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Search results 201 to 300 out of 1789 for Vasp

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 393  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 802  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 524  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 804  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 785  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 789  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 789  
Fragment?: false
Publication
First Author: Thomson DM
Year: 2011
Journal: Biochem Biophys Res Commun
Title: Phosphorylation of VASP by AMPK alters actin binding and occurs at a novel site.
Volume: 414
Issue: 1
Pages: 215-9
Publication
First Author: Coppolino MG
Year: 2001
Journal: J Cell Sci
Title: Evidence for a molecular complex consisting of Fyb/SLAP, SLP-76, Nck, VASP and WASP that links the actin cytoskeleton to Fcgamma receptor signalling during phagocytosis.
Volume: 114
Issue: Pt 23
Pages: 4307-18
Publication
First Author: Rachlin AS
Year: 2006
Journal: J Cell Sci
Title: Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin.
Volume: 119
Issue: Pt 6
Pages: 995-1004
Publication
First Author: Dobson L
Year: 2023
Journal: Cell Rep
Title: GSK3 and lamellipodin balance lamellipodial protrusions and focal adhesion maturation in mouse neural crest migration.
Volume: 42
Issue: 9
Pages: 113030
Publication
First Author: Smith MA
Year: 2010
Journal: Dev Cell
Title: A zyxin-mediated mechanism for actin stress fiber maintenance and repair.
Volume: 19
Issue: 3
Pages: 365-76
Publication
First Author: Kliewe F
Year: 2024
Journal: Commun Biol
Title: Zyxin is important for the stability and function of podocytes, especially during mechanical stretch.
Volume: 7
Issue: 1
Pages: 446
Publication  
First Author: Boyer NP
Year: 2020
Journal: J Cell Biol
Title: A pair of E3 ubiquitin ligases compete to regulate filopodial dynamics and axon guidance.
Volume: 219
Issue: 1
Publication
First Author: Maass PG
Year: 2015
Journal: Nat Genet
Title: PDE3A mutations cause autosomal dominant hypertension with brachydactyly.
Volume: 47
Issue: 6
Pages: 647-53
Publication
First Author: Lambrechts A
Year: 2000
Journal: J Biol Chem
Title: cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains.
Volume: 275
Issue: 46
Pages: 36143-51
Publication
First Author: Worth AJ
Year: 2013
Journal: Blood
Title: Disease-associated missense mutations in the EVH1 domain disrupt intrinsic WASp function causing dysregulated actin dynamics and impaired dendritic cell migration.
Volume: 121
Issue: 1
Pages: 72-84
Publication
First Author: Dovere L
Year: 2013
Journal: PLoS One
Title: The niche-derived glial cell line-derived neurotrophic factor (GDNF) induces migration of mouse spermatogonial stem/progenitor cells.
Volume: 8
Issue: 4
Pages: e59431
Publication
First Author: Nishikimi A
Year: 2014
Journal: Sci Signal
Title: Rab13 acts downstream of the kinase Mst1 to deliver the integrin LFA-1 to the cell surface for lymphocyte trafficking.
Volume: 7
Issue: 336
Pages: ra72
Publication
First Author: Artelt N
Year: 2021
Journal: PLoS One
Title: The podocyte-specific knockout of palladin in mice with a 129 genetic background affects podocyte morphology and the expression of palladin interacting proteins.
Volume: 16
Issue: 12
Pages: e0260878
Publication
First Author: May CJ
Year: 2023
Journal: Kidney Int
Title: Podocyte protease activated receptor 1 stimulation in mice produces focal segmental glomerulosclerosis mirroring human disease signaling events.
Volume: 104
Issue: 2
Pages: 265-278
Publication
First Author: Kolb TM
Year: 2021
Journal: Physiol Rep
Title: PDE9A deficiency does not prevent chronic-hypoxic pulmonary hypertension in mice.
Volume: 9
Issue: 18
Pages: e15057
Publication
First Author: Ponceau A
Year: 2015
Journal: PLoS One
Title: αII-spectrin regulates invadosome stability and extracellular matrix degradation.
Volume: 10
Issue: 4
Pages: e0120781
Publication
First Author: Chen W
Year: 2020
Journal: Arterioscler Thromb Vasc Biol
Title: Stabilization of Perivascular Mast Cells by Endothelial CNP (C-Type Natriuretic Peptide).
Volume: 40
Issue: 3
Pages: 682-696
Protein Domain
Type: Family
Description: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity, such as axon guidance and lamellipodial and filopodial dynamics in migrating cells [, ]. Ena/VASP proteins possess a modular domain organization, including a conserved tetramerization domain (TD) mediates the formation of Ena/VASP tetramers []. In vertebrates there are three Ena-VASP family members: Mena (Mammalian enabled), VASP, and EVL (Ena-VASP like).This entry includes VASP and Ena/VASP-like (EVL) proteins.
