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Search results 401 to 500 out of 606 for Nsf

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Type Details Score
UniProt Feature
UniProt Feature
Begin: 1
Description: Alpha-soluble NSF attachment protein
Type: chain
End: 295
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Publication
10747018 | J:82714
First Author: Sagiv Y
Year: 2000
Journal: EMBO J
Title: GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28.
Volume: 19
Issue: 7
Pages: 1494-504
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Publication
7846761 | -
First Author: Ordway RW
Year: 1994
Journal: Trends Biochem Sci
Title: A TPR domain in the SNAP secretory proteins.
Volume: 19
Issue: 12
Pages: 530-1
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Publication
12140265 | -
First Author: Koticha DK
Year: 2002
Journal: J Cell Sci
Title: Plasma membrane targeting of SNAP-25 increases its local concentration and is necessary for SNARE complex formation and regulated exocytosis.
Volume: 115
Issue: Pt 16
Pages: 3341-51
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Publication
10445030 | -
First Author: Rice LM
Year: 1999
Journal: Mol Cell
Title: Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly.
Volume: 4
Issue: 1
Pages: 85-95
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Publication
17634982 | -
First Author: Bitto E
Year: 2008
Journal: Proteins
Title: Structure and dynamics of gamma-SNAP: insight into flexibility of proteins from the SNAP family.
Volume: 70
Issue: 1
Pages: 93-104
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Publication
16981829 | -
First Author: Andreeva AV
Year: 2006
Journal: Expert Opin Ther Targets
Title: A ubiquitous membrane fusion protein alpha SNAP: a potential therapeutic target for cancer, diabetes and neurological disorders?
Volume: 10
Issue: 5
Pages: 723-33
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Publication
17397838 | -
First Author: Zhao C
Year: 2007
Journal: FEBS Lett
Title: Cellular functions of NSF: not just SNAPs and SNAREs.
Volume: 581
Issue: 11
Pages: 2140-9
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Publication
19762473 | -
First Author: Winter U
Year: 2009
Journal: J Biol Chem
Title: A conserved membrane attachment site in alpha-SNAP facilitates N-ethylmaleimide-sensitive factor (NSF)-driven SNARE complex disassembly.
Volume: 284
Issue: 46
Pages: 31817-26
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Publication
12730228 | -
First Author: Marz KE
Year: 2003
Journal: J Biol Chem
Title: Defining the SNARE complex binding surface of alpha-SNAP: implications for SNARE complex disassembly.
Volume: 278
Issue: 29
Pages: 27000-8
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Protein Domain
IPR000744 | NSF_attach
Type: Family
Description: Regulated exocytosis of neurotransmitters and hormones, as well as intracellular traffic, requires fusion of two lipid bilayers. SNARE proteins are thought to form a protein bridge, the SNARE complex, between an incoming vesicle and the acceptor compartment. SNARE proteins contribute to the specificity of membrane fusion, implying that the mechanisms by which SNAREs are targeted to subcellular compartments are important for specific docking and fusion of vesicles. This mechanism involves a family of conserved proteins, members of which appear to function at all sites of constitutive and regulated secretion in eukaryotes []. Among them are 2 types of cytosolic protein, NSF (N-ethyl-maleimide-sensitive protein) and the SNAPs (alpha-, beta- and gamma-soluble NSF attachment proteins). The yeast vesicular fusion protein, sec17, a cytoplasmic peripheral membrane protein involved in vesicular transport between the endoplasmic reticulum and the golgi apparatus, shows a high degree of sequence similarity to the alpha-SNAP family.Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and Sec17 show similar all-helical structures consisting of an N-terminal extended twisted sheet of four tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle [, , , , , , , ].SNAP-25 and its non-neuronal homologue Syndet/SNAP-23 are synthesized as soluble proteins in the cytosol. Both SNAP-25 and Syndet/SNAP-23 are palmitoylated at cysteine residues clustered in a loop between two N- and C-terminal coils and palmitoylation is essential for membrane binding and plasma membrane targeting. The C-terminal and the N-terminal helices of SNAP-25, are each targeted to the plasma membrane by two distinct cysteine-rich domains and appear to regulate the availability of SNAP to form complexes with SNARE [].
