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Search results 601 to 700 out of 1221 for Vwf

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Type Details Score
Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Allele
Vwf<tm1.1(VWF*D1472H)Vhf> | MGI:7574301
Name: Von Willebrand factor; targeted mutation 1.1, Veronica H Flood
Allele Type: Targeted
Attribute String: Humanized sequence, Inserted expressed sequence
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Publication
32369573 | J:295188
First Author: Braun LJ
Year: 2020
Journal: Blood
Title: Platelets docking to VWF prevent leaks during leukocyte extravasation by stimulating Tie-2.
Volume: 136
Issue: 5
Pages: 627-639
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Publication
37128919 | J:359628
First Author: Ozawa K
Year: 2023
Journal: Arterioscler Thromb Vasc Biol
Title: Elevated LDL Cholesterol Increases Microvascular Endothelial VWF and Thromboinflammation After Myocardial Infarction.
Volume: 43
Issue: 6
Pages: 1041-1053
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Allele
Vwf<tm1Wgr> | MGI:2153009
Name: Von Willebrand factor; targeted mutation 1, Denisa D Wagner
Allele Type: Targeted
Attribute String: Null/knockout
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Protein
Q8CIZ8
Organism: Mus musculus/domesticus
Length: 2813  
Fragment?: false
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Publication
16204318 | J:127571
First Author: Bonnefoy A
Year: 2006
Journal: Blood
Title: Thrombospondin-1 controls vascular platelet recruitment and thrombus adherence in mice by protecting (sub)endothelial VWF from cleavage by ADAMTS13.
Volume: 107
Issue: 3
Pages: 955-64
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Publication
20644116 | J:166480
First Author: Huang J
Year: 2010
Journal: Blood
Title: Shiga toxin B subunits induce VWF secretion by human endothelial cells and thrombotic microangiopathy in ADAMTS13-deficient mice.
Volume: 116
Issue: 18
Pages: 3653-9
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Protein
Q8CIZ8-2
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
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Allele
Vwf<tm1.1Geno> | MGI:6258653
Name: Von Willebrand factor; targeted mutation 1.1, Genoway
Allele Type: Targeted
Attribute String: Humanized sequence
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Genotype
Genotype
Symbol: Vwf/Vwf<+>
Background: involves: C57BL/6
Zygosity: ht
Has Mutant Allele: true
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DO Term
DOID:0060574 | von Willebrand's disease 2
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Genotype
Genotype
Symbol: Vwf/Vwf
Background: involves: C57BL/6
Zygosity: hm
Has Mutant Allele: true
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DO Term
DOID:0060573 | von Willebrand's disease 1
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Allele
Vwf<em1(cre/ERT2)Cya> | MGI:7439361
Name: Von Willebrand factor; endonuclease-mediated mutation 1, Cyagen Biosciences
Allele Type: Endonuclease-mediated
Attribute String: Inducible, Recombinase, Reporter
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MP Term
MP:0031165 | increased circulating von Willebrand factor level
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MP Term
MP:0031163 | abnormal circulating von Willebrand factor level
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Allele
Hprt1<tm2(VWF-lacZ)Aird> | MGI:2447169
Name: hypoxanthine phosphoribosyltransferase 1; targeted mutation 2, William C Aird
Allele Type: Targeted
Attribute String: Reporter
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Allele
Hprt1<tm6(VWF-lacZ)Aird> | MGI:4888493
Name: hypoxanthine phosphoribosyltransferase 1; targeted mutation 6, William C Aird
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Hprt1<tm7(VWF-lacZ)Aird> | MGI:4888494
Name: hypoxanthine phosphoribosyltransferase 1; targeted mutation 7, William C Aird
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Hprt1<tm8(VWF-lacZ)Aird> | MGI:4888495
Name: hypoxanthine phosphoribosyltransferase 1; targeted mutation 8, William C Aird
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Hprt1<tm9(VWF-lacZ)Aird> | MGI:4888496
Name: hypoxanthine phosphoribosyltransferase 1; targeted mutation 9, William C Aird
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Hprt1<tm10(VWF-lacZ)Aird> | MGI:4888497
Name: hypoxanthine phosphoribosyltransferase 1; targeted mutation 10, William C Aird
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Vwf<tm3.1(VWF)Diac> | MGI:5637368
Name: Von Willebrand factor; targeted mutation 3.1, Thomas G Diacovo
Allele Type: Targeted
Attribute String: Humanized sequence, Inserted expressed sequence
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MP Term
MP:0031164 | decreased circulating von Willebrand factor level
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DO Term
DOID:0111054 | von Willebrand's disease 3
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Gene
3674 | ITGA2B
Type: gene
Organism: human
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Gene
3673 | ITGA2
Type: gene
Organism: human
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Genotype
Genotype
Symbol: Vwf/Vwf
Background: Not Specified
Zygosity: hm
Has Mutant Allele: true
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Gene
5327 | PLAT
Type: gene
Organism: human
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Publication
20980682 | J:168401
First Author: Liu J
Year: 2011
Journal: Blood
Title: Vascular bed-specific regulation of the von Willebrand factor promoter in the heart and skeletal muscle.
