kinases alk (Carna Inc)
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95
Structured Review
Carna Inc
kinases alk
Kinases Alk, supplied by Carna Inc, used in various techniques. Bioz Stars score: 95/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/kinases+alk/bio_rxiv__2025__07__04__663216-187-1-15?v=Carna+Inc
Average 95 stars, based on 24 article reviews
Kinases Alk, supplied by Carna Inc, used in various techniques. Bioz Stars score: 95/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/kinases+alk/bio_rxiv__2025__07__04__663216-187-1-15?v=Carna+Inc
Average 95 stars, based on 24 article reviews
kinases alk - by Bioz Stars,
2026-07
95/100 stars
Images
1) Product Images from "A Computational Workflow for Structure-Guided Design of Potent and Selective Kinase Peptide Substrates"
Article Title: A Computational Workflow for Structure-Guided Design of Potent and Selective Kinase Peptide Substrates
Journal: bioRxiv
doi: 10.1101/2025.07.04.663216
Figure Legend Snippet: Experimental validation of designed peptides shows improved kinase activity. ( A ) ADP-Glo assay baseline measurements showing kinase activity with parental substrates and background controls for all five tested kinases. ( B–F ) Relative percentage change in kinase activity for designed peptides compared to parental substrates for ALK ( B ), MET ( C ), ROS1 ( D ), EGFR L858R ( E ), and SRC ( F ). Designed peptides are color-coded with sequence information provided. Phosphosite residues that were fixed during design are highlighted in green. Four out of five kinases showed substantial activity improvements with at least one designed peptide.
Techniques Used: Biomarker Discovery, Activity Assay, Glo Assay, Sequencing, Phospho-proteomics
Figure Legend Snippet: Kinetic characterization reveals improved binding affinity of designed peptides. ( A ) Schematic of kinase phosphorylation reaction monitored by the LIMS-kinase assay. ( B ) Multiple reaction monitoring (MRM) setup showing the mass spectrometry detection pathway for ADP quantification. ( C–E ) Michaelis-Menten kinetic analysis comparing parental and optimized peptides for ROS1 ( C ), MET ( D ), and ALK ( E ). Left panels show time-course data at varying substrate concentrations; right panels show saturation curves with fitted K m values and 95% confidence intervals. The designed peptides demonstrated lower K m values, indicating improved apparent binding affinity.
Techniques Used: Binding Assay, Phospho-proteomics, Kinase Assay, Targeted Proteomics, Mass Spectrometry
Figure Legend Snippet: Structural analysis reveals molecular basis for improved activity. ( A-D ) Comparison of AlphaFold-Multimer predicted structures and hydrogen bonding networks for parental (green) versus designed (yellow) peptides in complex with ALK ( A ), ROS1 ( B ), MET ( C ), and EGFR L858R ( D ). Kinase structures are shown in gray ribbon representation. Green boxes highlight hydrogen bond interactions formed by parental peptides; yellow boxes show interactions formed by designed peptides. Designed peptides generally form additional or optimized hydrogen bonds that correlate with improved experimental activity.
Techniques Used: Activity Assay, Comparison