ArticleThe Journal of biological chemistry2018
LysMD3 is a type II membrane protein without an
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- The pathobiology of human fungal infections.Nature reviews. Microbiology · 2024Review
- Noninvasive Analysis of Peptidoglycan from Living Animals.Bioconjugate chemistry · 2024Article
- HOIL1 Regulates Group 3 Innate Lymphoid Cells in the Colon and Protects against Systemic Dissemination, Colonic Ulceration, and Lethality from Citrobacter rodentium Infection.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Dectin-1-Independent Macrophage Phagocytosis ofInternational journal of molecular sciences · 2023Article
- LYSMD3: A mammalian pattern recognition receptor for chitin.Cell reports · 2021Article
- Peptidoglycan Contribution to the B Cell Superantigen Activity of Staphylococcal Protein A.mBio · 2021Article
- Uptake, recognition and responses to peptidoglycan in the mammalian host.FEMS microbiology reviews · 2021Review
- Detection of fungal and bacterial carbohydrates: Do the similar structures of chitin and peptidoglycan play a role in immune dysfunction?PLoS pathogens · 2018Article
Corrections and comments
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Authors and funding
32 authors at 9 institutions in 1 country.
Funding
Abstract
Germline-encoded receptors recognizing common pathogen-associated molecular patterns are a central element of the innate immune system and play an important role in shaping the host response to infection. Many of the innate immune molecules central to these signaling pathways are evolutionarily conserved. LysMD3 is a novel molecule containing a putative peptidoglycan-binding domain that has orthologs in humans, mice, zebrafish, flies, and worms. We found that the lysin motif (LysM) of LysMD3 is likely related to a previously described peptidoglycan-binding LysM found in bacteria. Mouse LysMD3 is a type II integral membrane protein that co-localizes with GM130+ structures, consistent with localization to the Golgi apparatus. We describe here two lines of mLysMD3-deficient mice for
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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.