Publication
First Author: Nayak AP
Year: 2019
Journal: Am J Physiol Lung Cell Mol Physiol
Title: Regulation of ovarian cancer G protein-coupled receptor-1 expression and signaling.
Volume: 316
Issue: 5
Pages: L894-L902
Publication
First Author: Boukhelifa M
Year: 2004
Journal: Cell Motil Cytoskeleton
Title: Palladin is a novel binding partner for Ena/VASP family members.
Volume: 58
Issue: 1
Pages: 17-29
Publication
First Author: Luo H
Year: 2005
Journal: Mol Cell Neurosci
Title: Disruption of palladin results in neural tube closure defects in mice.
Volume: 29
Issue: 4
Pages: 507-15
Publication
First Author: Goicoechea S
Year: 2006
Journal: J Cell Sci
Title: Palladin binds to Eps8 and enhances the formation of dorsal ruffles and podosomes in vascular smooth muscle cells.
Volume: 119
Issue: Pt 16
Pages: 3316-24
Protein
Organism: Mus musculus/domesticus
Length: 46  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 36  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 95  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 48  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
Publication
First Author: Smith WJ
Year: 2003
Journal: J Biol Chem
Title: Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.
Volume: 278
Issue: 7
Pages: 4949-56
Publication
First Author: Dixon RD
Year: 2008
Journal: J Biol Chem
Title: Palladin is an actin cross-linking protein that uses immunoglobulin-like domains to bind filamentous actin.
Volume: 283
Issue: 10
Pages: 6222-31
Publication
First Author: Beck MR
Year: 2013
Journal: J Mol Biol
Title: Structure and function of palladin's actin binding domain.
Volume: 425
Issue: 18
Pages: 3325-37
Publication
First Author: Rönty M
Year: 2007
Journal: Exp Cell Res
Title: Palladin interacts with SH3 domains of SPIN90 and Src and is required for Src-induced cytoskeletal remodeling.
Volume: 313
Issue: 12
Pages: 2575-85
Publication
First Author: Chin YR
Year: 2010
Journal: Mol Cell
Title: The actin-bundling protein palladin is an Akt1-specific substrate that regulates breast cancer cell migration.
Volume: 38
Issue: 3
Pages: 333-44
Publication
First Author: Mykkänen OM
Year: 2001
Journal: Mol Biol Cell
Title: Characterization of human palladin, a microfilament-associated protein.
Volume: 12
Issue: 10
Pages: 3060-73
Publication
First Author: Boukhelifa M
Year: 2006
Journal: FEBS J
Title: The proline-rich protein palladin is a binding partner for profilin.
Volume: 273
Issue: 1
Pages: 26-33
Publication
First Author: Nguyen NU
Year: 2015
Journal: PLoS One
Title: Dual roles of palladin protein in in vitro myogenesis: inhibition of early induction but promotion of myotube maturation.
Volume: 10
Issue: 4
Pages: e0124762
Publication
First Author: Nguyen NU
Year: 2014
Journal: Biochem Biophys Res Commun
Title: Actin-associated protein palladin is required for migration behavior and differentiation potential of C2C12 myoblast cells.
Volume: 452
Issue: 3
Pages: 728-33
Publication
First Author: Jin L
Year: 2010
Journal: PLoS One
Title: The actin associated protein palladin is important for the early smooth muscle cell differentiation.
Volume: 5
Issue: 9
Pages: e12823
Publication
First Author: Jin L
Year: 2009
Journal: J Biol Chem
Title: The actin-associated protein Palladin is required for development of normal contractile properties of smooth muscle cells derived from embryoid bodies.
Volume: 284
Issue: 4
Pages: 2121-30
Protein Domain
Type: Domain
Description: Palladin is a cytoskeletal actin scaffold protein that regulates actin dynamics. The immunoglobulin-like domain of palladin is directly responsible for both actin binding and bundling [, ]. Palladin also interacts with different actin binding proteins and signalling intermediaries required for regulation of cytoskeleton organisation, including profilin [], VASP [], Eps8 [], ezrin [], Lasp-1 [], and Src []. Palladin plays an important role in smooth and skeletal muscle differentiation [, , ], contraction []and cell migration [, , ].Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions []. This entry represents the C-terminal immunoglobulin-like domain (Ig5).
Protein Domain
Type: Homologous_superfamily
Description: Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of signalling proteins, where they serve as simple targeting domains that bind lipids [, , ]. PH domains have a partly opened β-barrel topology that is capped by an alpha helix. The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1) [], Shc adaptor and Numb []; to the Ran-binding domain, found in Nup nuclear pore complex and Ranbp1 []; to the Enabled/VASP homology domain 1 (EVH1 domain), found in Enabled, VASP (vasodilator-stimulated phosphoprotein), Homer and WASP actin regulatory protein []; and to the third domain of FERM, found in moesin, radixin, ezrin, merlin and talin [].This superfamily represents the PH domain and structurally related domains.
Protein
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 320  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 412  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 37  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 633  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 602  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 578  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 681  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 578  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false