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Search results 20401 to 20500 out of 21064 for Camp

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Type Details Score
Publication
25148684 | J:215447
First Author: Mas C
Year: 2014
Journal: J Biol Chem
Title: Structural basis for different phosphoinositide specificities of the PX domains of sorting nexins regulating G-protein signaling.
Volume: 289
Issue: 41
Pages: 28554-68
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Protein
Q04998
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
A0A286YCS6
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
Q3U9R0
Organism: Mus musculus/domesticus
Length: 931  
Fragment?: false
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Protein
H7BX74
Organism: Mus musculus/domesticus
Length: 1544  
Fragment?: false
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Protein
H3BL62
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: true
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Protein
Q8BZJ9
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
A0A076N9U7
Organism: Mus musculus/domesticus
Length: 3309  
Fragment?: false
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Protein
A0A1L1SUG9
Organism: Mus musculus/domesticus
Length: 3309  
Fragment?: false
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Protein
A0A0G2JF64
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
A0A087WQV8
Organism: Mus musculus/domesticus
Length: 1143  
Fragment?: false
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Protein
Q8K011
Organism: Mus musculus/domesticus
Length: 627  
Fragment?: false
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Protein
A0A140LIH4
Organism: Mus musculus/domesticus
Length: 1193  
Fragment?: false
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Protein
Q4FJM4
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
B1ASC0
Organism: Mus musculus/domesticus
Length: 1473  
Fragment?: false
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Protein
Q3UXL8
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
J3QMG7
Organism: Mus musculus/domesticus
Length: 1121  
Fragment?: false
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Protein
A0A571BEJ4
Organism: Mus musculus/domesticus
Length: 1220  
Fragment?: false
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Protein
C6KI94
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
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Protein
Q3U1M9
Organism: Mus musculus/domesticus
Length: 915  
Fragment?: false
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Protein
A0A0R4J0P3
Organism: Mus musculus/domesticus
Length: 798  
Fragment?: false
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Protein
Q3UY39
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
H7BX92
Organism: Mus musculus/domesticus
Length: 1489  
Fragment?: false
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Protein
D3YZC0
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
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Protein
Q3UG03
Organism: Mus musculus/domesticus
Length: 627  
Fragment?: false
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Protein
A0A0G2JDH6
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
H7BWZ2
Organism: Mus musculus/domesticus
Length: 1577  
Fragment?: false
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Protein
Q3UEE0
Organism: Mus musculus/domesticus
Length: 627  
Fragment?: false
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Protein
Q8BKZ3
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
Q8BUB1
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
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Protein
Q0P6A0
Organism: Mus musculus/domesticus
Length: 239  
Fragment?: false
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Publication
10357859 | -
First Author: Taylor BL
Year: 1999
Journal: Microbiol Mol Biol Rev
Title: PAS domains: internal sensors of oxygen, redox potential, and light.
Volume: 63
Issue: 2
Pages: 479-506
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Publication
15705950 | -
First Author: Kang X
Year: 2005
Journal: Plant Cell
Title: HYPERSENSITIVE TO RED AND BLUE 1, a ZZ-type zinc finger protein, regulates phytochrome B-mediated red and cryptochrome-mediated blue light responses.
Volume: 17
Issue: 3
Pages: 822-35
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Publication
17009962 | -
First Author: Hnia K
Year: 2007
Journal: Biochem J
Title: ZZ domain of dystrophin and utrophin: topology and mapping of a beta-dystroglycan interaction site.
Volume: 401
Issue: 3
Pages: 667-77
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Publication
10374714 | -
First Author: Nilsson T
Year: 1999
Journal: Eur J Pharmacol
Title: Characterisation of 5-HT receptors in human coronary arteries by molecular and pharmacological techniques.
Volume: 372
Issue: 1
Pages: 49-56
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Publication
21618887 | -
 
First Author: Dunford PJ
Year: 2010
Journal: Adv Exp Med Biol
Title: The role of histamine in asthma.
