R
Rahul Chadda
Researcher at Washington University in St. Louis
Publications - 33
Citations - 2142
Rahul Chadda is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Lipid bilayer & Chemistry. The author has an hindex of 14, co-authored 21 publications receiving 1871 citations. Previous affiliations of Rahul Chadda include National Centre for Biological Sciences & University of Washington.
Papers
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Journal ArticleDOI
Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
Matthew Kirkham,Akikazu Fujita,Rahul Chadda,Susan J. Nixon,Teymuras V. Kurzchalia,Deepak Sharma,Richard E. Pagano,John F. Hancock,Satyajit Mayor,Robert G. Parton +9 more
TL;DR: Using quantitative light microscopy and a modified immunoelectron microscopic technique, the entry pathway of the cholera toxin binding subunit (CTB) in primary embryonic fibroblasts is characterized and the major carriers involved in initial entry of CTB were identified as uncoated tubular or ring-shaped structures.
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Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity.
Debanjan Goswami,Kripa Gowrishankar,Sameera Bilgrami,Subhasri Ghosh,Riya Raghupathy,Rahul Chadda,Ram A. Vishwakarma,Madan Rao,Madan Rao,Satyajit Mayor +9 more
TL;DR: A unique mechanism of complexation of cell-surface molecules regulated by cortical actin activity is suggested, with a nonrandom spatial distribution of nanoclusters, concentrated in optically resolvable domains.
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Dynamic Organizing Principles of the Plasma Membrane that Regulate Signal Transduction: Commemorating the Fortieth Anniversary of Singer and Nicolson's Fluid-Mosaic Model
Akihiro Kusumi,Takahiro K. Fujiwara,Rahul Chadda,Min Xie,Taka A. Tsunoyama,Ziya Kalay,Rinshi S. Kasai,Kenichi G. N. Suzuki +7 more
TL;DR: It is proposed that the cooperative action of the hierarchical three-tiered mesoscale (2-300 nm) domains--actin-membrane-skeleton induced compartments, raft domains, and dynamic protein complex domains--is critical for membrane function and distinguishes the plasma membrane from a classical Singer-Nicolson-type model.
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Cholesterol‐Sensitive Cdc42 Activation Regulates Actin Polymerization for Endocytosis via the GEEC Pathway
TL;DR: Using total internal reflection fluorescence microscopy at the single‐molecule scale, it is found that mild cholesterol depletion alters the dynamics of actin polymerization at the cell surface by inhibiting Cdc42 activation and consequently its stabilization at thecell surface.
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Raft-based interactions of gangliosides with a GPI-anchored receptor
Naoko Komura,Naoko Komura,Kenichi G. N. Suzuki,Kenichi G. N. Suzuki,Hiromune Ando,Hiromune Ando,Miku Konishi,Miku Konishi,Machi Koikeda,Akihiro Imamura,Rahul Chadda,Takahiro K. Fujiwara,Hisae Tsuboi,Ren Sheng,Wonhwa Cho,Koichi Furukawa,Keiko Furukawa,Yoshio Yamauchi,Hideharu Ishida,Akihiro Kusumi,Akihiro Kusumi,Makoto Kiso,Makoto Kiso +22 more
TL;DR: Methods for systematically synthesizing analogs that behave like their native counterparts in regard to partitioning into raft-related membrane domains or preparations show that gangliosides continually and dynamically exchange between raft domains and the bulk domain, indicating that raft domains are dynamic entities.