multiple sequence alignment software bioedit 7 2 Search Results


bioedit 7 2  (Bioedit Company)
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Bioedit Company bioedit 7 2
Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure B and D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
Bioedit 7 2, supplied by Bioedit Company, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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bioedit 7 2 - by Bioz Stars, 2026-05
86/100 stars
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multiple sequence alignment software bioedit 7 2  (Bioedit Company)
86
Bioedit Company multiple sequence alignment software bioedit 7 2
Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure B and D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
Multiple Sequence Alignment Software Bioedit 7 2, supplied by Bioedit Company, 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/result/multiple sequence alignment software bioedit 7 2/product/Bioedit Company
Average 86 stars, based on 1 article reviews
multiple sequence alignment software bioedit 7 2 - by Bioz Stars, 2026-05
86/100 stars
  Buy from Supplier

Image Search Results


Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure B and D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.

Journal: International Journal of Biological Sciences

Article Title: Budding Yeast Ubiquitin Ligases Rad5 and Rad18 Bind a Novel PCNA Surface, which Is Required for their Functions in DNA-Damage Tolerance

doi: 10.7150/ijbs.124441

Figure Lengend Snippet: Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure B and D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.

Article Snippet: Multiple alignments were performed and presented by BioEdit 7.2 ( https://bioedit.software.informer.com/7.2/ ).

Techniques: Sequencing, Binding Assay, Y2H Assay, Mutagenesis