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Von Willebrand factor A domain containing 1

wARP, von Willebrand factor A domain-related protein
VWA1 belongs to the von Willebrand factor (VWF; MIM 613160) A (VWFA) domain superfamily of extracellular matrix proteins and appears to play a role in cartilage structure and function (Fitzgerald et al., 2002 [PubMed 12062410]).[supplied by OMIM, Nov 2010] (from NCBI)
Top mentioned proteins: MANF, SET, CAN, STEP, HAD
Papers on wARP
Breeding Strategy Determines Rupture Incidence in Post-Infarct Healing WARPing Cardiovascular Research.
Papageorgiou et al., Maastricht, Netherlands. In Plos One, 2014
BACKGROUND: Von Willebrand A domain Related Protein (WARP), is a recently identified extracellular matrix protein.
Protein phasing at non-atomic resolution by combining Patterson and VLD techniques.
Mazzone et al., Italy. In Acta Crystallogr D Biol Crystallogr, 2014
The applications include the use of ARP/wARP to check the quality of the final electron-density maps in an objective way.
A small molecule glycosaminoglycan mimetic blocks Plasmodium invasion of the mosquito midgut.
Dinglasan et al., Baltimore, United States. In Plos Pathog, 2012
Through direct-binding assays, we observed that VS1 bound to two critical ookinete micronemal proteins, each containing at least one von Willebrand factor A (vWA) domain: (i) circumsporozoite protein and thrombospondin-related anonymous protein-related protein (CTRP) and (ii) vWA domain-related protein (WARP).
Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex.
Boggon et al., New Haven, United States. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
A structure solution obtained by molecular replacement followed by ARP/wARP automatic model building allowed a 'sequence-by-crystallography' approach to discover that the contaminating protein was lysozyme.
WARP interacts with collagen VI-containing microfibrils in the pericellular matrix of human chondrocytes.
Fitzgerald et al., Münster, Germany. In Plos One, 2011
Collagen VI and WARP are extracellular structural macromolecules present in cartilage and associated with BM suprastructures in non-skeletal tissues.
Immunocytochemical distribution of WARP (von Willebrand A domain-related protein) in the inner ear.
GeneRIF
Ishiyama et al., Los Angeles, United States. In Brain Res, 2011
The distinct localization of WARP in the human and mouse inner ear blood vessels suggests an important role maintaining the integrity of the vasculature.
Crystallization and calcium/sulfur SAD phasing of the human EF-hand protein S100A2.
Fritz et al., Konstanz, Germany. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010
The electron-density map obtained was well interpretable and could be used for automated model building by ARP/wARP.
Cloning, expression and transmission-blocking activity of anti-PvWARP, malaria vaccine candidate, in Anopheles stephensi mysorensis.
Djadid et al., Tehrān, Iran. In Malar J, 2009
Ookinete-secreted protein, Plasmodium vivax von Willebrand factor A domain-related protein (PvWARP), is a candidate for malaria transmission-blocking vaccines (TBVs).
Mice lacking the extracellular matrix protein WARP develop normally but have compromised peripheral nerve structure and function.
GeneRIF
Bateman et al., Australia. In J Biol Chem, 2009
although WARP is not essential for basement membrane formation or musculoskeletal development, it has critical roles in the structure and function of peripheral nerves.
De novo sulfur SAD phasing of the lysosomal 66.3 kDa protein from mouse.
Ficner et al., Göttingen, Germany. In Acta Crystallogr D Biol Crystallogr, 2009
Density modification using SOLOMON and DM resulted in a high-quality electron-density map, enabling automatic model building with ARP/wARP.
"Conditional Restraints": Restraining the Free Atoms in ARP/wARP.
Perrakis et al., Amsterdam, Netherlands. In Structure, 2009
In the ARP/wARP approach, model building is facilitated by initially interpreting a density map with free atoms of unknown chemical identity; all structural information for such chemically unassigned atoms is discarded.
Analysis of von Willebrand factor A domain-related protein (WARP) polymorphism in temperate and tropical Plasmodium vivax field isolates.
Ladoni et al., Tehrān, Iran. In Malar J, 2008
Here, the sequence analysis of an extra-cellular malaria protein expressed in ookinetes, named von Willebrand factor A domain-related protein (WARP), is reported in 91 Plasmodium vivax isolates circulating in different regions of Iran.
The extracellular matrix protein WARP is a novel component of a distinct subset of basement membranes.
GeneRIF
Bateman et al., Melbourne, Australia. In Matrix Biol, 2008
identification of WARP as a component of a limited range of specialized basement membranes provides further evidence for the heterogeneous composition of basement membranes between different tissues
A knowledge-driven approach for crystallographic protein model completion.
Perrakis et al., Netherlands. In Acta Crystallogr D Biol Crystallogr, 2008
The average root-mean-square deviation of the C(alpha) atoms in the loops built during validation was less than 0.4 A. When implemented in the context of automated model building in ARP/wARP, Loopy can increase the completeness of the built models.
Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7.
Perrakis et al., Hamburg, Germany. In Nat Protoc, 2007
ARP/wARP is a software suite to build macromolecular models in X-ray crystallography electron density maps.
Conformational stability and domain unfolding of the Von Willebrand factor A domains.
GeneRIF
Moake et al., Houston, United States. In J Mol Biol, 2007
Urea was used as a surrogate for shear to study denaturation of the individual VWF recombinant A domains, A1, A2, and A3, and the domain triplet, A1-A2-A3.
WARP is a novel multimeric component of the chondrocyte pericellular matrix that interacts with perlecan.
GeneRIF
Fitzgerald et al., Melbourne, Australia. In J Biol Chem, 2006
WARP forms macromolecular structures that interact with perlecan to contribute to the assembly and/or maintenance of "permanent" cartilage structures during development and in mature cartilages
Applications of ACORN to data at 1.45 A resolution.
Review
Velmurugan et al., Chennai, India. In J Synchrotron Radiat, 2004
An initial model can automatically be built by ARP/wARP followed by REFMAC for refinement.
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