gene editing Search Results


94
TargetMol small molecule database
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Small Molecule Database, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/High-Efficiency+Gene+Editing+Small+Molecule+Library/pmc10100900-226-6-10
Average 94 stars, based on 1 article reviews
small molecule database - by Bioz Stars, 2026-11
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94
Hera BioLabs piggybac transposase
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Piggybac Transposase, supplied by Hera BioLabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
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96
Nepa Gene Co Ltd cuy21 pro vitro
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Cuy21 Pro Vitro, supplied by Nepa Gene Co Ltd, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/CUY21EDIT+Electroporator/pm24416124-276-38-40
Average 96 stars, based on 1 article reviews
cuy21 pro vitro - by Bioz Stars, 2026-11
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86
Revivicor inc revivicor 10 gene edited pig
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Revivicor 10 Gene Edited Pig, supplied by Revivicor inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/10+gene+edit+pig+donor/pm39349802-38-44-44
Average 86 stars, based on 1 article reviews
revivicor 10 gene edited pig - by Bioz Stars, 2026-11
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90
Cellectis sa genome editing
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Genome Editing, supplied by Cellectis sa, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/gene+editing/pmc05240599-61-4-26
Average 90 stars, based on 1 article reviews
genome editing - by Bioz Stars, 2026-11
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90
Desktop Genetics gene-editing frequency assay
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Gene Editing Frequency Assay, supplied by Desktop Genetics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/gene+editing+frequency+assay/pmc07114625-226-16-8
Average 90 stars, based on 1 article reviews
gene-editing frequency assay - by Bioz Stars, 2026-11
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90
Allen Institute for Cell Science gene-edited hips cell lines
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Gene Edited Hips Cell Lines, supplied by Allen Institute for Cell Science, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/gene+edited+hips+cell+lines/pmc06838938__mmc9-309-15-4
Average 90 stars, based on 1 article reviews
gene-edited hips cell lines - by Bioz Stars, 2026-11
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90
Biomedical Technologies crispr-cas9
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Crispr Cas9, supplied by Biomedical Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/gene+editing/pmc08074506-58-6-3
Average 90 stars, based on 1 article reviews
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90
Gene Codes Inc sequence editing software sequencher 3.0
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Sequence Editing Software Sequencher 3.0, supplied by Gene Codes Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/sequence+editing+software+sequencher+3+0/10__1111_slash_zsc__12015-102-13-18
Average 90 stars, based on 1 article reviews
sequence editing software sequencher 3.0 - by Bioz Stars, 2026-11
90/100 stars
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90
Vertex Pharmaceuticals gene editing therapies
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Gene Editing Therapies, supplied by Vertex Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
gene editing therapies - by Bioz Stars, 2026-11
90/100 stars
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90
Waisman Biomanufacturing imaging and hpsc/gene editing cores
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Imaging And Hpsc/Gene Editing Cores, supplied by Waisman Biomanufacturing, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/imaging+and+hpsc+gene+editing+cores/pmc09669399__mmc2-199-23-23
Average 90 stars, based on 1 article reviews
imaging and hpsc/gene editing cores - by Bioz Stars, 2026-11
90/100 stars
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90
Sangamo Inc gene-edited cells
Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to <t>a</t> <t>small-molecule</t> pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.
Gene Edited Cells, supplied by Sangamo Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gene+editing/gene+editing/pm26560278-29-17-2
Average 90 stars, based on 1 article reviews
gene-edited cells - by Bioz Stars, 2026-11
90/100 stars
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Image Search Results


Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to a small-molecule pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.

Journal: Microbiology Spectrum

Article Title: Virtual Screening and In Vitro Experimental Verification of LuxS Inhibitors for Escherichia coli O157:H7

doi: 10.1128/spectrum.03502-22

Figure Lengend Snippet: Structure of LuxS protein of E. coli . (A) The pocket (red) of LuxS protein binds to a small-molecule pocket. The length, width, and depth of the pocket are 21.33, 26.50, and 18.67 Å, respectively. (B) The amino acids in the small-molecule binding pocket of the sequence are labeled red. (C) In the pocket attribute, the red part is the metal-binding site, and the green part was the methionine-binding site.

Article Snippet: The ChemDiv database, a commercially available small-molecule database from Shanghai TopScience Biotechnology Co. with more than 1 million compounds, was used as the screening library.

Techniques: Binding Assay, Sequencing, Labeling