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Search results 901 to 1000 out of 1369 for Vip

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Hits by Strain

Type Details Score
Allele
Tg(Vip-EGFP)JN37Gsat | MGI:4847532
Name: transgene insertion JN37, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
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Allele
Tg(Vip-cre)PH13Gsat | MGI:5086166
Name: transgene insertion PH13, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Recombinase
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Allele
Vip<em1(icre)Smoc> | MGI:7293133
Name: vasoactive intestinal polypeptide; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Recombinase
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GXD Expression
GXD Expression
 
Probe: MGI:6159093
Assay Type: Immunohistochemistry
Annotation Date: 2018-07-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:2692226
Pattern: Not Specified
Stage: TS26
Assay Id: MGI:6164710
Age: embryonic day 18.5
Note: Co-expression analysis was done with neurotransmitters and neuropeptides: TH, NPY, and 5-HT (in the stomach) and CGRP, Calb1, Nos1 and VIP (in the small intestine). Co-expression was seen with Th, NPY, 5-HT and VIP and partial co-expression was seen with CGRP, Calb1 and Nos1.
Specimen Label: Table 3A
Detected: true
Specimen Num: 3
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GXD Expression
GXD Expression
 
Probe: MGI:6159067
Assay Type: Immunohistochemistry
Annotation Date: 2018-07-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:2692226
Pattern: Not Specified
Stage: TS26
Assay Id: MGI:6164682
Age: embryonic day 18.5
Note: Co-expression analysis was done with neurotransmitters and neuropeptides: TH, NPY, and 5-HT (in the stomach) and CGRP, Calb1, Nos1 and VIP (in the small intestine). Partial co-expression was seen with with CGRP, 5-HT, and VIP and no co-expression with the rest.
Specimen Label: Table 3B
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
 
Probe: MGI:6159101
Assay Type: Immunohistochemistry
Annotation Date: 2018-07-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:2692226
Pattern: Not Specified
Stage: TS26
Assay Id: MGI:6164708
Age: embryonic day 18.5
Note: Co-expression analysis was done with neurotransmitters and neuropeptides: TH, NPY, and 5-HT (in the stomach) and CGRP, Calb1, Nos1 and VIP (in the small intestine). Co expression was seen with Th, CGRP, 5-HT and VIP, partial co-expression with Calb1 and Nos1, and no co-expression with NPY.
Specimen Label: Table 3B
Detected: true
Specimen Num: 1
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GO Term
GO:0044519 | envenomation resulting in modulation of vasoactive intestinal polypeptide receptor activity in another organism
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Strain
MGI:5004062 | STOCK Tg(Vip-EGFP)JN37Gsat/Mmucd
Attribute String: mutant stock, transgenic
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Publication
21060720 | J:264877
 
First Author: Chamberland S
Year: 2010
Journal: Front Cell Neurosci
Title: Synapse-specific inhibitory control of hippocampal feedback inhibitory circuit.
Volume: 4
Pages: 130
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Publication
27679813 | J:268882
 
First Author: Guet-McCreight A
Year: 2016
Journal: eNeuro
Title: Using a Semi-Automated Strategy to Develop Multi-Compartment Models That Predict Biophysical Properties of Interneuron-Specific 3 (IS3) Cells in Hippocampus.
Volume: 3
Issue: 4
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Publication
34819310 | J:351800
 