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Protein
A0A494BA49
Organism: Mus musculus/domesticus
Length: 48  
Fragment?: false
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Protein
A0A494BBF5
Organism: Mus musculus/domesticus
Length: 38  
Fragment?: true
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Protein
A0A1B0GR35
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
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Publication
24478316 | J:217251
First Author: Ramakrishnan NA
Year: 2014
Journal: J Biol Chem
Title: Calcium regulates molecular interactions of otoferlin with soluble NSF attachment protein receptor (SNARE) proteins required for hair cell exocytosis.
Volume: 289
Issue: 13
Pages: 8750-66
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Gene
108716403 | napb.L
Type: gene
Organism: frog, African clawed
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Gene
444301 | napa.L
Type: gene
Organism: frog, African clawed
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Gene
446832 | napb.S
Type: gene
Organism: frog, African clawed
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Protein
Q9CXX1
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
Q8C1T5
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
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Protein Coding Gene
MGI:104561 | Napg
Type: protein_coding_gene
Organism: mouse, laboratory
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Allele
Nsf<em1Smoc> | MGI:7291420
Name: N-ethylmaleimide sensitive fusion protein; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Strain
MGI:6429289 | C57BL/6JSmoc-Nsf<em1Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Publication
11823419 | -
First Author: Müller O
Year: 2002
Journal: EMBO J
Title: The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation.
Volume: 21
Issue: 3
Pages: 259-69
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Protein
Q9ERB0
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: false
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Protein
P46460
Organism: Mus musculus/domesticus
Length: 744  
Fragment?: false
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Publication
9705316 | J:49274
First Author: Xu Y
Year: 1998
Journal: J Biol Chem
Title: A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (Vti1-rp2) implicated in protein trafficking in the secretory pathway.
Volume: 273
Issue: 34
Pages: 21783-9
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Protein Coding Gene
MGI:104562 | Napb
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
6306133 | J:7108
First Author: Hartley JW
Year: 1983
Journal: J Exp Med
Title: A mouse gene on chromosome 5 that restricts infectivity of mink cell focus-forming recombinant murine leukemia viruses.
Volume: 158
Issue: 1
Pages: 16-24
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DO Term
DOID:0070377 | developmental and epileptic encephalopathy 96
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Protein Coding Gene
MGI:104563 | Napa
Type: protein_coding_gene
Organism: mouse, laboratory
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Allele
Tg(Nsf-EGFP)IL288Gsat | MGI:4847278
Name: transgene insertion IL288, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
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Strain
MGI:5004033 | STOCK Tg(Nsf-EGFP)IL288Gsat/Mmucd
Attribute String: mutant stock, transgenic
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Publication
12682051 | J:84117
First Author: Zeng Q
Year: 2003
Journal: J Biol Chem
Title: The cytoplasmic domain of Vamp4 and Vamp5 is responsible for their correct subcellular targeting: the N-terminal extenSion of VAMP4 contains a dominant autonomous targeting signal for the trans-Golgi network.
Volume: 278
Issue: 25
Pages: 23046-54
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Protein Domain
IPR042166 | Vamp5
Type: Family
Description: Vesicle-associated membrane protein 5 (Vamp5) is part of the Vamp family of SNAREs (soluble NSF attachment protein receptor), whose members are proteins responsible for the last stage of docking and subsequent fusion in diverse intracellular membrane transport events [].
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Publication
9695844 | J:47887
First Author: Götte M
Year: 1998
Journal: Trends Cell Biol
Title: A new beat for the SNARE drum.
Volume: 8
Issue: 6
Pages: 215-8
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Publication
12106288 | J:15086
First Author: Kato K
Year: 1990
Journal: Eur J Neurosci
Title: A Collection of cDNA Clones with Specific Expression Patterns in Mouse Brain.
Volume: 2
Issue: 8
Pages: 704-711
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Publication
21378973 | J:172303
First Author: Nouvian R
Year: 2011
Journal: Nat Neurosci
Title: Exocytosis at the hair cell ribbon synapse apparently operates without neuronal SNARE proteins.
