Joshua L. Andersen
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View article: Multiomics combined with machine learning defines unique molecular subtypes of cholangiocarcinoma and identifies TNK1 as a therapeutic target
Multiomics combined with machine learning defines unique molecular subtypes of cholangiocarcinoma and identifies TNK1 as a therapeutic target Open
Background and Aims: Cholangiocarcinoma (CCA) is one of the most lethal cancers, characterized by molecular heterogeneity and treatment resistance. To uncover new biological signals and therapeutic opportunities, we employed multiomic char…
View article: Characterization of the BRAF interactome identifies BRAF<sup>V600E</sup><=>TP53 interaction in melanoma
Characterization of the BRAF interactome identifies BRAF<sup>V600E</sup><=>TP53 interaction in melanoma Open
Melanoma is a highly aggressive and frequently metastatic cancer with its incidence reported to be on the rise. Although most oncogenic drivers in melanoma converge on activation of the RAS>RAF>MEK>ERK MAPK signaling pathway, not all MAPK-…
View article: Abstract 1139 Shedding light on the dark kinome: Elucidating the regulation and physiological function of an odd tyrosine kinase
Abstract 1139 Shedding light on the dark kinome: Elucidating the regulation and physiological function of an odd tyrosine kinase Open
View article: dataset 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary dataset 2. Driver mutations identified using ML method that are not included in the training data set.
View article: Supplementary Figure 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
DriverMutPTM application predicts potential PTM disrupting driver mutations.
View article: Supplementary Figure 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
ACK1 frameshift mutatants have similar RNA expression levels as ACK1 WT.
View article: dataset 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary data set 4. PTMs disrupting potential missense driver mutations.
View article: dataset 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary data set 3. Potential dominant and co-drivers identified my the ML approach.
View article: Supplementary Figure 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Comparison of ACK1 WT and mutants by phospho-substrate protein array.
View article: Supplementary Figure 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Machine learning model predicts cancer driver mutations.
View article: dataset 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary dataset 1. Potential driver mutations identified against cancer types.
View article: dataset 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary dataset 2. Driver mutations identified using ML method that are not included in the training data set.
View article: Data from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Data from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Beyond the most common oncogenes activated by mutation (mut-drivers), there likely exists a variety of low-frequency mut-drivers, each of which is a possible frontier for targeted therapy. To identify new and understudied mut-drivers, we d…
View article: Supplementary Figure 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Machine learning model predicts cancer driver mutations.
View article: dataset 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary data set 3. Potential dominant and co-drivers identified my the ML approach.
View article: Supplementary Figure 5 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 5 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
ACK1 P633* and UBA truncation is stabilizes ACK1.
View article: dataset 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary data set 4. PTMs disrupting potential missense driver mutations.
View article: Data from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Data from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Beyond the most common oncogenes activated by mutation (mut-drivers), there likely exists a variety of low-frequency mut-drivers, each of which is a possible frontier for targeted therapy. To identify new and understudied mut-drivers, we d…
View article: Supplementary Figure 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 3 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
ACK1 frameshift mutatants have similar RNA expression levels as ACK1 WT.
View article: dataset 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
dataset 1 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Supplementary dataset 1. Potential driver mutations identified against cancer types.
View article: Supplementary Figure 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 4 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Comparison of ACK1 WT and mutants by phospho-substrate protein array.
View article: Supplementary Figure 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 2 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
DriverMutPTM application predicts potential PTM disrupting driver mutations.
View article: Supplementary Figure 5 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Supplementary Figure 5 from Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
ACK1 P633* and UBA truncation is stabilizes ACK1.
View article: Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation
Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation Open
Beyond the most common oncogenes activated by mutation (mut-drivers), there likely exists a variety of low-frequency mut-drivers, each of which is a possible frontier for targeted therapy. To identify new and understudied mut-drivers, we d…
View article: Fusion crystallization reveals the behavior of both the 1TEL crystallization chaperone and the TNK1 UBA domain
Fusion crystallization reveals the behavior of both the 1TEL crystallization chaperone and the TNK1 UBA domain Open
View article: Data‐Dependent Acquisition with Precursor Coisolation Improves Proteome Coverage and Measurement Throughput for Label‐Free Single‐Cell Proteomics**
Data‐Dependent Acquisition with Precursor Coisolation Improves Proteome Coverage and Measurement Throughput for Label‐Free Single‐Cell Proteomics** Open
We combined efficient sample preparation and ultra‐low‐flow liquid chromatography with a newly developed data acquisition and analysis scheme termed wide window acquisition (WWA) to quantify >3,000 proteins from single cells in rapid label…
View article: Fusion crystallization reveals the behavior of both the 1TEL crystallization chaperone and the TNK1 UBA domain
Fusion crystallization reveals the behavior of both the 1TEL crystallization chaperone and the TNK1 UBA domain Open
Summary Human thirty-eight-negative kinase-1 (TNK1) is implicated in cancer progression. The TNK1-UBA domain binds polyubiquitin and plays a regulatory role in TNK1 activity and stability. Sequence analysis suggests an unusual architecture…
View article: Supplementary Table 8 from SIRT5 Is a Druggable Metabolic Vulnerability in Acute Myeloid Leukemia
Supplementary Table 8 from SIRT5 Is a Druggable Metabolic Vulnerability in Acute Myeloid Leukemia Open
Plasmids.
View article: Supplementary Table 1 from SIRT5 Is a Druggable Metabolic Vulnerability in Acute Myeloid Leukemia
Supplementary Table 1 from SIRT5 Is a Druggable Metabolic Vulnerability in Acute Myeloid Leukemia Open
Patient sample information.
View article: Supplementary Table 1 from SIRT5 Is a Druggable Metabolic Vulnerability in Acute Myeloid Leukemia
Supplementary Table 1 from SIRT5 Is a Druggable Metabolic Vulnerability in Acute Myeloid Leukemia Open
Patient sample information.