The high mobility group (HMG) boxes of the nuclear protein HMG1 induce chemotaxis and cytoskeleton reorganization in rat smooth muscle cells (Q28570659): Difference between revisions

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scientific journal article

Language	Label	Description	Also known as
English	The high mobility group (HMG) boxes of the nuclear protein HMG1 induce chemotaxis and cytoskeleton reorganization in rat smooth muscle cells	scientific journal article

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scholarly article

1 reference

PubMed publication ID

31 January 2017

The high mobility group (HMG) boxes of the nuclear protein HMG1 induce chemotaxis and cytoskeleton reorganization in rat smooth muscle cells (English)

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PubMed publication ID

31 January 2017

author name string

B. Degryse

1

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31 January 2017

T. Bonaldi

2

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PubMed publication ID

31 January 2017

P. Scaffidi

3

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PubMed publication ID

31 January 2017

S. Müller

4

1 reference

PubMed publication ID

31 January 2017

M. Resnati

5

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31 January 2017

F. Sanvito

6

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31 January 2017

G. Arrigoni

7

1 reference

PubMed publication ID

31 January 2017

M. E. Bianchi

8

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PubMed publication ID

31 January 2017

publication date

19 March 2001

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31 January 2017

Journal of Cell Biology

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PubMed publication ID

31 January 2017

152

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31 January 2017

6

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31 January 2017

1197–1206

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PubMed publication ID

31 January 2017

Chemokine receptors and their role in inflammation and infectious diseases

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Chemoattractant receptors activate distinct pathways for chemotaxis and secretion. Role of G-protein usage

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RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides

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HMG-1 as a late mediator of endotoxin lethality in mice

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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

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The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice

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Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy

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Structure of the HMG box motif in the B-domain of HMG1

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Amphoterin, the 30-kDa protein in a family of HMG1-type polypeptides. Enhanced expression in transformed cells, leading edge localization, and interactions with plasminogen activation

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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

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Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

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PMC publication ID

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PubMed publication ID

1 reference

PubMed publication ID

31 January 2017

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