Site-specific O-glycosylation on the MUC2 mucin protein inhibits cleavage by the Porphyromonas gingivalis secreted cysteine protease (RgpB).
about
Protease inhibition as new therapeutic strategy for GI diseasesTherapeutic Potential to Modify the Mucus Barrier in Inflammatory Bowel DiseaseUlcerative colitis as a polymicrobial infection characterized by sustained broken mucus barrierDeregulation of intestinal anti-microbial defense by the dietary additive, maltodextrinKeeping bugs in check: The mucus layer as a critical component in maintaining intestinal homeostasisInhibitor of ppGalNAc-T3-mediated O-glycosylation blocks cancer cell invasiveness and lowers FGF23 levels.Membrane protein profiling of human colon reveals distinct regional differencesMucus and the goblet cell.Development of isoform-specific sensors of polypeptide GalNAc-transferase activity.Podoplanin requires sialylated O-glycans for stable expression on lymphatic endothelial cells and for interaction with platelets.Multiple enzyme approach for the characterization of glycan modifications on the C-terminus of the intestinal MUC2mucin.The mucus and mucins of the goblet cells and enterocytes provide the first defense line of the gastrointestinal tract and interact with the immune system.Salivary mucin 19 glycoproteins: innate immune functions in Streptococcus mutans-induced caries in mice and evidence for expression in human salivaThe composition of the gut microbiota shapes the colon mucus barrier.Microbiota-mediated inflammation and antimicrobial defense in the intestine.Inhibition of Cyclooxygenase-2 Prevents Chronic and Recurrent Cystitis.Human Breast Milk and Infant Formulas Differentially Modify the Intestinal Microbiota in Human Infants and Host Physiology in Rats.Deconstruction of O-glycosylation--GalNAc-T isoforms direct distinct subsets of the O-glycoproteome.Mucin-type O-glycans and their roles in intestinal homeostasis.The role of glycosylation in IBD.Mucus layers in inflammatory bowel disease.Targeted methods for quantitative analysis of protein glycosylation.Simple sugars to complex disease--mucin-type O-glycans in cancer.The Densely O-Glycosylated MUC2 Mucin Protects the Intestine and Provides Food for the Commensal Bacteria.The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation.Activity Detection of GalNAc Transferases by Protein-Based Fluorescence Sensors In Vivo.Epithelial Barrier Function in Gut-Bone Signaling.Contribution of bacterial pathogens to evoking serological disease markers and aggravating disease activity in rheumatoid arthritis.Intestinal Muc2 mucin O-glycosylation is affected by microbiota and regulated by differential expression of glycosyltranferases.Presence of commensal house dust mite allergen in human gastrointestinal tract: a potential contributor to intestinal barrier dysfunction.
P2860
Q26747722-984E9B45-003E-495D-9A64-2A4AAC5507A1Q26771122-4312E4A2-1A0E-4E8E-8BE1-0A39155FADECQ26825483-EC9F1C8D-9A7A-4F7D-BA40-46036A5D37D7Q26998404-F8026165-1B97-4FD7-AC53-200C7936D8DCQ27010149-71624A3D-68D4-4C50-83A6-ECE4E5FA9AC4Q33611054-FB809452-FCD5-4684-B999-446666E74183Q34157647-0AE7FC0E-E4F4-4C96-9925-CDB232C2264CQ34385980-4D2A46B3-B4D7-4655-90EE-029D42FA7EF9Q34431015-7A7FFA1B-CB53-45B1-B6A5-F66B0B05D959Q34636909-F307BBE4-746B-415D-8EFC-8C46D1E4545CQ34669466-9A4088DA-A542-4F97-9AF1-A86551C32C5CQ34798439-BE7066AC-DC0B-4CEF-86C6-B1B7C5FABC7EQ35048981-0E8528AD-7AB5-45FA-8D62-89ECD2EFD608Q35084532-97881313-C256-4EB7-9D57-A3A56E118332Q35541605-8255F641-7870-465F-B36D-C30AC32EEF28Q35687994-633462C3-5F0B-45A1-A1B5-FB8851FF2AECQ35870699-461C1D59-A85F-461A-AF4A-100A358422D5Q36410184-C4B67F15-B3EA-4D40-9549-272600DC4DF5Q37380400-CCDA29D7-5761-4694-B603-28D287C5FFFEQ38218832-41F06BFA-BA9A-478D-B6DB-32BD41206AECQ38229690-62D06B6D-301E-4097-ABE6-73EA1C145F20Q38293204-7CBCEEF1-0999-4D66-8671-E6840C2BA8AAQ38366325-6F1DD393-9F4F-4751-81F2-F722CA644B25Q38734952-CFF0AD94-944A-4686-AAE8-62D85FFD5941Q41047615-5836F0C5-6EB7-4B40-AC3C-BFCDA4D29B15Q41321273-53566A81-796A-4D8B-B963-C995F5374FA4Q47129733-7C7822AE-E109-4E35-8E9A-3D04BBA5AF70Q48097598-FF1E6E42-8FFE-4E4F-9142-898E1DC24EF2Q51168862-15991087-4447-417C-A0C4-2723AF6A7B09Q51567089-292F21E1-C16D-42F5-9789-B65D2296C0D0
P2860
Site-specific O-glycosylation on the MUC2 mucin protein inhibits cleavage by the Porphyromonas gingivalis secreted cysteine protease (RgpB).
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Site-specific O-glycosylation ...... eted cysteine protease (RgpB).
@en
type
label
Site-specific O-glycosylation ...... eted cysteine protease (RgpB).
@en
prefLabel
Site-specific O-glycosylation ...... eted cysteine protease (RgpB).
@en
P2093
P2860
P50
P356
P1476
Site-specific O-glycosylation ...... reted cysteine protease (RgpB)
@en
P2093
Gunnar Dahlén
Henrik Clausen
Malene B Vester-Christensen
Malin Bäckström
P2860
P304
14636-14646
P356
10.1074/JBC.M113.459479
P407
P50
P577
2013-04-01T00:00:00Z