Reduced Granulation Tissue and Wound Strength in the Absence of α11β1 Integrin-Reference-Cited by-同舟云学术

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Reduced Granulation Tissue and Wound Strength in the Absence of α11β1 Integrin

Published:2015-05 Issue:5 Volume:135 Page:1435-1444
ISSN:0022-202X
Container-title:Journal of Investigative Dermatology
language:en
Short-container-title:Journal of Investigative Dermatology

Author:

Schulz Jan-Niklas,Zeltz Cédric,Sørensen Ida W.,Barczyk Malgorzata,Carracedo Sergio,Hallinger Ralf,Niehoff Anja,Eckes Beate,Gullberg Donald

Publisher

Elsevier BV

Subject

Cell Biology,Dermatology,Molecular Biology,Biochemistry

Reference42 articles.

1. alpha11beta1 integrin-mediated MMP-13-dependent collagen lattice contraction by fibroblasts: Evidence for integrin-coordinated collagen proteolysis;Barczyk;J Cell Physiol,2013

2. The fibroblast integrin alpha11beta1 is induced in a mechanosensitive manner involving activin A and regulates myofibroblast differentiation;Carracedo;J Biol Chem,2010

3. A review of fibroblast-populated collagen lattices;Dallon;Wound Repair Regen,2008

4. Distinct fibroblast lineages determine dermal architecture in skin development and repair;Driskell;Nature,2013

5. The matricellular protein periostin contributes to proper collagen function and is downregulated during skin aging;Egbert;J Dermatol Sci,2014

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3. Roles for epithelial integrin α3β1 in regulation of the microenvironment during normal and pathological tissue remodeling;American Journal of Physiology-Cell Physiology;2024-05-01

4. Fibroblast and myofibroblast activation in normal tissue repair and fibrosis;Nature Reviews Molecular Cell Biology;2024-04-08

5. KRT17 From Keratinocytes With High Glucose Stimulation Inhibit Dermal Fibroblasts Migration Through Integrin α11;Journal of the Endocrine Society;2024-01-02

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