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Search results 3001 to 3100 out of 3144 for Gli1

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Type Details Score
Publication
First Author: Kwon IK
Year: 2015
Journal: Biochim Biophys Acta
Title: Mitochondrial function contributes to oxysterol-induced osteogenic differentiation in mouse embryonic stem cells.
Volume: 1853
Issue: 3
Pages: 561-72
Publication
First Author: Xia W
Year: 2017
Journal: Cell Death Differ
Title: Histone variant H3.3 orchestrates neural stem cell differentiation in the developing brain.
Volume: 24
Issue: 9
Pages: 1548-1563
Publication  
First Author: Woods S
Year: 2019
Journal: Matrix Biol
Title: miR-324-5p is up regulated in end-stage osteoarthritis and regulates Indian Hedgehog signalling by differing mechanisms in human and mouse.
Volume: 77
Pages: 87-100
Publication  
First Author: Dobson THW
Year: 2019
Journal: Sci Signal
Title: Transcriptional repressor REST drives lineage stage-specific chromatin compaction at Ptch1 and increases AKT activation in a mouse model of medulloblastoma.
Volume: 12
Issue: 565
Publication
First Author: Chen JL
Year: 2019
Journal: Cereb Cortex
Title: Gli2 Rescues Delays in Brain Development Induced by Kif3a Dysfunction.
Volume: 29
Issue: 2
Pages: 751-764
Publication
First Author: Mazzone A
Year: 2019
Journal: FASEB J
Title: Direct repression of anoctamin 1 (ANO1) gene transcription by Gli proteins.
Volume: 33
Issue: 5
Pages: 6632-6642
Publication  
First Author: Infante P
Year: 2021
Journal: Cancer Lett
Title: Glabrescione B delivery by self-assembling micelles efficiently inhibits tumor growth in preclinical models of Hedgehog-dependent medulloblastoma.
Volume: 499
Pages: 220-231
Publication
First Author: Bauer J
Year: 2021
Journal: Oncogene
Title: Context-dependent modulation of aggressiveness of pediatric tumors by individual oncogenic RAS isoforms.
Volume: 40
Issue: 31
Pages: 4955-4966
Publication
First Author: Grachtchouk M
Year: 2021
Journal: Carcinogenesis
Title: Constitutive Hedgehog/GLI2 signaling drives extracutaneous basaloid squamous cell carcinoma development and bone remodeling.
Volume: 42
Issue: 8
Pages: 1100-1109
Publication
First Author: Brennan-Crispi DM
Year: 2015
Journal: Oncotarget
Title: Crosstalk between Desmoglein 2 and Patched 1 accelerates chemical-induced skin tumorigenesis.
Volume: 6
Issue: 11
Pages: 8593-605
Publication
First Author: Saeki N
Year: 2022
Journal: Exp Cell Res
Title: Pregnane X receptor (PXR) represses osteoblast differentiation through repression of the Hedgehog signaling pathway.
Volume: 416
Issue: 1
Pages: 113156
Publication
First Author: Sementino E
Year: 2022
Journal: Mol Cancer Res
Title: Inactivation of p21-Activated Kinase 2 (Pak2) Inhibits the Development of Nf2-Deficient Tumors by Restricting Downstream Hedgehog and Wnt Signaling.
Volume: 20
Issue: 5
Pages: 699-711
Publication  
First Author: Hu Y
Year: 2022
Journal: Front Pharmacol
Title: Gypenosides ameliorate ductular reaction and liver fibrosis via inhibition of hedgehog signaling.
Volume: 13
Pages: 1033103
Publication
First Author: Ansari-Lari MA
Year: 1998
Journal: Genome Res
Title: Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6.
Volume: 8
Issue: 1
Pages: 29-40
Publication
First Author: Gloriam DE
Year: 2005
Journal: Biochim Biophys Acta
Title: Nine new human Rhodopsin family G-protein coupled receptors: identification, sequence characterisation and evolutionary relationship.
Volume: 1722
Issue: 3
Pages: 235-46
Publication
First Author: Ansari-Lari MA
Year: 1997
Journal: Genome Res
Title: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination.
Volume: 7
Issue: 3
Pages: 268-80
Publication
First Author: Ansari-Lari MA
Year: 1996
Journal: Genome Res
Title: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13.
Volume: 6
Issue: 4
Pages: 314-26
Publication
First Author: Sreedharan S
Year: 2011
Journal: FEBS J
Title: The G protein coupled receptor Gpr153 shares common evolutionary origin with Gpr162 and is highly expressed in central regions including the thalamus, cerebellum and the arcuate nucleus.
Volume: 278
Issue: 24
Pages: 4881-94
Protein Domain
Type: Family
Description: G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].Computational methods, including percent identity plots, hydropathy profiles and BLAST, have been used to analyse a gene-rich cluster at human chromosome 12p13 and to compare it with its syntenic region in mouse chromosome 6 [, , ]. Of 6 genes identified, a number were novel receptors, including GPR153 (also known as PGR1) and GPR162 (also known as GRCA) []. GPR153 is a cerebellar target of the Gli1 transcription factor, which is involved in the maintenance and proliferation of grabule neuron precursor cells in the cerebellum, and like GPR162 has a noted role in food uptake and decision making processes [].This entry represents G-protein coupled receptor 153 and G-protein coupled receptor 162.
