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Search results 1501 to 1600 out of 5729 for Nlrp3

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Type Details Score
Publication
First Author: Tan YJ
Year: 2005
Journal: J Virol
Title: The severe acute respiratory syndrome coronavirus 3a protein up-regulates expression of fibrinogen in lung epithelial cells.
Volume: 79
Issue: 15
Pages: 10083-7
Publication
First Author: Oostra M
Year: 2006
Journal: J Virol
Title: Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.
Volume: 80
Issue: 5
Pages: 2326-36
Publication
First Author: Lu W
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Severe acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release.
Volume: 103
Issue: 33
Pages: 12540-5
Publication
First Author: Yu CJ
Year: 2004
Journal: FEBS Lett
Title: Identification of a novel protein 3a from severe acute respiratory syndrome coronavirus.
Volume: 565
Issue: 1-3
Pages: 111-6
Publication
First Author: Shen S
Year: 2005
Journal: Biochem Biophys Res Commun
Title: The severe acute respiratory syndrome coronavirus 3a is a novel structural protein.
Volume: 330
Issue: 1
Pages: 286-92
Publication
First Author: Minakshi R
Year: 2009
Journal: PLoS One
Title: The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor.
Volume: 4
Issue: 12
Pages: e8342
Publication  
First Author: Farag NS
Year: 2020
Journal: Int J Biochem Cell Biol
Title: Viroporins and inflammasomes: A key to understand virus-induced inflammation.
Volume: 122
Pages: 105738
Publication
First Author: Miao G
Year: 2021
Journal: Dev Cell
Title: ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated assembly of the SNARE complex required for autolysosome formation.
Volume: 56
Issue: 4
Pages: 427-442.e5
Publication
First Author: Kern DM
Year: 2021
Journal: Nat Struct Mol Biol
Title: Cryo-EM structure of SARS-CoV-2 ORF3a in lipid nanodiscs.
Volume: 28
Issue: 7
Pages: 573-582
Protein Domain
Type: Family
Description: Coronavirus encodes two viroporins, E protein and protein 3a, which act as ion-conductive pores in planar lipid bilayers and are required for maximal SARS-CoV replication and virulence []. In betacoronavirus, this protein plays a role in viral egress via lysosomal trafficking [, ]. Protein 3a from SARS-CoV-2 also blocks autolysosomes formation by binding and sequestering the host component VPS39 for homotypic fusion and protein sorting (HOPS) on late endosomes. This prevents fusion of autophagosomes with lysosomes, disrupting autophagy and facilitating virus egress [].This entry represents protein 3a encoded by Orf3/3a, also known as X1, which forms homotetrameric potassium, sodium or calcium sensitive ion channels (viroporin) and may modulate virus release. It has also been shown to up-regulate expression of fibrinogen subunits FGA, FGBand FGG in host lung epithelial cells [, , , ].3a protein is a pro-apoptosis-inducing protein. It localises to the endoplasmic reticulum (ER)-Golgi compartment. SARS-CoV causes apoptosis of infected cells through NLRP3 inflammasome activation, as ORF3a is a potent activator of the signals required for this activation, pro-IL-1beta gene transcription and protein maturation. This protein also promotes the ubiquitination of apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) mediated by its interaction with TNF receptor-associated factor 3 (TRAF3). The expression of ORF3a induces NF-kappa B activation and up-regulates fibrinogen secretion with the consequent high cytokine production [, , , ]. Another apoptosis mechanism described for this protein is the activation of the PERK pathway of unfolded protein response (UPR), which causes phosphorylation of eIF2alpha and leads to reduced translation of cellular proteins as well as the activation of pro-apoptotic downstream effectors (i.e ATF4, CHOP) [].
Publication  
First Author: Szabó D
Year: 2022
Journal: Brain Behav Immun
Title: Maternal P2X7 receptor inhibition prevents autism-like phenotype in male mouse offspring through the NLRP3-IL-1β pathway.
Volume: 101
Pages: 318-332
Publication
First Author: Zhang JR
Year: 2024
Journal: Nat Commun
Title: Augmented microglial endoplasmic reticulum-mitochondria contacts mediate depression-like behavior in mice induced by chronic social defeat stress.
Volume: 15
Issue: 1
Pages: 5199
Publication
First Author: Shenderov K
Year: 2014
Journal: J Immunol
Title: Cutting edge: Endoplasmic reticulum stress licenses macrophages to produce mature IL-1β in response to TLR4 stimulation through a caspase-8- and TRIF-dependent pathway.
