ArticleBMC immunology2009
Understanding diversity of human innate immunity receptors: analysis of surface features of leucine-rich repeat domains in NLRs and TLRs.
Article in BMC immunology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- Unconventional posttranslational modification in innate immunity.Cellular and molecular life sciences : CMLS · 2024Review
- LRRC15 inhibits SARS-CoV-2 cellular entry in trans.PLoS biology · 2022Article
- Bioinformatics Approaches for Analyzing Multigene Families Encoding Immune Receptors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- LRRC15 is an inhibitory receptor blocking SARS-CoV-2 spike-mediated entrybioRxiv : the preprint server for biology · 2021Article
- Pathophysiological Implication of Pattern Recognition Receptors in Fetal Membranes Rupture: RAGE and NLRP Inflammasome.Biomedicines · 2021Review
- Inflammation and tumor progression: signaling pathways and targeted intervention.Signal transduction and targeted therapy · 2021Article
- Structure and Emerging Functions of LRCH Proteins in Leukocyte Biology.Frontiers in cell and developmental biology · 2020Review
- Bacterial Derived Carbohydrates Bind Cyr1 and Trigger Hyphal Growth in Candida albicans.ACS infectious diseases · 2018Article
- Biocomputational analysis of evolutionary relationship between toll-like receptor and nucleotide-binding oligomerization domain-like receptors genes.Veterinary world · 2016Article
- Compartmentalizing intestinal epithelial cell toll-like receptors for immune surveillance.Cellular and molecular life sciences : CMLS · 2015Review
- Consensus design of a NOD receptor leucine rich repeat domain with binding affinity for a muramyl dipeptide, a bacterial cell wall fragment.Protein science : a publication of the Protein Society · 2014Article
- The characterization of sponge NLRs provides insight into the origin and evolution of this innate immune gene family in animals.Molecular biology and evolution · 2014Article
- NLRC5, at the Heart of Antigen Presentation.Frontiers in immunology · 2013Review
- A molecular model of the full-length human NOD-like receptor family CARD domain containing 5 (NLRC5) protein.BMC bioinformatics · 2013Article
- Article
- Ecrg4 attenuates the inflammatory proliferative response of mucosal epithelial cells to infection.PloS one · 2013Article
- Computational analysis predicts the Kaposi's sarcoma-associated herpesvirus tegument protein ORF63 to be alpha helical.Proteins · 2012Article
- Development of a Grp94 inhibitor.Journal of the American Chemical Society · 2012Article
- Inhibitor of growth-4 mediates chromatin modification and has a suppressive effect on tumorigenesis and innate immunity.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2012Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe human innate immune system uses a system of extracellular Toll-like receptors (TLRs) and intracellular Nod-like receptors (NLRs) to match the appropriate level of immune response to the level of threat from the current environment. Almost all NLRs and TLRs have a domain consisting of multiple leucine-rich repeats (LRRs), which is believed to be involved in ligand binding. LRRs, found also in thousands of other proteins, form a well-defined "horseshoe"-shaped structural scaffold that can be used for a variety of functions, from binding specific ligands to performing a general structural role. The specific functional roles of LRR domains in NLRs and TLRs are thus defined by their detailed surface features. While experimental crystal structures of four human TLRs have been solved, no structure data are available for NLRs.
resultsWe report a quantitative, comparative analysis of the surface features of LRR domains in human NLRs and TLRs, using predicted three-dimensional structures for NLRs. Specifically, we calculated amino acid hydrophobicity, charge, and glycosylation distributions within LRR domain surfaces and assessed their similarity by clustering. Despite differences in structural and genomic organization, comparison of LRR surface features in NLRs and TLRs allowed us to hypothesize about their possible functional similarities. We find agreement between predicted surface similarities and similar functional roles in NLRs and TLRs with known agonists, and suggest possible binding partners for uncharacterized NLRs.
conclusionDespite its low resolution, our approach permits comparison of molecular surface features in the absence of crystal structure data. Our results illustrate diversity of surface features of innate immunity receptors and provide hints for function of NLRs whose specific role in innate immunity is yet unknown.
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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.