Volume: 14
Issue: 4
Pages: 411-3
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Protein
Q9CQ56
Organism: Mus musculus/domesticus
Length: 270  
Fragment?: false
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Protein
Q05CJ0
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
Q5I940
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: true
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Protein
E9Q496
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
Q9CYN8
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
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Protein
D3Z6D3
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
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Publication
12853481 | -
First Author: Dilcher M
Year: 2003
Journal: EMBO J
Title: Use1p is a yeast SNARE protein required for retrograde traffic to the ER.
Volume: 22
Issue: 14
Pages: 3664-74
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Publication
11352269 | -
 
First Author: Whiteheart SW
Year: 2001
Journal: Int Rev Cytol
Title: N-ethylmaleimide sensitive factor (NSF) structure and function.
Volume: 207
Pages: 71-112
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Publication
11031229 | -
 
First Author: Lin RC
Year: 2000
Journal: Annu Rev Cell Dev Biol
Title: Mechanisms of synaptic vesicle exocytosis.
Volume: 16
Pages: 19-49
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Protein Domain
IPR019150 | Vesicle_transport_protein_Use1
Type: Family
Description: This entry represents a family of proteins, approximately 300 residues in length, involved in vesicle transport. They have a single C-terminal transmembrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor]domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport [].
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Protein Domain
IPR039812 | Vesicle-fus_ATPase
Type: Family
Description: This family of vesicle-fusing ATPases includes NSF, an essential protein in membrane fusion events. NSF playsthe role of a chaperone by activating SNAP receptor proteins (SNAREs) so that they can participate in membrane fusion. For subsequent rounds of fusion, the SNARE complex must be disassembled, and NSF, in conjunction with SNAPs, utilises its intrinsic ATPase activity to provide a driving force that disassembles SNARE complexes [, , ].
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Protein Coding Gene
MGP_CAROLIEiJ_G0022341 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0024497 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0024464 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0024434 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0024463 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0024231 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_104561 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0024910 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0023704 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0024201 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0024331 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0024297 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0024415 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0024326 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0024957 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0023447 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0023768 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0019070 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0023252 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
7874497 | J:26804
First Author: Nehls M
Year: 1994
Journal: Curr Biol
Title: The sequence complexity of exons trapped from the mouse genome.
Volume: 4
Issue: 11
Pages: 983-9
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GXD Expression
GXD Expression
   
Probe: MGI:3819452
Assay Type: RNA in situ
Annotation Date: 2009-01-23
Strength: Ambiguous
Sex: Not Specified
Emaps: EMAPS:1603911
Pattern: Not Specified
Stage: TS11
Assay Id: MGI:3828701
Age: embryonic day 7.5
Note: Expression is weak to non-existent.
Specimen Label: E7.5
Specimen Num: 1
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GXD Expression
GXD Expression
   
Probe: MGI:3819452
Assay Type: RNA in situ
Annotation Date: 2009-01-23
Strength: Ambiguous
Sex: Not Specified
Emaps: EMAPS:1603913
Pattern: Not Specified
Stage: TS13
Assay Id: MGI:3828701
Age: embryonic day 8.5
Note: Expression is weak to non-existent.
Specimen Label: E8.5
Specimen Num: 2
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Publication
24744148 | J:263474
First Author: Geerts CJ
Year: 2015
Journal: Brain Struct Funct
Title: Tomosyn-2 is required for normal motor performance in mice and sustains neurotransmission at motor endplates.
Volume: 220
Issue: 4
Pages: 1971-82
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Publication
18936251 | J:140649
First Author: Sakisaka T
Year: 2008
Journal: J Cell Biol
Title: Dual inhibition of SNARE complex formation by tomosyn ensures controlled neurotransmitter release.
Volume: 183
Issue: 2
Pages: 323-37
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Publication
18195106 | -
First Author: Ganley IG
Year: 2008
Journal: J Cell Biol
Title: A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells.
Volume: 180
Issue: 1
Pages: 159-72
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Publication
19509055 | -
First Author: Struthers MS
Year: 2009
Journal: J Cell Sci
Title: Functional homology of mammalian syntaxin 16 and yeast Tlg2p reveals a conserved regulatory mechanism.