Volume: 709
Pages: 53-66
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Publication
7644667 | -
 
First Author: Zingel V
Year: 1995
Journal: Prog Drug Res
Title: Developments in histamine H1-receptor agonists.
Volume: 44
Pages: 49-85
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Publication
2160972 | -
First Author: Hla T
Year: 1990
Journal: J Biol Chem
Title: An abundant transcript induced in differentiating human endothelial cells encodes a polypeptide with structural similarities to G-protein-coupled receptors.
Volume: 265
Issue: 16
Pages: 9308-13
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Publication
7908055 | -
First Author: Roth BL
Year: 1994
Journal: J Pharmacol Exp Ther
Title: Binding of typical and atypical antipsychotic agents to 5-hydroxytryptamine-6 and 5-hydroxytryptamine-7 receptors.
Volume: 268
Issue: 3
Pages: 1403-10
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Publication
7947717 | -
First Author: Shen D
Year: 1994
Journal: Biochemistry
Title: A human opsin-related gene that encodes a retinaldehyde-binding protein.
Volume: 33
Issue: 44
Pages: 13117-25
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Publication
23044854 | -
First Author: Anantharaman V
Year: 2012
Journal: Mol Biosyst
Title: Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing.
Volume: 8
Issue: 12
Pages: 3142-65
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Publication
10910360 | -
First Author: Kupperman E
Year: 2000
Journal: Nature
Title: A sphingosine-1-phosphate receptor regulates cell migration during vertebrate heart development.
Volume: 406
Issue: 6792
Pages: 192-5
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Publication
9721278 | -
First Author: Tal R
Year: 1998
Journal: J Bacteriol
Title: Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes.
Volume: 180
Issue: 17
Pages: 4416-25
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Publication
21103974 | -
 
First Author: Keppler D
Year: 2011
Journal: Handb Exp Pharmacol
Title: Multidrug resistance proteins (MRPs, ABCCs): importance for pathophysiology and drug therapy.
Issue: 201
Pages: 299-323
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Publication
9192069 | J:40791
First Author: Jia Z
Year: 1997
Journal: Biochem Cell Biol
Title: Protein phosphatases: structures and implications.
Volume: 75
Issue: 1
Pages: 17-26
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Protein Domain
IPR004063 | EDG5_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 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 [, , ].Lysophospholipids (LPs), such as lysophosphatidic acid (LPA), sphingosine1-phosphate (S1P) and sphingosylphosphorylcholine (SPC), have long been known to act as signalling molecules in addition to their roles as intermediates in membrane biosynthesis []. They have roles in the regulation of cell growth, differentiation, apoptosis and development, and have been implicated in a wide range of pathophysiological conditions, including: blood clotting, corneal wounding, subarachinoid haemorrhage, inflammation and colitis []. A number of G protein-coupled receptors bind members of the lysophopholipid family - these include: the cannabinoid receptors; platelet activating factor receptor; OGR1, an SPC receptor identified in ovarian cancer cell lines; PSP24, an orphan receptor that has been proposed to bind LPA; and at least 8 closely related receptors, theEDG family, that bind LPA and S1P [].S1P is released from activated platelets and is also produced by a number of other cell types in response to growth factors and cytokines []. It is proposed to act both as an extracellular mediator and as an intracellularsecond messenger. The cellular effects of S1P include growth related effects, such as proliferation, differentiation, cell survival and apoptosis, and cytoskeletal effects, such as chemotaxis, aggregation, adhesion, morphological change and secretion. The molecule has been implicated in control of angiogenesis, inflammation, heart-rate and tumour progression, and may play an important role in a number of disease states, such as atherosclerosis, and breast and ovarian cancer []. Recently, 5 G protein-coupled receptors have been identified that act as high affinity receptors for S1P, and also as low affinity receptors for the related lysophospholipid, SPC []. EDG-1, EDG-3, EDG-5 and EDG-8 share a high degree of similarity, and are also referred to as lpB1, lpB3, lpB2 and lpB4, respectively. EDG-6 is referred to as lpC1, reflecting its more distant relationship to the other S1P receptors.EDG-5 is expressed abundantly in the heart and lung and at lower levels inthe adult brain. It is also expressed strongly in the embryonic brain [, ]. Binding of S1P to EDG-5 activates G proteins of the Gi and Gq classes. G12 and G13 proteins are also constitutively activated by the receptor. These couplings produce a wide range of cellular effects, including: increased cyclic AMP and calcium levels, activation of MAP kinases and actinrearrangement [, ]. The receptor may have a role in neuronal development and, in zebrafish, has been found to be involved in the control of cell migration during development and organogenesis of the heart [].
