Non-enzymatic glycation of bone collagen modifies osteoclastic activity and differentiation. (Q38700889)

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22 December 2019

title

Non-enzymatic glycation of bone collagen modifies osteoclastic activity and differentiation (English)

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22 December 2019

1

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22 December 2019

author name string

Blandine Merle

2

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22 December 2019

Evelyne Gineyts

3

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22 December 2019

Stéphanie Viguet-Carrin

4

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22 December 2019

Pierre D Delmas

5

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22 December 2019

Patrick Garnero

6

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22 December 2019

language of work or name

English

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publication date

1 December 2006

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Journal of Biological Chemistry

22 December 2019

published in

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22 December 2019

volume

282

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22 December 2019

issue

8

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22 December 2019

page(s)

5691-5703

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Maillard reaction products in tissue proteins: new products and new perspectives

22 December 2019

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A breaker of advanced glycation end products attenuates diabetes-induced myocardial structural changes

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Advanced glycation end-products attenuate human mesenchymal stem cells and prevent cognate differentiation into adipose tissue, cartilage, and bone

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Advanced glycation endproducts interefere with integrin-mediated osteoblastic attachment to a type-I collagen matrix

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Advanced glycation end-products (AGEs) induce concerted changes in the osteoblastic expression of their receptor RAGE and in the activation of extracellular signal-regulated kinases (ERK).

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Cross-linking in collagen by nonenzymatic glycation increases the matrix stiffness in rabbit achilles tendon

21 January 2018

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21 January 2018

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21 January 2018

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Identifiers

DOI

10.1074/JBC.M610536200

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17142454%20AND%20SRC:MED&resulttype=core&format=json

22 December 2019

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