Volume: 117
Issue: 1
Pages: 342-51
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Vwf/Vwf<+>
Background: involves: 129S6/SvEvTac * C57BL/6NCrl
Zygosity: cn
Has Mutant Allele: true
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Publication
12871266 | -
First Author: Ruggeri ZM
Year: 2003
Journal: J Thromb Haemost
Title: Von Willebrand factor, platelets and endothelial cell interactions.
Volume: 1
Issue: 7
Pages: 1335-42
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Publication
10961880 | -
First Author: Haberichter SL
Year: 2000
Journal: Blood
Title: von Willebrand factor storage and multimerization: 2 independent intracellular processes.
Volume: 96
Issue: 5
Pages: 1808-15
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Publication
27959741 | -
First Author: Leebeek FW
Year: 2016
Journal: N Engl J Med
Title: Von Willebrand's Disease.
Volume: 375
Issue: 21
Pages: 2067-2080
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Publication
11943773 | -
First Author: Nakayama T
Year: 2002
Journal: J Biol Chem
Title: Identification of the regulatory elements of the human von Willebrand factor for binding to platelet GPIb. Importance of structural integrity of the regions flanked by the CYS1272-CYS1458 disulfide bond.
Volume: 277
Issue: 24
Pages: 22063-72
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Publication
18505722 | -
First Author: Remacle AG
Year: 2008
Journal: J Biol Chem
Title: Substrate cleavage analysis of furin and related proprotein convertases. A comparative study.
Volume: 283
Issue: 30
Pages: 20897-906
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Protein Domain
IPR037578 | Von_Willebrand_factor
Type: Family
Description: Von Willebrand factor (VWF) is a multimeric adhesive protein involved in the initiation and progression of thrombus formation at sites of vascular injury []. VWF allows platelets to adhere to sites of vascular injury, forming a bridge between the sub-endothelial collagen matrix and the platelet-surface receptor complex GPIb-IX-V []. VWF is also a chaperone for coagulation factor VIII, delivering it to the injury site and protecting it from clearance from the plasma []. The protein is multidomain with four VWFD domains, four TIL domains, three VWFA domains, three VWFC domains and a C-terminal CTCK domain []. VWF is cleaved to release von Willebrand antigen 2 by a furin-like endopeptidase []. Von Willebrand diseases 1, 2 and 3 are deficiencies of VWF, resulting in impaired platelet aggregation and prolonged bleeding after trauma []. Von Willebrand disease 3 results in haemophilia.
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Publication
22490677 | -
First Author: Zhou YF
Year: 2012
Journal: Blood
Title: Sequence and structure relationships within von Willebrand factor.
Volume: 120
Issue: 2
Pages: 449-58
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Publication
16219351 | J:106749
First Author: Hao X
Year: 2006
Journal: Leuk Res
Title: Histologic and molecular characterizations of megakaryocytic leukemia in mice.