First Author: Wyeth M
Year: 2021
Journal: eNeuro
Title: Lack of Hyperinhibition of Oriens Lacunosum-Moleculare Cells by Vasoactive Intestinal Peptide-Expressing Cells in a Model of Temporal Lobe Epilepsy.
Volume: 8
Issue: 6
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Strain
MGI:5493413 | STOCK Tg(Vip-cre)PH13Gsat/Mmucd
Attribute String: mutant stock, transgenic
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Allele
Vip<tm1.1(cre)Pful> | MGI:6718935
Name: vasoactive intestinal polypeptide; targeted mutation 1.1, Patrick M Fuller
Allele Type: Targeted
Attribute String: Recombinase
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Strain
MGI:6429782 | C57BL/6JSmoc-Vip<em1(icre)Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Publication
8784257 | J:36171
First Author: Delgado M
Year: 1996
Journal: J Neuroimmunol
Title: Differential expression of vasoactive intestinal peptide receptors 1 and 2 (VIP-R1 and VIP-R2) mRNA in murine lymphocytes.
Volume: 68
Issue: 1-2
Pages: 27-38
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HT Experiment
GSE145362 | Dlx1/2 mutant and wild type FACS-sorted ENCDCs at P0 and E14.5
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Vip-cre)PH13Gsat/?
Background: involves: 129S4/SvJaeSor * FVB/N
Zygosity: cn
Has Mutant Allele: true
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Publication
24671999 | J:210454
First Author: Tyan L
Year: 2014
Journal: J Neurosci
Title: Dendritic inhibition provided by interneuron-specific cells controls the firing rate and timing of the hippocampal feedback inhibitory circuitry.
Volume: 34
Issue: 13
Pages: 4534-47
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Vip/Vip<+>
Background: Not Specified
Zygosity: cn
Has Mutant Allele: true
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Publication
8542309 | J:109913
First Author: Laemle LK
Year: 1995
Journal: Brain Res
Title: Diurnal variations in vasoactive intestinal polypeptide-like immunoreactivity in the suprachiasmatic nucleus of congenitally anophthalmic mice.
Volume: 688
Issue: 1-2
Pages: 203-8
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Publication
14983060 | J:88640
First Author: Watkins CC
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: Carbon monoxide mediates vasoactive intestinal polypeptide-associated nonadrenergic/noncholinergic neurotransmission.
Volume: 101
Issue: 8
Pages: 2631-5
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Publication
29444424 | J:268845
First Author: Priya R
Year: 2018
Journal: Cell Rep
Title: Activity Regulates Cell Death within Cortical Interneurons through a Calcineurin-Dependent Mechanism.
Volume: 22
Issue: 7
Pages: 1695-1709
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Publication
12086606 | J:97146
First Author: Harmar AJ
Year: 2002
Journal: Cell
Title: The VPAC(2) receptor is essential for circadian function in the mouse suprachiasmatic nuclei.
Volume: 109
Issue: 4
Pages: 497-508
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Publication
8933357 | -
First Author: Wei Y
Year: 1996
Journal: J Neuroendocrinol
Title: Tissue specific expression of different human receptor types for pituitary adenylate cyclase activating polypeptide and vasoactive intestinal polypeptide: implications for their role in human physiology.
Volume: 8
Issue: 11
Pages: 811-7
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Publication
8392197 | -
First Author: Pisegna JR
Year: 1993
Journal: Proc Natl Acad Sci U S A
Title: Molecular cloning and functional expression of the pituitary adenylate cyclase-activating polypeptide type I receptor.
Volume: 90
Issue: 13
Pages: 6345-9
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Protein Domain
IPR002284 | GPCR_2_VIP_rcpt_2
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 secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. Vasoactive intestinal polypeptide (VIP) has a wide physiological profile.In the periphery, it induces relaxation in smooth muscle; inhibitssecretion in certain tissues, but stimulates secretion in others; andmodulates activity of cells in the immune system. In the CNS, it has arange of both excitatory and inhibitory actions. VIP receptors aredistributed widely in the periphery, and occur throughout the gastrointestinal tract and genitourinary system, other smooth muscles andsecretory glands. In the CNS, they are found abundantly in, e.g. the cortex,hippocampus and thalamus. All VIP receptors activate adenylyl cyclase.There are two structurally distinct receptors that recognise VIP peptidesand pituitary adenylate cyclase activating polypeptide (PACAP) with similaraffinities (PACAP/VIPR-1, PACAP/VIPR-2), as well as a specific receptor forthe PACAP peptide (PACAP-1). RNA transcripts for all three receptor typesare found in human heart, brain