Amyloid precursor protein mediates proinflammatory activation of monocytic lineage cells (Q40597791)

21 September 2017

Amyloid precursor protein mediates proinflammatory activation of monocytic lineage cells (English)

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21 September 2017

Cindy M Sondag

1

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PubMed ID

14732706

21 September 2017

Colin K Combs

series ordinal

2

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PubMed ID

14732706

21 September 2017

language of work or name

English

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publication date

19 January 2004

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Journal of Biological Chemistry

21 September 2017

8

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based on heuristic

inferred from page(s)

published in

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21 September 2017

279

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21 September 2017

14

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21 September 2017

14456-14463

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Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein

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A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors

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The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein

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Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins

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1 reference

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Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc

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Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain.

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Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I.

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VLA-4 integrin cross-linking on human monocytic THP-1 cells induces tissue factor expression by a mechanism involving mitogen-activated protein kinase.

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Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells. A possible signaling role for the Syk tyrosine kinase.

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Beta-amyloid precursor protein is detectable on monocytes and is increased in Alzheimer's disease

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cDNA cloning and chromosomal localization of human alpha(11) integrin. A collagen-binding, I domain-containing, beta(1)-associated integrin alpha-chain present in muscle tissues

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Selective binding of collagen subtypes by integrin alpha 1I, alpha 2I, and alpha 10I domains

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Interaction of type IV collagen with the isolated integrins alpha 1 beta 1 and alpha 2 beta 1

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Integrins as a primary signal transduction molecule regulating monocyte immediate-early gene induction

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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

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Signal transduction from the extracellular matrix

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A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration

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The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids

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The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene

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Integrins and signal transduction pathways: the road taken

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The engagement of β1 integrins on promonocytic cells promotes phosphorylation of Syk and formation of a protein complex containing Lyn and β1 integrin

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21 January 2018

Identifiers

DOI

10.1074/JBC.M313747200

1 reference

21 September 2017

1 reference

PubMed ID

14732706