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Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. De plus, nous expédions Amyloid beta (A4) Precursor Protein-Binding, Family B, Member 1 Interacting Protein Protéines (6) et beaucoup plus de produits pour cette protéine.
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Authors provide an overview of the structure and interactions of RIAM and discuss the implications of RIAM functions in innate and adaptive immunity and cancer. [Review]
The Rap1 (Montrer RABGEF1 Anticorps)-RIAM-talin axis of integrin activation and blood cell function
Disruption of the RIAM/lamellipodin (Montrer RAPH1 Anticorps)-integrin-talin complex markedly impairs cell migration.
RIAM is a critical component of the phagocytosis machinery downstream of Rap1 and mediates its function by recruiting talin to the phagocytic complement receptors.
integrin-triggered, RIAM-dependent MEK (Montrer MAP2K1 Anticorps) activation represents a key feedback event required for efficient focal adhesion disassembly.
RIAM was recruited to the lymphocyte plasma membrane through its Ras association and pleckstrin (Montrer PLEK Anticorps) homology domains, both of which were required for lymphocyte adhesion.
RIAM might contribute to the dissemination of melanoma cells.
by regulating the localization of PLC-gamma1, RIAM plays a central role in TCR signaling and the transcription of target genes.
all-trans-retinoic acid-inducible RARP1 selectively affects signal transduction and may contribute to myeloid and megakaryocytic differentiation.(RARP1)
Data pinpoint PREL1 as the first direct link between Ras signalling and cytoskeletal remodelling via Ena/VASP (Montrer VASP Anticorps) proteins during cell migration and spreading.
These data identify the requirement of RIAM for formation of immunological synapses and in resulting T cell functions in autoimmunity.
we show that leukocyte integrin activation critically depends on RIAM both in vitro and in vivo
These in vivo results confirm a role for RIAM in the regulation of some, but not all, leukocyte integrins and suggest that RIAM-regulated integrin activation is required for trafficking of lymphocytes
Conformational activation of talin by PREL-1 triggers integrin-mediated cell adhesion.
crystal structure of an active, GTP (Montrer AK3 Anticorps)-bound GTPase (Montrer RACGAP1 Anticorps) domain of Rap1 (Montrer TERF2IP Anticorps) in complex with the Ras association (RA)-pleckstrin (Montrer PLEK Anticorps) homology (PH) structural module of RIAM at 1.65 A, is reported.
generated RIAM-null mice and found that they are viable, fertile, and apparently healthy
As talin engages F-actin, force exerted on the R2R3 helical bundles disrupts RIAM binding and exposes the vinculin (Montrer VCL Anticorps) binding sites, which recruit vinculin (Montrer VCL Anticorps) to stabilize the complex.
Data demonstrate a novel mechanism by which alphavbeta3 integrin acts to locally suppress beta1 integrin activation and regulate VASP (Montrer VASP Anticorps) and RIAM to control cell adhesion and migration.
Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling.
amyloid beta A4 precursor protein-binding family B member 1-interacting protein
, APBB1-interacting protein 1
, Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
, amyloid beta (A4) precursor protein-binding, family B, member 1 interacting protein
, amyloid beta A4 precursor protein-binding family B member 1-interacting protein-like
, Rap1-GTP-interacting adaptor molecule
, Rap1-interacting adaptor molecule
, proline rich EVH1 ligand 1
, proline-rich EVH1 ligand 1
, proline-rich protein 73
, rap1-GTP-interacting adapter molecule
, retinoic acid-responsive proline-rich protein 1
, proline-rich protein 48