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Protein Domain
IPR004062 | EDG3_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 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 [,, ].Lysophospholipids (LPs), such as lysophosphatidic acid (LPA), sphingosine1-phosphate (S1P) and sphingosylphosphorylcholine (SPC), have long been known to act as signalling molecules in addition to their roles as intermediates in membrane biosynthesis []. They have roles in the regulation of cell growth, differentiation, apoptosis and development, and have been implicated in a wide range of pathophysiological conditions, including: blood clotting, corneal wounding, subarachinoid haemorrhage, inflammation and colitis []. A number of G protein-coupled receptors bind members of the lysophopholipid family - these include: the cannabinoid receptors; platelet activating factor receptor; OGR1, an SPC receptor identified in ovarian cancer cell lines; PSP24, an orphan receptor that has been proposed to bind LPA; and at least 8 closely related receptors, the EDG family, that bind LPA and S1P [].S1P is released from activated platelets and is also produced by a number of other cell types in response to growth factors and cytokines []. It is proposed to act both as an extracellular mediator and as an intracellularsecond messenger. The cellular effects of S1P include growth related effects, such as proliferation, differentiation, cell survival and apoptosis, and cytoskeletal effects, such as chemotaxis, aggregation, adhesion, morphological change and secretion. The molecule has been implicated in control of angiogenesis, inflammation, heart-rate and tumour progression, and may play an important role in a number of disease states, such as atherosclerosis, and breast and ovarian cancer []. Recently, 5 G protein-coupled receptors have been identified that act as high affinity receptors for S1P, and also as low affinity receptors for the related lysophospholipid, SPC []. EDG-1, EDG-3, EDG-5 and EDG-8 share a high degree of similarity, and are also referred to as lpB1, lpB3, lpB2 and lpB4, respectively. EDG-6 is referred to as lpC1, reflecting its more distant relationship to the other S1P receptors.EDG-3 is expressed at highest levels in the heart, kidney, placenta andliver of humans, with lower levels found in the lung []. In mouse, highest levels are found in the heart, lung, kidney and spleen, with lower levels in the brain, thymus, muscle and testis []. The receptor has also been found in rat Schwann cells, mouse embryonic brain and breast cancer cells []. Binding of S1P to EDG-3 leads to activation of Gi and Gq classes of G proteins. G12 and G13 can also be constitutively activated by the receptor []. These G proteins produce a range of effects, including: inhibition or activation or adenylyl cylase, MAP kinase activation, serum response element activation and phospholipase C activation, leading to cell proliferation and survival [, ].