Volume: 192
Issue: 5
Pages: 2029-2033
Publication
First Author: Hara H
Year: 2013
Journal: Nat Immunol
Title: Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity.
Volume: 14
Issue: 12
Pages: 1247-55
Publication
First Author: Dowling JK
Year: 2014
Journal: J Biol Chem
Title: Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation.
Volume: 289
Issue: 10
Pages: 6429-37
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
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: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication
First Author: Sun C
Year: 2012
Journal: J Biol Chem
Title: Inactivation of MARK4, an AMP-activated protein kinase (AMPK)-related kinase, leads to insulin hypersensitivity and resistance to diet-induced obesity.
Volume: 287
Issue: 45
Pages: 38305-15
Publication
First Author: Sultanakhmetov G
Year: 2024
Journal: Brain Commun
Title: Mark4 ablation attenuates pathological phenotypes in a mouse model of tauopathy.
Volume: 6
Issue: 3
Pages: fcae136
Publication
First Author: Kuhns S
Year: 2013
Journal: J Cell Biol
Title: The microtubule affinity regulating kinase MARK4 promotes axoneme extension during early ciliogenesis.
Volume: 200
Issue: 4
Pages: 505-22
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Khalafalla MG
Year: 2017
Journal: J Biol Chem
Title: P2X7 receptor antagonism prevents IL-1β release from salivary epithelial cells and reduces inflammation in a mouse model of autoimmune exocrinopathy.
Volume: 292
Issue: 40
Pages: 16626-16637
Publication  
First Author: Chuang HC
Year: 2021
Journal: eNeuro
Title: Lytic Cell Death in Specific Microglial Subsets Is Required for Preventing Atypical Behavior in Mice.
Volume: 8
Issue: 1
Protein Domain
Type: Family
Description: This family is specific for E proteins from alphacoronaviruses.E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembranedomains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
Protein Domain
Type: Family
Description: E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
Protein Domain
Type: Family
Description: This family is specific for E proteins from betacoronaviruses.E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
Protein Domain
Type: Family
Description: This entry represents the Envelope (E) small membrane protein of Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV) or COVID-19 virus.E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
Protein Domain
Type: Family
Description: This entry represents the Envelope (E) small membrane protein of Middle East respiratory syndrome (MERS) coronavirus (CoV), as well as E proteins from related coronaviruses.E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficienttrafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
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: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication
First Author: Chan CH
Year: 2019
Journal: Mol Cancer Res
Title: DNA Damage, Liver Injury, and Tumorigenesis: Consequences of DDX3X Loss.
Volume: 17
Issue: 2
Pages: 555-566
Publication
First Author: Chen HH
Year: 2016
Journal: J Neurosci
Title: DDX3 Modulates Neurite Development via Translationally Activating an RNA Regulon Involved in Rac1 Activation.
Volume: 36
Issue: 38
Pages: 9792-804
Publication
First Author: Jowhar Z
Year: 2024
Journal: Mol Syst Biol
Title: A ubiquitous GC content signature underlies multimodal mRNA regulation by DDX3X.
Volume: 20
Issue: 3
Pages: 276-290
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1689428
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 1
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1754428
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 2
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:3284528
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 3
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1697428
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 4
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1754928
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 5
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:3280928
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 6
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1778728
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 7
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1757728
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 8
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:3599828
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 9
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1619828
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 10
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:3598828
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 11
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 12
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1672828
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 13
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1876728
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 14
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1684628
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 15
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1720228
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 16
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Absent
Sex: Pooled
Emaps: EMAPS:1750328
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: false
Specimen Num: 17
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1737328
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 18
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1832128
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 19
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1842628
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 20
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1752528
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 21
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:3511228
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 22
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1914328
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 23
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1742828
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 24
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:3288928
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 25
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1718528
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 26
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1775128
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 27
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1683328
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 28
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1788628
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 29
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1789128
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 30
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1885228
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 31
GXD Expression    
Probe: MGI:1205192
Assay Type: RT-PCR
Annotation Date: 1998-06-01
Strength: Present
Sex: Pooled
Emaps: EMAPS:1866628
Stage: TS28
Assay Id: MGI:1205194
Age: postnatal week 6-8
Image: st96_422
Specimen Label: None
Detected: true
Specimen Num: 32