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COMPARISON OF MACHINE LEARNING TECHNIQUES FOR PREDICTING NLR PROTEINS

Biomedical Engineering: Applications, Basis and Communications, 2022
The nucleotide-binding domain leucine-rich repeat-containing (NLR) proteins plays significant role in the intestinal tissue repair and innate immunity. It recently added to the members of innate immunity effectors molecules. It also plays an essential role in intestinal microbiota and recently emerged as a crucial hit for developing ulcerative colitis
null Nadia   +2 more
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Functional diversification of structurally alike NLR proteins in plants

Plant Science, 2018
In due course of evolution many pathogens alter their effector molecules to modulate the host plants' metabolism and immune responses triggered upon proper recognition by the intracellular nucleotide-binding oligomerization domain containing leucine-rich repeat (NLR) proteins.
Joydeep, Chakraborty   +4 more
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NACHT-LRR proteins (NLRs) in bacterial infection and immunity

Trends in Microbiology, 2005
Eukaryotes have evolved systems to detect bacterial intrusion. Recognition of bacteria relies on the sensing of pathogen associated molecular patterns (PAMPs) by host pattern recognition molecules (PRMs), which include various families of leucine-rich repeat (LRR) bearing proteins in plants and animals.
Thomas A, Kufer   +2 more
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The chromatin-remodeling protein BAF60/SWP73A regulates the plant immune receptor NLRs

Cell Host & Microbe, 2021
In both plant and animal innate immune responses, surveillance of pathogen infection is mediated by membrane-associated receptors and intracellular nucleotide-binding domain and leucine-rich-repeat receptors (NLRs). Homeostasis of NLRs is under tight multilayered regulation to avoid over-accumulation or over-activation, which often leads to autoimmune ...
Chien-Yu, Huang   +7 more
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NLRs: Nucleotide-Binding Domain and Leucine-Rich-Repeat-Containing Proteins

EcoSal Plus, 2009
Eukaryotes have evolved strategies to detect microbial intrusion and instruct immune responses to limit damage from infection. Recognition of microbes and cellular damage relies on the detection of microbe-associated molecular patterns (MAMPs, also called PAMPS, or pathogen-associated molecular patterns) and so-called "danger signals" by ...
Leticia A M, Carneiro   +5 more
openaire   +2 more sources

Cytofluorometric Quantification of Cell Death Elicited by NLR Proteins

2016
Nucleotide-binding domain and leucine-rich repeat containing (NLR) proteins, also known as NOD-like receptors, are critical components of the molecular machinery that senses intracellular danger signals to initiate an innate immune response against invading pathogens or endogenous sources of hazard. The best characterized effect of NLR signaling is the
Valentina, Sica   +4 more
openaire   +2 more sources

The role of NLR proteins in Leishmaniasis

2018
<p>Leishmania species are vector-borne protozoan parasites that cause a spectrum of human diseases, with an estimated 12 million people infected in 88 countries. Inflammation plays distinct roles in the different clinical syndromes. Visceral leishmaniasis, in which parasites migrate from the site of infection and proliferate in liver and spleen ...
Gwendolyn Mary Clay   +5 more
openaire   +1 more source

Tsw: an NLR protein that keeps viruses away

Plant Cell Reports, 2023
Priya Gahlowt   +3 more
openaire   +2 more sources

Balanced plant helper NLR activation by a modified host protein complex

Nature
Nucleotide-binding leucine-rich repeat (NLR) receptors play crucial roles in plant immunity by sensing pathogen effectors1. In Arabidopsis, certain sensor NLRs function as NADases to catalyse the production of second messengers2,3, which can be recognized by enhanced disease susceptibility 1 (EDS1) with its partner senescence-associated gene 101 ...
Shijia Huang   +12 more
openaire   +3 more sources

Transfer and modification of NLR proteins for virus resistance in plants

Current Opinion in Virology, 2017
NLR proteins confer resistance to multiple types of biotrophic pathogens, including viruses. NLRs are highly variable in sequence, suggesting that they are under selection pressure, but also that they may be manipulated to generate proteins with new recognition specificities.
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