Protein Domain
Type: Family
Description: G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].Computational methods, including percent identity plots, hydropathy profiles and BLAST, have been used to analyse a gene-rich cluster at human chromosome 12p13 and to compare it with its syntenic region in mouse chromosome 6 [, , ]. Of 6 genes identified, a number were novel receptors, including GPR153 (also known as PGR1) and GPR162 (also known as GRCA) []. GPR153 is a cerebellar target of the Gli1 transcription factor, which is involved in the maintenance and proliferation of grabule neuron precursor cells in the cerebellum, and like GPR162 has a noted role in food uptake and decision making processes [].This entry represents G-protein coupled receptor 162.
Protein Domain
Type: Family
Description: G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].Computational methods, including percent identity plots, hydropathy profiles and BLAST, have been used to analyse a gene-rich cluster at human chromosome 12p13 and to compare it with its syntenic region in mouse chromosome 6 [, , ]. Of 6 genes identified, a number were novel receptors, including GPR153 (also known as PGR1) and GPR162 (also known as GRCA) []. GPR153 is a cerebellar target of the Gli1 transcription factor, which is involved in the maintenance and proliferation of grabule neuron precursor cells in the cerebellum, and like GPR162 has a noted role in food uptake and decision making processes [].This entry represents G-protein coupled receptor 153, identified by conserved sections along the length of the protein that characterise GP153 and distinguish itfrom closely related GP162 proteins.
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
Publication
First Author: Argenti B
Year: 2005
Journal: J Neurosci
Title: Hedgehog antagonist REN(KCTD11) regulates proliferation and apoptosis of developing granule cell progenitors.
Volume: 25
Issue: 36
Pages: 8338-46
Publication
First Author: Kalogeropoulos M
Year: 2010
Journal: FASEB J
Title: Zic1 transcription factor in bone: neural developmental protein regulates mechanotransduction in osteocytes.
Volume: 24
Issue: 8
Pages: 2893-903
Publication
First Author: Paudel S
Year: 2022
Journal: Carcinogenesis
Title: Chemopreventive efficacy of silibinin against basal cell carcinoma growth and progression in UVB-irradiated Ptch+/- mice.
Volume: 43
Issue: 6
Pages: 557-570
Publication
First Author: Zurawel RH
Year: 2000
Journal: Genes Chromosomes Cancer
Title: Evidence that haploinsufficiency of Ptch leads to medulloblastoma in mice.
Volume: 28
Issue: 1
Pages: 77-81
Publication
First Author: Eichenmüller M
Year: 2007
Journal: Int J Oncol
Title: Hedgehog-independent overexpression of transforming growth factor-beta1 in rhabdomyosarcoma of Patched1 mutant mice.
Volume: 31
Issue: 2
Pages: 405-12
Publication  
First Author: Li X
Year: 2004
Journal: BMC Dev Biol
Title: Hedgehog can drive terminal differentiation of amniote slow skeletal muscle.
Volume: 4
Pages: 9
Publication  
First Author: Hewitt SC
Year: 2020
Journal: Endocrinology
Title: Peri- and Postpubertal Estrogen Exposures of Female Mice Optimize Uterine Responses Later in Life.
Volume: 161
Issue: 8
Publication
First Author: Li X
Year: 2020
Journal: FASEB J
Title: Ciliary IFT80 is essential for intervertebral disc development and maintenance.
Volume: 34
Issue: 5
Pages: 6741-6756
Publication
First Author: Sheng H
Year: 2002
Journal: Cancer Res
Title: Dissecting the oncogenic potential of Gli2: deletion of an NH(2)-terminal fragment alters skin tumor phenotype.
Volume: 62
Issue: 18
Pages: 5308-16
Publication
First Author: Nicot A
Year: 2002
Journal: J Neurosci
Title: Pituitary adenylate cyclase-activating polypeptide and sonic hedgehog interact to control cerebellar granule precursor cell proliferation.
Volume: 22
Issue: 21
Pages: 9244-54
Publication  
First Author: Zhang J
Year: 2015
Journal: Neurobiol Dis
Title: Fingolimod treatment promotes proliferation and differentiation of oligodendrocyte progenitor cells in mice with experimental autoimmune encephalomyelitis.
Volume: 76
Pages: 57-66
Publication  
First Author: Shi X
Year: 2018
Journal: Front Immunol
Title: Sonic Hedgehog Signaling Regulates Hematopoietic Stem/Progenitor Cell Activation during the Granulopoietic Response to Systemic Bacterial Infection.
Volume: 9
Pages: 349
Protein
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
Publication
First Author: Rubin JB
Year: 2002
Journal: Cancer Cell
Title: Medulloblastoma: a problem of developmental biology.
Volume: 2
Issue: 1
Pages: 7-8
Publication
First Author: Taylor MD
Year: 2002
Journal: Nat Genet
Title: Mutations in SUFU predispose to medulloblastoma.
Volume: 31
Issue: 3
Pages: 306-10
Publication
First Author: Merchant M
Year: 2004
Journal: Mol Cell Biol
Title: Suppressor of fused regulates Gli activity through a dual binding mechanism.
Volume: 24
Issue: 19
Pages: 8627-41
Publication
First Author: Kang HS
Year: 2010
Journal: Histol Histopathol
Title: Gli-similar (Glis) Krüppel-like zinc finger proteins: insights into their physiological functions and critical roles in neonatal diabetes and cystic renal disease.
Volume: 25
Issue: 11
Pages: 1481-96
Protein
Organism: Mus musculus/domesticus
Length: 588  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 631  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 407  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 238  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 277  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 376  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 456  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 246  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 442  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: false