotes cell proliferation in Shh mutant. Analysis of Gli2(P1-4) protein in vivo reveals that the mutant protein is not processed and is twice as stable as wild type Gli2 protein. ...
To address these questions, we mutated these PKA sites in the mouse Gli2 locus to create the Gli2(P1-4) allele. Gli2
Gli2 protein expression level is a feasible marker of ligand-dependent hedgehog activation in pancreatic neoplasms.
Sugiyama Y, et al. Pol J Pathol 2016. PMID 27543868 Free article.
GLI2 protein is also expressed in both PanIN/IPMN and PDA. Although there was no difference in the nuclear staining, the cytoplasmic GLI2 level in PDA was modest in comparison to that in PanIN/IPMN. ...The results indicate that the GLI2 protein level could serve as a feasible marker of ligand-dependent hedgehog activation in pancreatic neoplasms....
GLI2 protein is also expressed in both PanIN/IPMN and PDA. Although there was no difference in the nuclear staining, the cytop
Pharmacological GLI2 inhibition prevents myofibroblast cell-cycle progression and reduces kidney fibrosis.
Kramann R, et al. J Clin Invest 2015. PMID 26193634 Free PMC article.
Pharmacologic targeting of this pathway with darinaparsin, an arsenical in clinical trials, reduced fibrosis through reduction of GLI2 protein levels and subsequent cell-cycle arrest in myofibroblasts. GLI2 overexpression rescued the cell-cycle effect of darinaparsin in vitro. While darinaparsin ameliorated fibrosis in WT and Gli1-KO mice, it was not effective in conditional Gli2-KO mice, supporting GLI2 as a direct darinaparsin target. ...
Pharmacologic targeting of this pathway with darinaparsin, an arsenical in clinical trials, reduced fibrosis through reduction of GLI2
Enpp1 inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling
Jin Y, et al. Development 2018. PMID 30111653 Free PMC article.
Recently, the ecto-enzyme Enpp1, a suppressor of pathological calcification, was reported to be decreased in joint cartilage with OA in both human and mouse, and Enpp1 deficiency causes joint calcification. ...Further activation of Hh signaling by removing the patched 1 gene in the Enpp1(-/-) mice enhanced ectopic joint calcification, whereas removing Gli2 partially rescued the ectopic calcification phenotype. ...
Recently, the ecto-enzyme Enpp1, a suppressor of pathological calcification, was reported to be decreased in joint cartilage with OA in both …
lncRNA directs cooperative epigenetic regulation downstream of chemokine signals
Xing Z, et al. Cell 2014. PMID 25416949 Free PMC article.
This mechanism activates a noncanonical Hedgehog/GLI2 transcriptional program that promotes cell migration. BCAR4 expression correlates with advanced breast cancers, and therapeutic delivery of locked nucleic acids (LNAs) targeting BCAR4 strongly suppresses breast cancer metastasis in mouse models. The findings reveal a disease-relevant lncRNA mechanism consisting of both direct coordinated protein recruitment and indirect regulation of transcription factors....
This mechanism activates a noncanonical Hedgehog/GLI2 transcriptional program that promotes cell migration. BCAR4 expression correlat …
Dual Regulatory Functions of SUFU and Targetome of GLI2 in SHH Subgroup Medulloblastoma.
Yin WC, et al. Dev Cell 2019. PMID 30554998 Free article.
Here, we report that loss of Sufu alone is unable to induce MB formation in mice, due to insufficient Gli2 activation. Simultaneous loss of Spop, an E3 ubiquitin ligase targeting Gli2, restores robust Gli2 activation and induces rapid MB formation in Sufu knockout background. ...Having established Gli2 activation as a key driver of SHH MB, we report a comprehensive analysis of its targetome. Furthermore, we identified Atoh1 as a target and molecular accomplice of Gli2 that activates core SHH MB signature genes in a synergistic manner. ...
Here, we report that loss of Sufu alone is unable to induce MB formation in mice, due to insufficient Gli2 activation. Simultaneous l …
Stromal Gli2 activity coordinates a niche signaling program for mammary epithelial stem cells.
Zhao C, et al. Science 2017. PMID 28280246
We find that Gli2, the major Hedgehog pathway transcriptional effector, acts within mouse mammary stromal cells to direct a hormone-responsive niche signaling program by activating expression of factors that regulate epithelial stem cells as well as receptors for the mammatrophic hormones estrogen and growth hormone. ...
We find that Gli2, the major Hedgehog pathway transcriptional effector, acts within mouse mammary stromal cells to direct a ho …
A novel protein-processing domain in Gli2 and Gli3 differentially blocks complete protein degradation by the proteasome.
Pan Y and Wang B. J Biol Chem 2007. PMID 17283082 Free article.
The repressor forms of Gli2 and Gli3 transcription factors are generated from their full-length proteins through limited proteasome-mediated protein degradation. ...This region, named processing determinant domain, functions as a signal for protein processing in the context of not only Gli2 and Gli3 protein sequences but also a heterologous hybrid protein, which would otherwise be completely degraded by the proteasome. ...
The repressor forms of Gli2 and Gli3 transcription factors are generated from their full-length proteins through limited proteasome-m …
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