| Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs. | Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs.
Williams HM, Moeller JB, Burns I, Schlosser A, Sorensen GL, Greenhough TJ, Holmskov U, Shrive AK., Free PMC Article | 02/13/2024 |
| The role of FIBCD1 in response to Aspergillus fumigatus in lung epithelial cells. | The role of FIBCD1 in response to Aspergillus fumigatus in lung epithelial cells.
Bhattacharya S, Maupin AJ, Schlosser AG, Füchtbauer EM, Gloria YC, Weber ANR, Holmskov U, Moeller JB, Templeton SP., Free PMC Article | 03/10/2023 |
| FIBCD1 is an endocytic GAG receptor associated with a novel neurodevelopmental disorder. | FIBCD1 is an endocytic GAG receptor associated with a novel neurodevelopmental disorder.
Fell CW, Hagelkruys A, Cicvaric A, Horrer M, Liu L, Li JSS, Stadlmann J, Polyansky AA, Mereiter S, Tejada MA, Kokotović T, Achuta VS, Scaramuzza A, Twyman KA, Morrow MM, Juusola J, Yan H, Wang J, Burmeister M, Choudhury B, Andersen TL, Wirnsberger G, Holmskov U, Perrimon N, Žagrović B, Monje FJ, Moeller JB, Penninger JM, Nagy V., Free PMC Article | 09/17/2022 |
| The myokine Fibcd1 is an endogenous determinant of myofiber size and mitigates cancer-induced myofiber atrophy. | The myokine Fibcd1 is an endogenous determinant of myofiber size and mitigates cancer-induced myofiber atrophy.
Graca FA, Rai M, Hunt LC, Stephan A, Wang YD, Gordon B, Wang R, Quarato G, Xu B, Fan Y, Labelle M, Demontis F., Free PMC Article | 05/14/2022 |
| thses findings support FIBCD1 as a lung epithelial pattern recognition receptor that recognizes the complex Aspergillus fumigatus cell wall polysaccharides and modulates the lung epithelial inflammatory response by suppressing inflammatory mediators and mucins | FIBCD1 Binds Aspergillus fumigatus and Regulates Lung Epithelial Response to Cell Wall Components.
Jepsen CS, Dubey LK, Colmorten KB, Moeller JB, Hammond MA, Nielsen O, Schlosser A, Templeton SP, Sorensen GL, Holmskov U., Free PMC Article | 10/5/2019 |
| FIBCD1 is expressed in epithelial cells derived from all three germ layers. Endodermal-derived epithelial cells throughout the gastrointestinal tract and the respiratory system showed high expression of FIBCD1 and also mesodermal-derived cells in the genitourinary system and ectodermal-derived epidermis and sebaceous glands cells expressed FIBCD1. | Immunohistochemical Localization of Fibrinogen C Domain Containing 1 on Epithelial and Mucosal Surfaces in Human Tissues.
von Huth S, Moeller JB, Schlosser A, Marcussen N, Nielsen O, Nielsen V, Sorensen GL, Holmskov U., Free PMC Article | 08/3/2019 |
| FIBCD1 may be a novel biomarker to evaluate the prognosis of gastric cancer. | Overexpression of FIBCD1 Is Predictive of Poor Prognosis in Gastric Cancer.
Jiang C, Zhu J, Zhou P, Zhu H, Wang W, Jin Q, Li P. | 05/11/2019 |
| The high affinity ligand N-acetylmannosamine (ManNAc) binds FIBCD1 in the S1 site, predominantly via the acetyl group with the oxygen and acetamide nitrogen hydrogen-bonded to the protein and the methyl group inserted into a hydrophobic pocket. | Crystal structure of the tetrameric fibrinogen-like recognition domain of fibrinogen C domain containing 1 (FIBCD1) protein.
Shrive AK, Moeller JB, Burns I, Paterson JM, Shaw AJ, Schlosser A, Sorensen GL, Greenhough TJ, Holmskov U., Free PMC Article | 04/12/2014 |
| Observational study of gene-disease association. (HuGE Navigator) | New genetic associations detected in a host response study to hepatitis B vaccine.
Davila S, Froeling FE, Tan A, Bonnard C, Boland GJ, Snippe H, Hibberd ML, Seielstad M. | 04/7/2010 |
| The recognition unit of FIBCD1 organizes into a noncovalently linked tetrameric structure and uses a hydrophobic funnel (S1) for acetyl group recognition. | The recognition unit of FIBCD1 organizes into a noncovalently linked tetrameric structure and uses a hydrophobic funnel (S1) for acetyl group recognition.
Thomsen T, Moeller JB, Schlosser A, Sorensen GL, Moestrup SK, Palaniyar N, Wallis R, Mollenhauer J, Holmskov U., Free PMC Article | 02/1/2010 |
| FIBCD1 is a high-affinity receptor for chitin and chitin fragments, and may play an important role in controlling the exposure of intestine to chitin and chitin fragments | Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin.
Schlosser A, Thomsen T, Moeller JB, Nielsen O, Tornøe I, Mollenhauer J, Moestrup SK, Holmskov U. | 01/21/2010 |