and adipose tissue []. VIPR-1 isconstitutively expressed, while the expression of VIPR-2 is induced onlyfollowing stimulation through the TCR-associated CD3 complex []. VIPinduces the expression of the VIPR-2 gene in the absence of additionalstimuli. Differential expression and regulation of the two VIP receptorsin T lymphocytes suggests different physiological roles in mediating theimmunomodulatory activities of VIP and related neuropeptides []. PACAP type I receptors arepresent in the hypothalamus and anterior pituitary, where they regulate therelease of adrenocorticotropin, luteinising hormone, growth hormone andprolactin, and in the adrenal medulla, where they regulate the release ofepinephrine []. The receptors are also found in high concentrations intesticular germ cells, where they may regulate spermatogenesis, and in sometransformed cell lines, such as the rat pancreatic acinar carcinoma cellAR4-2J [].This entry represents VIPR-2.
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Protein Domain
IPR001571 | GPCR_2_VIP_rcpt
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 evolutionaryrelationship, 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 secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. Vasoactive intestinal polypeptide (VIP) has a wide physiological profile.In the periphery, it induces relaxation in smooth muscle; inhibitssecretion in certain tissues, but stimulates secretion in others; andmodulates activity of cells in the immune system. In the CNS, it has arange of both excitatory and inhibitory actions. VIP receptors aredistributed widely in the periphery, and occur throughout the gastrointestinal tract and genitourinary system, other smooth muscles andsecretory glands. In the CNS, they are found abundantly in, e.g. the cortex,hippocampus and thalamus. All VIP receptors activate adenylyl cyclase.There are two structurally distinct receptors that recognise VIP peptidesand pituitary adenylate cyclase activating polypeptide (PACAP) with similaraffinities (PACAP/VIPR-1, PACAP/VIPR-2), as well as a specific receptor forthe PACAP peptide (PACAP-1). RNA transcripts for all three receptor typesare found in human heart, brain and adipose tissue []. VIPR-1 isconstitutively expressed, while the expression of VIPR-2 is induced onlyfollowing stimulation through the TCR-associated CD3 complex []. VIPinduces the expression of the VIPR-2 gene in the absence of additionalstimuli. Differential expression and regulation of the two VIP receptorsin T lymphocytes suggests different physiological roles in mediating theimmunomodulatory activities of VIP and related neuropeptides []. PACAPtype I receptors arepresent in the hypothalamus and anterior pituitary, where they regulate therelease of adrenocorticotropin, luteinising hormone, growth hormone andprolactin, and in the adrenal medulla, where they regulate the release ofepinephrine []. The receptors are also found in high concentrations intesticular germ cells, where they may regulate spermatogenesis, and in sometransformed cell lines, such as the rat pancreatic acinar carcinoma cellAR4-2J [].
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Protein Domain
IPR002285 | GPCR_2_PACAP_1_rcpt
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 secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. Vasoactive intestinal polypeptide (VIP) has a wide physiological profile.In the periphery, it induces relaxation in smooth muscle; inhibitssecretion in certain tissues, but stimulates secretion in others; andmodulates activity of cells in the immune system. In the CNS, it has arange of both excitatory and inhibitory actions. VIP receptors aredistributed widely in the periphery, and occur throughout the gastrointestinal tract and genitourinary system, other smooth muscles andsecretory glands. In the CNS, they are found abundantly in, e.g. the cortex,hippocampus and thalamus. All VIP receptors activate adenylyl cyclase.There are two structurally distinct receptors that recognise VIP peptidesand pituitary adenylate cyclase activating polypeptide (PACAP) with similaraffinities (PACAP/VIPR-1, PACAP/VIPR-2), as well as a specific receptor forthe PACAP peptide (PACAP-1). RNA transcripts for all three receptor typesare found in human heart, brain and adipose tissue []. VIPR-1 isconstitutively expressed, while the expression of VIPR-2 is induced onlyfollowing stimulation through the TCR-associated CD3 complex []. VIPinduces the expression of the VIPR-2 gene in the absence of additionalstimuli. Differential expression and regulation of the two VIP receptorsin T lymphocytes suggests different physiological roles in mediating theimmunomodulatory activities of VIP and related neuropeptides []. PACAP type I receptors arepresent in the hypothalamus and anterior pituitary, where they regulate therelease of adrenocorticotropin, luteinising hormone, growth hormone andprolactin, and in the adrenal medulla, where they regulate the release ofepinephrine []. The receptors are also found in high concentrations intesticular germ cells, where they may regulate spermatogenesis, and in sometransformed cell lines, such as the rat pancreatic acinar carcinoma cellAR4-2J [].This entry represents the PACAP-1 receptor.
