Reposted by Nicole Kabella
Did you ever come across a phosphosite in your proteomics data for which nothing was known? - I bet so!
We have developed a new strategy termed "potency coherence analysis" that leverages the drug potency dimension in decryptM to decode the kinases that shape the human phosphoproteome.
Read more:
We have developed a new strategy termed "potency coherence analysis" that leverages the drug potency dimension in decryptM to decode the kinases that shape the human phosphoproteome.
Read more:
Chemical proteomics decrypts the kinases that shape the dynamic human phosphoproteome
Mass-spectrometry-based phosphoproteomics enables the analysis of thousands of protein phosphorylation events across the human proteome. However, there is a lack of scalable, hypothesis-free, and stat...
doi.org
November 19, 2025 at 10:43 AM
Did you ever come across a phosphosite in your proteomics data for which nothing was known? - I bet so!
We have developed a new strategy termed "potency coherence analysis" that leverages the drug potency dimension in decryptM to decode the kinases that shape the human phosphoproteome.
Read more:
We have developed a new strategy termed "potency coherence analysis" that leverages the drug potency dimension in decryptM to decode the kinases that shape the human phosphoproteome.
Read more:
Reposted by Nicole Kabella
New preprint 🚨 We systematically measured 17 million phospho-specific dose-response curves (133 kinase inhibitors × 5 cell lines) to decrypt the kinases that shape the human phosphoproteome. We show that drug perturbation potency (not effect size) links kinases to substrates while controlling FDR.
Did you ever come across a phosphosite in your proteomics data for which nothing was known? - I bet so!
We have developed a new strategy termed "potency coherence analysis" that leverages the drug potency dimension in decryptM to decode the kinases that shape the human phosphoproteome.
Read more:
We have developed a new strategy termed "potency coherence analysis" that leverages the drug potency dimension in decryptM to decode the kinases that shape the human phosphoproteome.
Read more:
Chemical proteomics decrypts the kinases that shape the dynamic human phosphoproteome
Mass-spectrometry-based phosphoproteomics enables the analysis of thousands of protein phosphorylation events across the human proteome. However, there is a lack of scalable, hypothesis-free, and stat...
doi.org
November 20, 2025 at 11:59 AM
New preprint 🚨 We systematically measured 17 million phospho-specific dose-response curves (133 kinase inhibitors × 5 cell lines) to decrypt the kinases that shape the human phosphoproteome. We show that drug perturbation potency (not effect size) links kinases to substrates while controlling FDR.
Reposted by Nicole Kabella
How can we reform science? I have some ideas. But I am not sure you’ll like them, because they don’t promise much. elevanth.org/blog/2025/07...
Which Kind of Science Reform
What hope is there for science reform, if we can't agree on what to reform? Right now, principles are more important than practices.
elevanth.org
July 9, 2025 at 1:40 PM
How can we reform science? I have some ideas. But I am not sure you’ll like them, because they don’t promise much. elevanth.org/blog/2025/07...
Reposted by Nicole Kabella
Excited to share our latest work published in #ScienceSignaling! 🚀
www.science.org/doi/10.1126/...
(1/4)
www.science.org/doi/10.1126/...
(1/4)
Proteomic analyses identify targets, pathways, and cellular consequences of oncogenic KRAS signaling
Proteomic analyses offer insights into how KRAS inhibitors affect oncogenic KRAS signaling.
www.science.org
July 31, 2025 at 8:10 AM
Excited to share our latest work published in #ScienceSignaling! 🚀
www.science.org/doi/10.1126/...
(1/4)
www.science.org/doi/10.1126/...
(1/4)