Volume: 122
Issue: Pt 13
Pages: 2292-9
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Publication
11432826 | -
First Author: Bryant NJ
Year: 2001
Journal: EMBO J
Title: Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.
Volume: 20
Issue: 13
Pages: 3380-8
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Protein Domain
IPR028673 | STX16
Type: Family
Description: Syntaxin-16 (STX16) belongs to the syntaxin family, which is a group of the membrane integrated proteins participating in exocytosis. Syntaxins are associated with various intracellular membrane compartments and have been implicated in various physiological processes such as axonal growth and cell division []. This entry includes STX16 from mammals and it's homologue, Tlg2, from yeasts. Human STX16 is a component of a soluble NSF attachment protein receptor (SNARE) complex (consisting of STX10, STX16, Vti1a, and VAMP3) that is required for the mannose 6-phosphate receptor transport from early endosomes to the Golgi []. Budding yeast Tlg2 is a Syntaxin-like t-SNARE that regulates membrane traffic through the endocytic system [, ].
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Protein Domain
IPR029175 | EXOC2/Sec5
Type: Family
Description: This entry includes Sec5 from yeasts and EXOC2 from animals. In S. cerevisiae, Sec5 is an essential component of the exocyst complex, which is composed of Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84 []. The exocyst complex tethers post-Golgi secretory vesicles to the plasma membrane before soluble NSF attachment protein receptor (SNARE)-mediated membrane fusion [].In mammals, active form (GTP-bound) of Ral GTPase interacts with EXOC2 and Exo84 and regulates the assembly interface of a full octameric exocyst complex []. Similar to yeast exocyst, the mammalian exocyst has been directly linked to post-Golgi targeting of secretory vesicles to discreet membrane sites [].
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Protein Domain
IPR039481 | EXOC2/Sec5_N_dom
Type: Domain
Description: This entry represent a domain found at the N terminus of Sec5 from budding yeasts and EXOC2/VPS51 from animals.In S. cerevisiae, Sec5 is an essential component of the exocyst complex, which is composed of Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84 []. The exocyst complex tethers post-Golgi secretory vesicles to the plasma membrane before soluble NSF attachment protein receptor (SNARE)-mediated membrane fusion [].In mammals, active form (GTP-bound) of Ral GTPase interacts with EXOC2 and Exo84 and regulates the assembly interface of a full octameric exocyst complex []. Similar to yeast exocyst, the mammalian exocyst has been directly linked to post-Golgi targeting of secretory vesicles to discreet membrane sites [].
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Protein
Q8K2J3
Organism: Mus musculus/domesticus
Length: 636  
Fragment?: true
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Publication
21997494 | -
First Author: Liu J
Year: 2012
Journal: Protoplasma
Title: The exocyst complex in exocytosis and cell migration.
Volume: 249
Issue: 3
Pages: 587-97
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Publication
7615633 | -
First Author: TerBush DR
Year: 1995
Journal: J Cell Biol
Title: Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae.
Volume: 130
Issue: 2
Pages: 299-312
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Publication
21040848 | J:167753
First Author: Burgalossi A
Year: 2010
Journal: Neuron
Title: SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming.
Volume: 68
Issue: 3
Pages: 473-87
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Publication
17065550 | J:121010
First Author: Ren Q
Year: 2007
Journal: Mol Biol Cell
Title: Endobrevin/VAMP-8 is the primary v-SNARE for the platelet release reaction.
Volume: 18
Issue: 1
Pages: 24-33
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Publication
18227281 | J:131844
First Author: Williams D
Year: 2008
Journal: J Cell Biol
Title: Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes.
Volume: 180
Issue: 2
Pages: 375-87
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Publication
7989749 | J:21897
First Author: Schulte RJ
Year: 1994
Journal: J Immunol
Title: Tyrosine phosphorylation of VCP, the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein, is unusually sensitive to stimulation by sodium vanadate and hydrogen peroxide.
Volume: 153
Issue: 12
Pages: 5465-72
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Publication
19164751 | J:144173
First Author: Maximov A
Year: 2009
Journal: Science
Title: Complexin controls the force transfer from SNARE complexes to membranes in fusion.