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Protein Domain
IPR001771 | GPCR_2_VIP_rcpt_1
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 secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. Vasoactive intestinal polypeptide (VIP) has a wide physiological profile.In the periphery, it induces relaxation in smooth muscle; inhibitssecretion in certain tissues, but stimulates secretion in others; andmodulates activity of cells in the immune system. In the CNS, it has arange of both excitatory and inhibitory actions. VIP receptors aredistributed widely in the periphery, and occur throughout the gastrointestinal tract and genitourinary system, other smooth muscles andsecretory glands. In the CNS, they are found abundantly in, e.g. the cortex,hippocampus and thalamus. All VIP receptors activate adenylyl cyclase.There are two structurally distinct receptors that recognise VIP peptidesand pituitary adenylate cyclase activating polypeptide (PACAP) with similaraffinities (PACAP/VIPR-1, PACAP/VIPR-2), as well as a specific receptor forthe PACAP peptide (PACAP-1). RNA transcripts for all three receptor typesare found in human heart, brain and adipose tissue []. VIPR-1 isconstitutively expressed, while the expression of VIPR-2 is induced onlyfollowing stimulation through the TCR-associated CD3 complex []. VIPinduces the expression of the VIPR-2 gene in the absence of additionalstimuli. Differential expression and regulation of the two VIP receptorsin T lymphocytes suggests different physiological roles in mediating theimmunomodulatory activities of VIP and related neuropeptides []. PACAP type I receptors arepresent in the hypothalamus and anterior pituitary, where they regulate therelease of adrenocorticotropin, luteinising hormone, growth hormone andprolactin, and in the adrenal medulla, where they regulate the release ofepinephrine []. The receptors are also found in high concentrations intesticular germ cells, where they may regulate spermatogenesis, and in sometransformed cell lines, such as the rat pancreatic acinar carcinoma cellAR4-2J [].This entry represents VIPR-1.
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Protein
Q3UQJ8
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
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Publication
8784267 | J:36172
First Author: Johnson MC
Year: 1996
Journal: J Neuroimmunol
Title: Murine T-lymphocytes express vasoactive intestinal peptide receptor 1 (VIP-R1) mRNA.
Volume: 68
Issue: 1-2
Pages: 109-19
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Publication
12665475 | J:82662
First Author: Bangale Y
Year: 2003
Journal: FASEB J
Title: VIPase autoantibodies in Fas-defective mice and patients with autoimmune disease.
Volume: 17
Issue: 6
Pages: 628-35
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Publication
11602234 | J:110087
First Author: Laemle LK
Year: 2001
Journal: Brain Res
Title: The relationship between circadian rhythmicity and vasoactive intestinal polypeptide in the suprachiasmatic nucleus of congenitally anophthalmic mice.
Volume: 917
Issue: 1
Pages: 105-11
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Publication
26119026 | J:227431
First Author: Talbot S
Year: 2015
Journal: Neuron
Title: Silencing Nociceptor Neurons Reduces Allergic Airway Inflammation.
Volume: 87
Issue: 2
Pages: 341-54
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Publication
23972597 | J:201752
First Author: Cao R
Year: 2013
Journal: Neuron
Title: Translational control of entrainment and synchrony of the suprachiasmatic circadian clock by mTOR/4E-BP1 signaling.
Volume: 79
Issue: 4
Pages: 712-24
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Publication
30710088 | J:273789
First Author: Hamnett R
Year: 2019
Journal: Nat Commun
Title: Vasoactive intestinal peptide controls the suprachiasmatic circadian clock network via ERK1/2 and DUSP4 signalling.
Volume: 10
Issue: 1
Pages: 542
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Publication
38630591 | J:349799
First Author: Bhandari K
Year: 2024
Journal: Cell Rep
Title: Selective vulnerability of the ventral hippocampus-prelimbic cortex axis parvalbumin interneuron network underlies learning deficits of fragile X mice.
Volume: 43
Issue: 5
Pages: 114124
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Publication
37549024 | J:353422
 
