Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs-Reference-Cited by-同舟云学术

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Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs

Published:2024-01 Issue:1 Volume:300 Page:105552
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Williams Harry M.^ORCID,Moeller Jesper B.,Burns Ian,Schlosser Anders,Sorensen Grith L.,Greenhough Trevor J.,Holmskov Uffe,Shrive Annette K.

Funder

Science and Technology Facilities Council

Novo Nordisk Fonden

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin;Schlosser;J. Immunol.,2009

2. Immunohistochemical localization of fibrinogen C domain containing 1 on epithelial and mucosal surfaces in human tissues;von Huth;J. Histochem. Cytochem.,2017

3. Modulation of the fungal mycobiome is regulated by the chitin-binding receptor FIBCD1;Moeller;J. Exp. Med.,2019

4. FIBCD1 deficiency decreases disease severity in a murine model of invasive pulmonary aspergillosis;Bhattacharya;Immunohorizons,2021

5. The role of FIBCD1 in response to Aspergillus fumigatus in lung epithelial cells;Bhattacharya;PLoS One,2023

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