ReviewChembiochem : a European journal of chemical biology2013
Dissecting the molecular basis of the role of the O-mannosylation pathway in disease: α-dystroglycan and forms of muscular dystrophy.
Review in Chembiochem : a European journal of chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed.
- Global View of Domain-Specific O-Linked Mannose Glycosylation in Glycoengineered Cells.Molecular & cellular proteomics : MCP · 2024Article
- The schizophrenia-associated variant in SLC39A8 alters protein glycosylation in the mouse brain.Molecular psychiatry · 2022Article
- Contrasting the conformational effects of α-O-GalNAc and α-O-Man glycan protein modifications and their impact on the mucin-like region of alpha-dystroglycan.Glycobiology · 2021Article
- Facile Chemoenzymatic Synthesis of O-Mannosyl Glycans.Angewandte Chemie (International ed. in English) · 2018Article
- Discovery of an O-mannosylation pathway selectively serving cadherins and protocadherins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Induction of Antibodies Directed Against Branched Core O-Mannosyl Glycopeptides-Selectivity Complimentary to the ConA Lectin.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- ProteinThe Journal of biological chemistry · 2017Article
- Differentiation-related glycan epitopes identify discrete domains of the muscle glycocalyx.Glycobiology · 2016Article
- ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol phosphate onto α-dystroglycan.Nature communications · 2016Article
- Four-week rapamycin treatment improves muscular dystrophy in a fukutin-deficient mouse model of dystroglycanopathy.Skeletal muscle · 2016Article
- Article
- Chemoenzymatic synthesis of α-dystroglycan core M1 O-mannose glycans.Chemical communications (Cambridge, England) · 2015Article
- Mucin-Type O-Glycosylation in Invertebrates.Molecules (Basel, Switzerland) · 2015Review
- Intrafamilial variability in GMPPB-associated dystroglycanopathy: Broadening of the phenotype.Neurology · 2015Article
- Article
- Genetic Engineering of Dystroglycan in Animal Models of Muscular Dystrophy.BioMed research international · 2015Review
- B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan.eLife · 2014Article
- Development of rabbit monoclonal antibodies for detection of alpha-dystroglycan in normal and dystrophic tissue.PloS one · 2014Article
- The promiscuous binding pocket of SLC35A1 ensures redundant transport of CDP-ribitol to the Golgi.The Journal of biological chemistryArticle
- Distribution of myosin heavy chain isoforms in muscular dystrophy: insights into disease pathology.Musculoskeletal regenerationArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Dystroglycanopathies form a subgroup of muscular dystrophies that arise from defects in enzymes that are implicated in the recently elucidated O-mannosylation pathway, thereby resulting in underglycosylation of α-dystroglycan. The emerging identification of additional brain proteins modified by O-mannosylation provides a broader context for interpreting the range of neurological consequences associated with dystroglycanopathies. This form of glycosylation is associated with protein mucin-like domains that present numerous serine and threonine residues as possible sites for modification. Furthermore, the O-Man glycans coexist in this region with O-GalNAc glycans (conventionally associated with such protein sequences), thus resulting in a complex glycoconjugate landscape. Sorting out the relationships between the various molecular defects in glycosylation and the modes of disease presentation, as well as the regulatory interplay among the O-Man glycans and the effects on other modes of glycosylation in the same domain, is challenging. Here we provide a perspective on chemical biology approaches employing synthetic and analytical methods to address these questions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.