Cell biology, Biochemistry, C2 domain, Peripheral membrane protein and Phosphatidylserine are his primary areas of study. He has included themes like Membrane and Cytosol in his Cell biology study. His biological study spans a wide range of topics, including Biophysics and Stereochemistry.
His C2 domain study combines topics in areas such as Nuclear membrane, Plasma protein binding, Protein kinase A, Cell membrane and Protein kinase C. His Peripheral membrane protein research integrates issues from Membrane binding, Mitochondrial membrane transport protein and Function. His Phosphatidylserine research incorporates elements of Phosphatidylinositol, PX domain and Phosphatidic acid.
The scientist’s investigation covers issues in Cell biology, VP40, Biochemistry, Viral matrix protein and Biophysics. The study incorporates disciplines such as C2 domain, Cell membrane and Peripheral membrane protein in addition to Cell biology. His work deals with themes such as Virus Release, Marburg virus, Host cell plasma membrane and Viral budding, which intersect with Viral matrix protein.
His Biophysics research is multidisciplinary, incorporating elements of Liposome, Phosphatidylserine, Mutant, Membrane and Membrane curvature. His research integrates issues of Pi and Phosphatidylinositol in his study of Membrane. His Phosphatidylinositol research is multidisciplinary, incorporating perspectives in Pleckstrin homology domain and Binding site.
Robert V. Stahelin mostly deals with Biophysics, Cell biology, VP40, Viral matrix protein and Membrane. Robert V. Stahelin interconnects Mutant, Phosphatidylserine, Cytosol, Intracellular and Membrane lipids in the investigation of issues within Biophysics. His studies deal with areas such as Amino acid and Plasmodium falciparum as well as Cell biology.
His study on VP40 is covered under Ebola virus. His Viral matrix protein research is multidisciplinary, relying on both Membrane fluidity, Virion assembly, Host cell plasma membrane, Viral budding and Peripheral membrane protein. His study in C2 domain and Vesicle falls under the purview of Membrane.
His primary scientific interests are in Cell biology, Biophysics, Membrane, Stem cell and Plasmodium falciparum. As part of his studies on Cell biology, Robert V. Stahelin often connects relevant subjects like Peptide. The Biophysics study combines topics in areas such as Bioorganic chemistry, Phosphatidylserine binding, Phosphatidylserine, Lactadherin and Biosensor.
His Membrane study integrates concerns from other disciplines, such as VP40 and Ebola virus. The concepts of his Stem cell study are interwoven with issues in Cancer research and Ceramide kinase. His Plasmodium falciparum research incorporates themes from Mutation, Unfolded protein response and Proteostasis.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Membrane-protein interactions in cell signaling and membrane trafficking.
Wo nhwa Cho;Robert V. Stahelin.
Annual Review of Biophysics and Biomolecular Structure (2005)
A molecular mechanism of artemisinin resistance in Plasmodium falciparum malaria
Alassane Mbengue;Souvik Bhattacharjee;Trupti Pandharkar;Haining Liu.
Binding of the PX domain of p47phox to phosphatidylinositol 3,4‐bisphosphate and phosphatidic acid is masked by an intramolecular interaction
Dimitrios Karathanassis;Robert V. Stahelin;Jerónimo Bravo;Olga Perisic.
The EMBO Journal (2002)
Membrane binding and subcellular targeting of C2 domains.
Wonhwa Cho;Robert V. Stahelin.
Biochimica et Biophysica Acta (2006)
Sphingosine analogue drug FTY720 targets I2PP2A/SET and mediates lung tumour suppression via activation of PP2A-RIPK1-dependent necroptosis.
Sahar A. Saddoughi;Salih Gencer;Yuri K. Peterson;Katherine E. Ward.
Embo Molecular Medicine (2013)
Contrasting Membrane Interaction Mechanisms of AP180 N-terminal Homology (ANTH) and Epsin N-terminal Homology (ENTH) Domains*
Robert V. Stahelin;Fei Long;Brian J. Peter;Diana Murray.
Journal of Biological Chemistry (2003)
Phosphatidylinositol 3-Phosphate Induces the Membrane Penetration of the FYVE Domains of Vps27p and Hrs
Robert V. Stahelin;Fei Long;Karthikeyan Diraviyam;Karol S. Bruzik.
Journal of Biological Chemistry (2002)
The mechanism of membrane targeting of human sphingosine kinase 1
Robert V. Stahelin;Jeong H. Hwang;Jin Hahn Kim;Zee Yong Park.
Journal of Biological Chemistry (2005)
Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2.
Robert V. Stahelin;Wonhwa Cho.
Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains.
Bharath Ananthanarayanan;Robert V. Stahelin;Michelle A. Digman;Wonhwa Cho.
Journal of Biological Chemistry (2003)
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