First Author: Shao F
Year: 2023
Journal: J Exp Med
Title: FOXO1 orchestrates the intestinal homeostasis via neuronal signaling in group 3 innate lymphoid cells.
Volume: 220
Issue: 10
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Publication
29557780 | J:264187
   
First Author: Niquille M
Year: 2018
Journal: Elife
Title: Neurogliaform cortical interneurons derive from cells in the preoptic area.
Volume: 7
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Publication
24411939 | J:210546
First Author: Yulyaningsih E
Year: 2014
Journal: Cell Metab
Title: Pancreatic polypeptide controls energy homeostasis via Npy6r signaling in the suprachiasmatic nucleus in mice.
Volume: 19
Issue: 1
Pages: 58-72
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Publication
11262614 | J:69454
First Author: Zhang M
Year: 2000
Journal: Curr Eye Res
Title: Vasoactive intestinal peptide (VIP) exacerbates endotoxin-induced uveitis (EIU) in mice.
Volume: 21
Issue: 6
Pages: 913-7
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Publication
8224221 | J:34452
First Author: Lutz EM
Year: 1993
Journal: FEBS Lett
Title: The VIP2 receptor: molecular characterisation of a cDNA encoding a novel receptor for vasoactive intestinal peptide.
Volume: 334
Issue: 1
Pages: 3-8
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Publication
11880348 | J:75044
First Author: Duong CV
Year: 2002
Journal: Development
Title: The developmental expression of vasoactive intestinal peptide (VIP) in cholinergic sympathetic neurons depends on cytokines signaling through LIFRbeta-containing receptors.
Volume: 129
Issue: 6
Pages: 1387-96
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Publication
12502497 | J:80997
First Author: Rachdi L
Year: 2003
Journal: Diabetes
Title: Role for VPAC2 receptor-mediated signals in pancreas development.
Volume: 52
Issue: 1
Pages: 85-92
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Publication
18055217 | J:132687
First Author: Miao T
Year: 2008
Journal: Mol Cell Neurosci
Title: SOCS3 suppresses AP-1 transcriptional activity in neuroblastoma cells through inhibition of c-Jun N-terminal kinase.
Volume: 37
Issue: 2
Pages: 367-75
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Publication
24630718 | J:211998
First Author: Fu Y
Year: 2014
Journal: Cell
Title: A cortical circuit for gain control by behavioral state.
Volume: 156
Issue: 6
Pages: 1139-1152
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Publication
29128567 | J:257461
First Author: Lai B
Year: 2018
Journal: Am J Pathol
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Protein
H3BJW2
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Fragment?: true
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Protein
E9QAL0
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Fragment?: true
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23753526 | J:212781
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15862536 | J:98024
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7510877 | J:21555
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Publication
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Publication
38391908 | J:360451
 
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Publication
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