Volume: 30
Issue: 4
Pages: 397-406
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Protein
Q02788
Organism: Mus musculus/domesticus
Length: 1034  
Fragment?: false
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Protein
Q8C6K9
Organism: Mus musculus/domesticus
Length: 2265  
Fragment?: false
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Protein
A6H584
Organism: Mus musculus/domesticus
Length: 2640  
Fragment?: false
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Protein
Q8BND4
Organism: Mus musculus/domesticus
Length: 861  
Fragment?: false
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Protein
A2AX52
Organism: Mus musculus/domesticus
Length: 2309  
Fragment?: false
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Protein
Q04857
Organism: Mus musculus/domesticus
Length: 1025  
Fragment?: false
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Protein
Q6PCM2
Organism: Mus musculus/domesticus
Length: 883  
Fragment?: false
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Protein
Q3UVV9
Organism: Mus musculus/domesticus
Length: 1148  
Fragment?: false
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Protein
A0A286YCT5
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
A0A140T8W1
Organism: Mus musculus/domesticus
Length: 2640  
Fragment?: false
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Protein
D3Z7D5
Organism: Mus musculus/domesticus
Length: 933  
Fragment?: false
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Protein
B0LAD9
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: true
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Protein
B9EK79
Organism: Mus musculus/domesticus
Length: 1182  
Fragment?: false
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Protein
Q5U481
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: true
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Protein
J9JI28
Organism: Mus musculus/domesticus
Length: 736  
Fragment?: false
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Protein
Q8C6Y0
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
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Protein
Q99LW4
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: true
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Protein
O88494
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
E9Q0W9
Organism: Mus musculus/domesticus
Length: 609  
Fragment?: false
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Protein
A0A087WQN9
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
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Protein
A0A2I3BPI1
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein
Q05504
Organism: Mus musculus/domesticus
Length: 959  
Fragment?: true
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Protein
A0A140T8T7
Organism: Mus musculus/domesticus
Length: 2640  
Fragment?: false
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Protein
E9Q6A6
Organism: Mus musculus/domesticus
Length: 2265  
Fragment?: false
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Protein
A0A1L1SSY2
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: true
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Protein
E9PXU1
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
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Protein
Q8CCX8
Organism: Mus musculus/domesticus
Length: 444  
Fragment?: false
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Protein
Q9JHA8
Organism: Mus musculus/domesticus
Length: 891  
Fragment?: false
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Protein
Q8VD76
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
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Protein
B2RQ76
Organism: Mus musculus/domesticus
Length: 891  
Fragment?: false
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Protein
D7RV91
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: true
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Protein
B9EJA5
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Protein
A0A2I3BPJ3
Organism: Mus musculus/domesticus
Length: 49  
Fragment?: true
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Protein
Q8VH45
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
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Protein
Q8R1J5
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: true
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Protein
Q9CTL0
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
Q3UZB8
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
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Protein
S4R2R0
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q8C5I2
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
A0A286YE06
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: false
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Protein
Q497G7
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein
Q8C716
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Publication
2311582 | -
First Author: Voorberg J
Year: 1990
Journal: EMBO J
Title: Domains involved in multimer assembly of von willebrand factor (vWF): multimerization is independent of dimerization.
Volume: 9
Issue: 3
Pages: 797-803
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Publication
9759493 | -
 
First Author: Sadler JE
Year: 1998
Journal: Annu Rev Biochem
Title: Biochemistry and genetics of von Willebrand factor.
Volume: 67
Pages: 395-424
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Publication
10807780 | -
First Author: Jorieux S
Year: 2000
Journal: Blood
Title: Conformational changes in the D' domain of von Willebrand factor induced by CYS 25 and CYS 95 mutations lead to factor VIII binding defect and multimeric impairment.
Volume: 95
Issue: 10
Pages: 3139-45
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Publication
30642920 | -
First Author: Dong X
Year: 2019
Journal: Blood
Title: The von Willebrand factor D'D3 assembly and structural principles for factor VIII binding and concatemer biogenesis.
Volume: 133
Issue: 14
Pages: 1523-1533
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Protein Domain
IPR002035 | VWF_A
Type: Domain
Description: The von Willebrand factor is a large multimeric glycoprotein found in blood plasma. Mutant forms are involved in the aetiology of bleeding disorders []. In von Willebrand factor, the type A domain (vWF) is the prototype for a protein superfamily. The vWF domain is found in various plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins [, , ]. Although the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription, DNA repair, ribosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWF domains participate in numerous biological events (e.g. cell adhesion, migration, homing, pattern formation, and signal transduction), involving interaction with a large array of ligands []. A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of α-helices and β-strands []. The vWF domain fold is predicted to be a doubly-wound, open, twisted β-sheet flanked by α-helices []. 3D structures have been determined for the I-domains of integrins alpha-M (CD11b; with bound magnesium) []and alpha-L (CD11a; with bound manganese) []. The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this site represents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands []. The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved, but the manner in which the metal ion is coordinated differs slightly [].