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Protein Domain
IPR000987 | EDG1_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 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 [, , ].Lysophospholipids (LPs), such as lysophosphatidic acid (LPA), sphingosine1-phosphate (S1P) and sphingosylphosphorylcholine (SPC), have long been known to act as signalling molecules in addition to their roles as intermediates in membrane biosynthesis []. They have roles in the regulation of cell growth, differentiation, apoptosis and development, and have been implicated in a wide range of pathophysiological conditions, including: blood clotting, corneal wounding, subarachinoid haemorrhage, inflammation and colitis []. A number of G protein-coupled receptors bind members of the lysophopholipid family - these include: the cannabinoid receptors; platelet activating factor receptor; OGR1, an SPC receptor identified in ovarian cancer cell lines; PSP24, an orphan receptor that has been proposed to bind LPA; and at least 8 closely related receptors, the EDG family, that bind LPA and S1P [].S1P is released from activated platelets and is also produced by a number of other cell types in response to growth factors and cytokines []. It is proposed to act both as an extracellular mediator and as an intracellularsecond messenger. The cellular effects of S1P include growth related effects, such as proliferation, differentiation, cell survival and apoptosis, and cytoskeletal effects, such as chemotaxis, aggregation, adhesion, morphological change and secretion. The molecule has been implicated in control of angiogenesis, inflammation, heart-rate and tumour progression, and may play an important role in a number of disease states, such as atherosclerosis, and breast and ovarian cancer []. Recently, 5 G protein-coupled receptors have been identified that act as high affinity receptors for S1P, and also as low affinity receptors for the related lysophospholipid, SPC []. EDG-1, EDG-3, EDG-5 and EDG-8 share a high degree of similarity, and are also referred to as lpB1, lpB3, lpB2 and lpB4, respectively. EDG-6 is referred to as lpC1, reflecting its more distant relationship to the other S1P receptors.EDG-1 was the first member of the family to be cloned (from phorbol-esterdifferentiated human endothelial cells); its ligand, however, was unknown, so it was named endothelial differentiation gene (EDG) 1, reflecting its potential function []. EDG-1 is expressed widely, with highest levels in the brain, heart, lung, liver and spleen. Moderate levels are also found in the thymus, kidney and muscle []. Within these regions, EDG-1 is expressed in endothelial cells, vascular smooth muscle, fibroblasts, melanocytes and cells of epithelioid origin []. Upon binding of S1P, the receptor can couple to Gi1, Gi2, Gi3, Go and Gz type G proteins, leading to inhibition of adenylyl cylase, phospholipase C activation and MAP kinase activation [, ].
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Protein Domain
IPR000433 | Znf_ZZ
Type: Domain
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents ZZ-type zinc finger domains, named because of their ability to bind two zinc ions []. These domains contain 4-6 Cys residues that participate in zinc binding (plus additional Ser/His residues), including a Cys-X2-Cys motif found in other zinc finger domains. These zinc fingers are thought to be involved in protein-protein interactions. The structure of the ZZ domain shows that it belongs to the family of cross-brace zinc finger motifs that include the PHD, RING, and FYVE domains []. ZZ-type zinc finger domains are found in:Transcription factors P300 and CBP.Plant proteins involved in light responses, such as Hrb1.E3 ubiquitin ligases MEX and MIB2 ().Dystrophin and its homologues.Single copies of the ZZ zinc finger occur in the transcriptional adaptor/coactivator proteins P300, in cAMP response element-binding protein (CREB)-binding protein (CBP) and ADA2. CBP provides several binding sites for transcriptional coactivators. The site of interaction with the tumour suppressor protein p53 and the oncoprotein E1A with CBP/P300 is a Cys-rich region that incorporates two zinc-binding motifs: ZZ-type and TAZ2-type. The ZZ-type zinc finger of CBP contains two twisted anti-parallel β-sheets and a short α-helix, and binds two zinc ions []. One zinc ion is coordinated by four cysteine residues via 2 Cys-X2-Cys motifs, and the third zinc ion viaa third Cys-X-Cys motif and a His-X-His motif. The first zinc cluster is strictly conserved, whereas the second zinc cluster displays variability in the position of the two His residues.In Arabidopsis thaliana (Mouse-ear cress), the hypersensitive to red and blue 1 (Hrb1) protein, which regulating both red and blue light responses, contains a ZZ-type zinc finger domain [].ZZ-type zinc finger domains have also been identified in the testis-specific E3 ubiquitin ligase MEX that promotes death receptor-induced apoptosis []. MEX has four putative zinc finger domains: one ZZ-type, one SWIM-type and two RING-type. The region containing the ZZ-type and RING-type zinc fingers is required for interaction with UbcH5a and MEX self-association, whereas the SWIM domain was critical for MEX ubiquitination.In addition, the Cys-rich domains of dystrophin, utrophin and an 87kDa post-synaptic protein contain a ZZ-type zinc finger with high sequence identity to P300/CBP ZZ-type zinc fingers. In dystrophin and utrophin, the ZZ-type zinc finger lies between a WW domain (flanked by and EF hand) and the C-terminal coiled-coil domain. Dystrophin is thought to act as a link between the actin cytoskeleton and the extracellular matrix, and perturbations of the dystrophin-associated complex, for example, between dystrophin and the transmembrane glycoprotein beta-dystroglycan, may lead to muscular dystrophy. Dystrophin and its autosomal homologue utrophin interact with beta-dystroglycan via their C-terminal regions, which are comprised of a WW domain, an EF hand domain and a ZZ-type zinc finger domain []. The WW domain is the primary site of interaction between dystrophin or utrophin and dystroglycan, while the EF hand and ZZ-type zinc finger domains stabilise and strengthen this interaction.
