A
Ayyappan K. Rajasekaran
Researcher at Alfred I. duPont Hospital for Children
Publications - 70
Citations - 5722
Ayyappan K. Rajasekaran is an academic researcher from Alfred I. duPont Hospital for Children. The author has contributed to research in topics: Na+/K+-ATPase & Tight junction. The author has an hindex of 36, co-authored 70 publications receiving 5335 citations. Previous affiliations of Ayyappan K. Rajasekaran include Wilmington University & Christiana Care Health System.
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Journal ArticleDOI
Reassessing epithelial to mesenchymal transition as a prerequisite for carcinoma invasion and metastasis.
TL;DR: In this paper, the authors provide a review of these reports and describe mechanisms to explain the morphologic and molecular heterogeneity and plasticity of malignant carcinoma cells, including incomplete epithelial to mesenchymal transition (EMT), reversion to an epithelial phenotype, and collective migration.
Journal Article
Monoclonal Antibodies to the Extracellular Domain of Prostate-specific Membrane Antigen Also React with Tumor Vascular Endothelium
He Liu,Peggy Moy,Sae Kim,Yan Xia,Ayyappan K. Rajasekaran,Vincent Navarro,Beatrice S. Knudsen,Neil H. Bander +7 more
TL;DR: Competitive binding studies indicate these antibodies define two distinct, noncompeting epitopes on the extracellular domain of PSMA, which should prove useful for in vivo targeting to prostate cancer, as well as to the vascular compartment of a wide variety of carcinomas.
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A Functional Role for Intra-Axonal Protein Synthesis during Axonal Regeneration from Adult Sensory Neurons
Jun-Qi Zheng,Theresa K. Kelly,Bieshia Chang,Sergey Ryazantsev,Ayyappan K. Rajasekaran,Kelsey C. Martin,Jeffery L. Twiss +6 more
TL;DR: It is shown that axons of adult mammalian neurons can synthesize proteins and suggest that, under some circumstances, intra-axonal translation contributes to structural integrity of the growth cone in regenerating axons.
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A Novel Cytoplasmic Tail MXXXL Motif Mediates the Internalization of Prostate-specific Membrane Antigen
Sigrid A. Rajasekaran,Gopalakrishnapillai Anilkumar,Eri Oshima,James U. Bowie,He Liu,Warren D. W. Heston,Neil H. Bander,Ayyappan K. Rajasekaran +7 more
TL;DR: It is suggested that a novel MXXXL motif in the cytoplasmic tail mediates PSMA internalization, and it is shown that dominant negative micro2 of the adaptor protein (AP)-2 complex strongly inhibits the internalization of PSMA, indicating that AP-2 is involved in the internalized of PSma mediated by the M XXXL motif.
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Is prostate-specific membrane antigen a multifunctional protein?
TL;DR: It is suggested that PSMA may function as a receptor internalizing a putative ligand, an enzyme playing a role in nutrient uptake, and a peptidase involved in signal transduction in prostate epithelial cells.