Volume: 323
Issue: 5913
Pages: 516-21
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Publication
26005852 | J:224478
First Author: Siegert S
Year: 2015
Journal: Nat Neurosci
Title: The schizophrenia risk gene product miR-137 alters presynaptic plasticity.
Volume: 18
Issue: 7
Pages: 1008-16
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Protein
A0A0U1RP87
Organism: Mus musculus/domesticus
Length: 83  
Fragment?: false
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Publication
9243180 | -
First Author: Terrian DM
Year: 1997
Journal: Eur J Cell Biol
Title: Phylogenetic analysis of membrane trafficking proteins: a family reunion and secondary structure predictions.
Volume: 73
Issue: 3
Pages: 198-204
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Publication
12145319 | -
First Author: Scales SJ
Year: 2002
Journal: J Biol Chem
Title: Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly.
Volume: 277
Issue: 31
Pages: 28271-9
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Protein Domain
IPR042855 | V_SNARE_CC
Type: Domain
Description: The process of vesicular membrane fusion in eukaryotic cells depends on a conserved fusion machinery called SNARE (soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors). In the process of vesicle docking, proteins present on the vesicle (v-SNARE) have to bind to their counterpart on the target membrane (t-SNARE) to form a core complex that can then recruit the soluble proteins NSF and SNAP. This so called fusion complex can then disassemble after ATP hydrolysis mediated by the ATPase NSF in a process that leads to membrane fusion and the release of the vesicle contents. v-SNAREs include proteins homologous to synaptobrevin [, , ].Structurally the SNARE complex is generally a four-helix bundle comprised of three coiled-coil-forming domains from t-SNAREs and one fromv-SNARE. Although sequence similarity in the t- and v-SNARE coiled-coil homology domains are low there is a striking conservation of theso-called heptad repeat that is of central importance in forming a coiled-coil structure. In a coiled-coil motif, seven residues constitute a canonicalheptad and are designated 'a' through 'g', with 'a' and 'd' being occupied by hydrophobic residues. The association of the four α-helices in the SNARE fusion complex structure produces highly conserved layers of interacting amino acid side chains in the centre of the four-helix bundle. The centre of the bundle is made up of 15 hydrophobic layers from the 'a' and 'd' positions of the heptad repeats of the coiled-coil-forming domains, whereas the central 'ionic' layer is highly conserved and polar in nature, containing a glutamine residue in the three t-SNAREs and an arginine in the v-SNARE, hence the classification of v- and t-SNAREs as R- and Q-SNAREs, respectively. The v-SNARE coiled-coil homology domain is around 60 amino acids in length [, , ].The entry represents the entire v-SNARE coiled-coil homology domain.
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Protein
O70480
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: false
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Protein
Q8BSN6
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: false
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Publication
14525976 | -
First Author: Moskalenko S
Year: 2003
Journal: J Biol Chem
Title: Ral GTPases regulate exocyst assembly through dual subunit interactions.
Volume: 278
Issue: 51
Pages: 51743-8
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Publication
18596155 | J:137824
First Author: Friedrich R
Year: 2008
Journal: J Neurosci
Title: DOC2B acts as a calcium switch and enhances vesicle fusion.
Volume: 28
Issue: 27
Pages: 6794-806
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Publication
25246573 | J:216463
First Author: Burré J
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation.
Volume: 111
Issue: 40
Pages: E4274-83
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Publication
15659226 | J:96244
First Author: Groffen AJ
Year: 2005
Journal: J Neurochem
Title: Two distinct genes drive expression of seven tomosyn isoforms in the mammalian brain, sharing a conserved structure with a unique variable domain.
Volume: 92
Issue: 3
Pages: 554-68
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Publication
14988733 | J:88876
First Author: Dreveny I
Year: 2004
Journal: EMBO J
Title: Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47.
Volume: 23
Issue: 5
Pages: 1030-9
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Publication
31758001 | J:289132
First Author: de Paola M
Year: 2019
Journal: Sci Rep
Title: Pleiotropic effects of alpha-SNAP M105I mutation on oocyte biology: ultrastructural and cellular changes that adversely affect female fertility in mice.
Volume: 9
Issue: 1
Pages: 17374
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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