Periostin C-Terminal Is Intrinsically Disordered and Interacts with 143 Proteins in an In Vitro Epidermal Model of Atopic Dermatitis-Reference-Cited by-同舟云学术

Periostin C-Terminal Is Intrinsically Disordered and Interacts with 143 Proteins in an In Vitro Epidermal Model of Atopic Dermatitis

Published:2023-09-13 Issue:19 Volume:62 Page:2803-2815
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rusbjerg-Weberskov Christian E.¹,Johansen Mette Liere¹,Nowak Jan S.¹²,Otzen Daniel E.¹²^ORCID,Pedersen Jan Skov³²^ORCID,Enghild Jan J.¹^ORCID,Nielsen Nadia Sukusu¹

Affiliation:

1. Department of Molecular Biology and Genetics, Aarhus University, Aarhus C 8000, Denmark

2. Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus C 8000, Denmark

3. Department of Chemistry, Aarhus University, Aarhus C 8000, Denmark

Funder

LEO Fondet

Danmarks Frie Forskningsfond

Novo Nordisk Fonden

Velux Fonden

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.3c00176

Reference77 articles.

1. The role of periostin in tissue remodeling across health and disease

2. Incorporation of Tenascin-C into the Extracellular Matrix by Periostin Underlies an Extracellular Meshwork Architecture

3. Interaction between Periostin and BMP-1 Promotes Proteolytic Activation of Lysyl Oxidase

4. Periostin regulates collagen fibrillogenesis and the biomechanical properties of connective tissues

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