Alexander Beeser
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Associate Professor of Biology
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Alexander Beeser's research focuses on molecular biology, specifically investigating the function of proteins in biological systems. His work includes mutational analyses of protein domains, such as the cysteine-rich domain of Yvh1, a protein crucial for translational competency in yeast. This research contributes to understanding fundamental biological processes at the molecular level.
Metrics
- h-index: 15
- Publications: 21
- Citations: 2,452
Selected Publications
-
Mutational Analyses of the Cysteine-Rich Domain of Yvh1, a Protein Required for Translational Competency in Yeast (2022)
-
Overexpression of eIF5 or its protein mimic 5MP perturbs eIF2 function and induces ATF4 translation through delayed re-initiation (2016)
-
ArhGAP15, a Rac-specific GTPase-activating Protein, Plays a Dual Role in Inhibiting Small GTPase Signaling (2013)
-
Emerging Roles of Atypical Dual Specificity Phosphatases in Cancer (2013)
-
Characterization of a Human Cell Line Stably Over-Expressing the Candidate Oncogene, Dual Specificity Phosphatase 12 (2011)
-
Identification of the Atypical MAPK Erk3 as a Novel Substrate for p21-activated Kinase (Pak) Activity (2011)
-
An Isoform-Selective, Small-Molecule Inhibitor Targets the Autoregulatory Mechanism of p21-Activated Kinase (2008)
-
Specificity Profiling of Pak Kinases Allows Identification of Novel Phosphorylation Sites (2007)
-
The kinase-inhibitory domain of p21-activated kinase 1 (PAK1) inhibits cell cycle progression independent of PAK1 kinase activity (2006)
-
Role of Group A p21-activated Kinases in Activation of Extracellular-regulated Kinase by Growth Factors (2005)
-
Production and use of a cell permeable inhibitor of group A Paks (TAT-PID) to analyze signal transduction (2005)
-
Vav1 Transduces T Cell Receptor Signals to the Activation of the Ras/ERK Pathway via LAT, Sos, and RasGRP1 (2004)
-
p21-Activated Kinase 5 (Pak5) Localizes to Mitochondria and Inhibits Apoptosis by Phosphorylating BAD (2003)
-
Apoptotic Phosphorylation of Histone H2B Is Mediated by Mammalian Sterile Twenty Kinase (2003)
-
Rapid Induction of Dendritic Spine Morphogenesis by trans-Synaptic EphrinB-EphB Receptor Activation of the Rho-GEF Kalirin (2003)
Collaboration Network
Top Collaborators
- Apoptotic Phosphorylation of Histone H2B Is Mediated by Mammalian Sterile Twenty Kinase
- Rapid Induction of Dendritic Spine Morphogenesis by trans-Synaptic EphrinB-EphB Receptor Activation of the Rho-GEF Kalirin
- An Isoform-Selective, Small-Molecule Inhibitor Targets the Autoregulatory Mechanism of p21-Activated Kinase
- p21-activated Kinase Links Rac/Cdc42 Signaling to Merlin
- p21-Activated Kinase 5 (Pak5) Localizes to Mitochondria and Inhibits Apoptosis by Phosphorylating BAD
Showing 5 of 12 shared publications
- The Dual-Specificity Protein Phosphatase Yvh1p Regulates Sporulation, Growth, and Glycogen Accumulation Independently of Catalytic Activity in Saccharomyces cerevisiae via the Cyclic AMP-Dependent Protein Kinase Cascade
- TheS. cerevisiae nitrogen starvation-induced Yvh1p and Ptp2p phosphatases play a role in control of sporulation
- Control of Nitrogen Catabolite Repression Is Not Affected by the tRNA Gln-CUU Mutation, Which Results in Constitutive Pseudohyphal Growth of Saccharomyces cerevisiae
- The Dual-Specificity Protein Phosphatase Yvh1p Acts Upstream of the Protein Kinase Mck1p in Promoting Spore Development in Saccharomyces cerevisiae
- Functional Domain Mapping and Subcellular Distribution of Dal82p in Saccharomyces cerevisiae
- An Isoform-Selective, Small-Molecule Inhibitor Targets the Autoregulatory Mechanism of p21-Activated Kinase
- Specificity Profiling of Pak Kinases Allows Identification of Novel Phosphorylation Sites
- An Isoform-Selective, Small-Molecule Inhibitor Targets the Autoregulatory Mechanism of p21-Activated Kinase
- Specificity Profiling of Pak Kinases Allows Identification of Novel Phosphorylation Sites
- An Isoform-Selective, Small-Molecule Inhibitor Targets the Autoregulatory Mechanism of p21-Activated Kinase
- Specificity Profiling of Pak Kinases Allows Identification of Novel Phosphorylation Sites
- p21-Activated Kinase 5 (Pak5) Localizes to Mitochondria and Inhibits Apoptosis by Phosphorylating BAD
- Role of Group A p21-activated Kinases in Activation of Extracellular-regulated Kinase by Growth Factors
- Emerging Roles of Atypical Dual Specificity Phosphatases in Cancer
- Rapid Induction of Dendritic Spine Morphogenesis by trans-Synaptic EphrinB-EphB Receptor Activation of the Rho-GEF Kalirin
- Rapid Induction of Dendritic Spine Morphogenesis by trans-Synaptic EphrinB-EphB Receptor Activation of the Rho-GEF Kalirin
- Rapid Induction of Dendritic Spine Morphogenesis by trans-Synaptic EphrinB-EphB Receptor Activation of the Rho-GEF Kalirin
- Rapid Induction of Dendritic Spine Morphogenesis by trans-Synaptic EphrinB-EphB Receptor Activation of the Rho-GEF Kalirin
- Rapid Induction of Dendritic Spine Morphogenesis by trans-Synaptic EphrinB-EphB Receptor Activation of the Rho-GEF Kalirin
- ArhGAP15, a Rac-specific GTPase-activating Protein, Plays a Dual Role in Inhibiting Small GTPase Signaling
- ArhGAP15, a Rac-specific GTPase-activating Protein, Plays a Dual Role in Inhibiting Small GTPase Signaling
- ArhGAP15, a Rac-specific GTPase-activating Protein, Plays a Dual Role in Inhibiting Small GTPase Signaling
Similar Researchers
Based on overlapping research topics