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Publication
27217161 | J:305418
First Author: Smith SJ
Year: 2016
Journal: Dev Biol
Title: The cardiac-restricted protein ADP-ribosylhydrolase-like 1 is essential for heart chamber outgrowth and acts on muscle actin filament assembly.
Volume: 416
Issue: 2
Pages: 373-88
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Publication
16308421 | J:104202
First Author: Shaw RJ
Year: 2005
Journal: Science
Title: The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin.
Volume: 310
Issue: 5754
Pages: 1642-6
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Publication
22974638 | J:193213
First Author: Ambivero CT
Year: 2012
Journal: Biochim Biophys Acta
Title: ATF4 interacts with Abro1/KIAA0157 scaffold protein and participates in a cytoprotective pathway.
Volume: 1823
Issue: 12
Pages: 2149-56
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Publication
10486206 | J:57779
First Author: Nakashima H
Year: 1999
Journal: Genomics
Title: Two novel mouse genes--Nubp2, mapped to the t-complex on chromosome 17, and Nubp1, mapped to chromosome 16--establish a new gene family of nucleotide-binding proteins in eukaryotes.
Volume: 60
Issue: 2
Pages: 152-60
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Publication
23894536 | J:204704
First Author: Chew TG
Year: 2013
Journal: PLoS One
Title: A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption.
Volume: 8
Issue: 7
Pages: e69764
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Publication
1371974 | J:2973
First Author: Nishizawa M
Year: 1992
Journal: FEBS Lett
Title: cDNA clones encoding leucine-zipper proteins which interact with G-CSF gene promoter element 1-binding protein.
Volume: 299
Issue: 1
Pages: 36-8
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Publication
10777215 | J:61657
First Author: De Graeve F
Year: 2000
Journal: Oncogene
Title: A murine ATFa-associated factor with transcriptional repressing activity.
Volume: 19
Issue: 14
Pages: 1807-19
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Publication
11836498 | J:75144
First Author: Suzuki T
Year: 2002
Journal: Nat Genet
Title: Hermansky-Pudlak syndrome is caused by mutations in HPS4, the human homolog of the mouse light-ear gene.
Volume: 30
Issue: 3
Pages: 321-4
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Publication
11784868 | J:73971
First Author: Ponnio T
Year: 2002
Journal: Mol Cell Biol
Title: The nuclear receptor Nor-1 is essential for proliferation of the semicircular canals of the mouse inner ear.
Volume: 22
Issue: 3
Pages: 935-45
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Publication
19523439 | J:151527
First Author: Nonogaki K
Year: 2009
Journal: Biochem Biophys Res Commun
Title: Serotonin 5-HT2C receptor-independent expression of hypothalamic NOR1, a novel modulator of food intake and energy balance, in mice.
Volume: 386
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