Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42 (Q24323192)

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English	Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42	scientific article

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Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42 (English)

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Vivette D'Agati

6

object named as

Vivette D'Agati

author given names

Vivette

author last names

D'Agati

1 reference

20 October 2023

1

object named as

Barry I Hudson

author given names

Barry I

author last names

Hudson

1 reference

20 October 2023

Anastasia Z. Kalea

object named as

Anastasia Z Kalea

2

author given names

Anastasia Z

author last names

Kalea

1 reference

20 October 2023

object named as

Eric Boulanger

5

author given names

Eric

author last names

Boulanger

1 reference

20 October 2023

Ann Marie Schmidt

7

author given names

Ann Marie

author last names

Schmidt

object named as

Ann Marie Schmidt

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20 October 2023

author name string

Maria Del Mar Arriero

3

author given names

Maria

author last names

Del Mar Arriero

1 reference

20 October 2023

Evis Harja

4

author given names

Evis

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Harja

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20 October 2023

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publication date

5 December 2008

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Journal of Biological Chemistry

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283

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49

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34457-68

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1 reference

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19 March 2017

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19 March 2017

Receptor for advanced glycation end products (RAGE)-mediated neurite outgrowth and activation of NF-kappaB require the cytoplasmic domain of the receptor but different downstream signaling pathways

1 reference

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19 March 2017

Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous

1 reference

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1 reference

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Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins

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1 reference

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1 reference

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19 March 2017

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1 reference

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19 March 2017

Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2

1 reference

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19 March 2017

The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition

1 reference

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19 March 2017

Role of receptor for advanced glycation end-product (RAGE) and the JAK/STAT-signaling pathway in AGE-induced collagen production in NRK-49F cells

1 reference

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19 March 2017

Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling

1 reference

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19 March 2017

N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression

1 reference

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19 March 2017

The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system

1 reference

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19 March 2017

Activation of TRPP2 through mDia1-dependent voltage gating

1 reference

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27 September 2017

Vascular and inflammatory stresses mediate atherosclerosis via RAGE and its ligands in apoE-/- mice

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2590709

27 September 2017

Receptor for advanced glycation end products (RAGE) mediates neuronal differentiation and neurite outgrowth.

1 reference

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HMGB1 as an autocrine stimulus in human T98G glioblastoma cells: role in cell growth and migration

1 reference

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LARG and mDia1 link Galpha12/13 to cell polarity and microtubule dynamics

1 reference

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Structure of the autoinhibitory switch in formin mDia1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2590709

27 September 2017

Formin proteins: a domain-based approach.

1 reference

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Cholesterol binding, efflux, and a PDZ-interacting domain of scavenger receptor-BI mediate HDL-initiated signaling

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27 September 2017

Receptor tyrosine kinase signaling and trafficking--paradigms revisited.

1 reference

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27 September 2017

Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1.

1 reference

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27 September 2017

DIP (mDia interacting protein) is a key molecule regulating Rho and Rac in a Src-dependent manner

1 reference

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SH2 and PTB domains in tyrosine kinase signaling

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Central role of RAGE-dependent neointimal expansion in arterial restenosis

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1 reference

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Suppression of accelerated diabetic atherosclerosis by the soluble receptor for advanced glycation endproducts

1 reference

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The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyl

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30 May 2018

Identification, classification, and expression of RAGE gene splice variants

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2590709

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The regulation of mDia1 by autoinhibition and its release by Rho*GTP.

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2590709

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Structural basis of Rho GTPase-mediated activation of the formin mDia1.

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Blockade of late stages of autoimmune diabetes by inhibition of the receptor for advanced glycation end products

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Receptor for advanced glycation end products mediates inflammation and enhanced expression of tissue factor in vasculature of diabetic apolipoprotein E-null mice.

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12 December 2020

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10.1074/JBC.M801465200

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release_5btj7g2p65dqjoq5cdntjvjt4a

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