Works (4)

Updated: July 5th, 2023 15:37

2019 journal article

An Autoinducer Analogue Reveals an Alternative Mode of Ligand Binding for the LasR Quorum-Sensing Receptor

ACS CHEMICAL BIOLOGY, 14(3), 378–389.

MeSH headings : 4-Butyrolactone / analogs & derivatives; 4-Butyrolactone / chemistry; 4-Butyrolactone / metabolism; Amino Acids / chemistry; Bacterial Proteins / metabolism; Escherichia coli / drug effects; Ligands; Molecular Structure; Mutation; Protein Binding; Pseudomonas aeruginosa / drug effects; Quorum Sensing / drug effects; Signal Transduction; Structure-Activity Relationship; Trans-Activators / metabolism
TL;DR: The ability of LasR to bind ligands in different conformations, and in so doing, alter their potency as agonists, could explain the difficulties that have been encountered in the development of competitive LasR inhibitors. (via Semantic Scholar)
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Source: Web Of Science
Added: April 2, 2019

2017 journal article

Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions

PLOS ONE, 12(4).

By: Z. Li n, S. Chakraborty n & G. Xu n

MeSH headings : Amino Acid Sequence; Arabidopsis Proteins / chemistry; Arabidopsis Proteins / metabolism; Binding Sites; Molecular Structure; Protein Binding; Protein Kinases / metabolism; Sequence Homology, Amino Acid
TL;DR: These studies will open different unknown avenues of TDR-TDIF signaling pathways that will enhance knowledge in this field highlighting the receptor ligand interaction, receptor activation, signaling network, modes of action and will serve as a structure function relationship model between the ligand and the receptor for various similar leucine-rich repeat receptor-like kinases (LRR-RLKs). (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2016 journal article

Structure, regulation, and inhibition of the quorum-sensing signal integrator LuxO

PLoS Biology, 14(5).

By: H. Boyaci, T. Shah, A. Hurley, B. Kokona, Z. Li, C. Ventocilla, P. Jeffrey, M. Semmelhack ...

Source: NC State University Libraries
Added: August 6, 2018

2016 journal article

X-ray crystallographic studies of the extracellular domain of the first plant ATP receptor, DORN1, and the orthologous protein from Camelina sativa

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 72, 782–787.

By: Z. Li n, S. Chakraborty n & G. Xu n

author keywords: plant ATP receptor; DORN1; lectin receptor kinase I.9; glycosylation; Arabidopsis thaliana; Camelina sativa
MeSH headings : Adenosine Triphosphate / chemistry; Adenosine Triphosphate / metabolism; Amino Acid Sequence; Arabidopsis / chemistry; Arabidopsis / metabolism; Arabidopsis Proteins / chemistry; Arabidopsis Proteins / genetics; Arabidopsis Proteins / metabolism; Baculoviridae / genetics; Baculoviridae / metabolism; Brassicaceae / chemistry; Brassicaceae / metabolism; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Gene Expression; Glycosylation; Plasmids / chemistry; Plasmids / metabolism; Protein Kinases / chemistry; Protein Kinases / genetics; Protein Kinases / metabolism; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; X-Ray Diffraction
TL;DR: The extracellular domain of the A. thaliana ATP receptor DORN1 has been expressed and purified; a protein orthologous to Dorn1 from C. sativa has been crystallized and its X-ray diffraction data have been collected. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

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