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Protein Domain
IPR033881 | vWA_BatA_type
Type: Domain
Description: Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif [, ].The von Willebrand factor is a large multimeric glycoprotein found in blood plasma. Mutant forms are involved in the aetiology of bleeding disorders []. In von Willebrand factor, the type A domain (vWF) is the prototype for a protein superfamily. The vWF domain is found in various plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins [, , ]. Although the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription, DNA repair, ribosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWF domains participate in numerous biological events (e.g. cell adhesion, migration, homing, pattern formation, and signal transduction), involving interaction with a large array of ligands []. A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of α-helices and β-strands []. The vWF domain fold is predicted to be a doubly-wound, open, twisted β-sheet flanked by α-helices []. 3D structures have been determined for the I-domains of integrins alpha-M (CD11b; with bound magnesium) []and alpha-L (CD11a; with bound manganese) []. The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this site represents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands []. The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved, but the manner in which the metal ion is coordinated differs slightly [].
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Protein Domain
IPR036465 | vWFA_dom_sf
Type: Homologous_superfamily
Description: The von Willebrand factor is a large multimeric glycoprotein found in blood plasma. Mutant forms are involved in the aetiology of bleeding disorders []. In von Willebrand factor, the type A domain (vWF) is the prototype for a protein superfamily. The vWF domain is found in various plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins [, , ]. Although the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription, DNA repair, ribosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWF domains participate in numerous biological events (e.g. cell adhesion, migration, homing, pattern formation, and signal transduction), involving interaction with a large array of ligands []. A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of α-helices and β-strands []. The vWF domain fold is predicted to be a doubly-wound, open, twisted β-sheet flanked by α-helices []. 3D structures have been determined for the I-domains of integrins alpha-M (CD11b; with bound magnesium) []and alpha-L (CD11a; with bound manganese) []. The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this site represents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands []. The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved, but the manner in which the metal ion is coordinated differs slightly [].
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Protein Domain
IPR001846 | VWF_type-D
Type: Domain
Description: Von Willebrand factor (VWF) is a large, multimeric blood glycoproteinsynthesized in endothelial cells and megakaryocytes, that is required fornormal hemostasis. Mutant forms are involved in the most common inheritedbleeding disorder (von Willebrand disease: VWD). VWF mediates the adhesion ofplatelets to sites of vascular damage by binding to specific platelet membraneglycoproteins and to constituents of exposed connective tissue. It is alsoessential for the transport of the blood clotting factor VIII [, ].VWF is a large multidomain protein. The type D domain (VWFD) is not onlyrequired for blood clotting factor VIII binding but also for normalmultimerization of VWF [, ]. The interaction between blood clotting factorVIII and VWF is necessary for normal survival of blood clotting factor VIII inblood circulation. The VWFD domain is a highly structured region, in which thefirst conserved Cys has been found to form a disulfide bridge with the secondconserved one [, ].The VWFD domain can occur in association with a lot of different domains likevitellogenin, VWFC, VWFA, and ZP.Proteins with a VWFD domain are listed below:Mammalian von Willebrand factor (VWF), a multifunctional protein involvedin maintaining homeostasis. It consists of 4 VWFD domains (D1-4), 3 VWFA domains,3 VWFB domains, 2 VWFC domains, an X domain and a C-terminal cystine knot [].There might be a third VWFC domain within the type B domain region []. The structure of the VWF D3 domain has been revealed []. Mammalian zonadhesin, which binds in a species-specific manner to the zonapellucida of the egg.Mammalian bone morphogenetic protein-binding (BMP-binding) endothelialregulator protein.Mammalian alpha-tectorin, which is one of the major non-collagenouscomponents of the tectorial membrane.Mammalian mucins, glycoproteins that are major constituents of theglycocalyx that covers mucosal epithelium.Mammalian vitellogenin, a major lipoprotein in many oviparous animals,which is a precursor of a lipid-binding product named as lipovitellin.This entry represents the VWFD domain.
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Protein
Q8C8N3
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: false
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Protein
Q505H4
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: false
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Protein
F6UH68
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: true
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Protein
D7RV94
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
A0A338P7C1
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: false
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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