S
Subashchandrabose Chinnathambi
Researcher at National Chemical Laboratory
Publications - 83
Citations - 2096
Subashchandrabose Chinnathambi is an academic researcher from National Chemical Laboratory. The author has contributed to research in topics: Tau protein & Microglia. The author has an hindex of 19, co-authored 71 publications receiving 1509 citations. Previous affiliations of Subashchandrabose Chinnathambi include Indian Institute of Science & German Center for Neurodegenerative Diseases.
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Journal ArticleDOI
Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation.
Sadasivam Jeganathan,Antje Hascher,Subashchandrabose Chinnathambi,Jacek Biernat,Eva Maria Mandelkow,Eckhard Mandelkow +5 more
TL;DR: The results provide a framework for the global folding of Tau dependent on proline-directed phosphorylation in the domains flanking the repeats and the consequences for pathological properties of Tau.
Journal ArticleDOI
Evidence for a role of the rare p.A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer's diseases
Giovanni Coppola,Subashchandrabose Chinnathambi,Jason Lee,Beth A. Dombroski,Matt Baker,Alexandra I. Soto-Ortolaza,Suzee E. Lee,Eric Klein,Alden Y. Huang,Renee L. Sears,Jessica Lane,Anna Karydas,Robert O. Kenet,Jacek Biernat,Li-San Wang,Carl W. Cotman,Charles DeCarli,Allan I. Levey,John M. Ringman,Mario F. Mendez,Helena C. Chui,Isabelle Le Ber,Isabelle Le Ber,Alexis Brice,Alexis Brice,Michelle K. Lupton,Elisavet Preza,Simon Lovestone,John Powell,Neill R. Graff-Radford,Ronald C. Petersen,Bradley F. Boeve,Carol F. Lippa,Eileen H. Bigio,Ian R. A. Mackenzie,Elizabeth Finger,Andrew Kertesz,Richard J. Caselli,Marla Gearing,Jorge L. Juncos,Bernardino Ghetti,Salvatore Spina,Yvette Bordelon,Wallace W. Tourtellotte,Matthew P. Frosch,Jean Paul Vonsattel,Chris Zarow,Thomas G. Beach,Roger L. Albin,Andrew P. Lieberman,Virginia M.-Y. Lee,John Q. Trojanowski,Vivianna M. Van Deerlin,Thomas D. Bird,Douglas Galasko,Eliezer Masliah,Charles L. White,Juan C. Troncoso,Didier Hannequin,Adam L. Boxer,Michael D. Geschwind,Satish Kumar,Eva Maria Mandelkow,Zbigniew K. Wszolek,Ryan J. Uitti,Dennis W. Dickson,Jonathan L. Haines,Richard Mayeux,Margaret A. Pericak-Vance,Lindsay A. Farrer,Liana G. Apostolova,Steven E. Arnold,Clinton T. Baldwin,Robert Barber,M. Michael Barmada,Thomas G. Beach,Gary W. Beecham,Duane Beekly,David A. Bennett,Deborah Blacker,James D. Bowen,A. Boxer,James R. Burke,Jacqueline L. Buros,Joseph D. Buxbaum,Nigel J. Cairns,Laura B. Cantwell,Chuanhai Cao,Christopher S. Carlson,Regina M. Carney,Minerva M. Carrasquillo,Steven L. Carroll,David G. Clark,Jason J. Corneveaux,Paul K. Crane,Carlos Cruchaga,Jeffrey L. Cummings,Philip L. De Jager,Philip L. De Jager,Charles C. DeCarli,Steven T. DeKosky,F. Yesim Demirci,Ramon Diaz-Arrastia,Malcolm B. Dick,Ranjan Duara,William G. Ellis,Nilufer Ertekin-Taner,Denis A. Evans,Kelley Faber,Kenneth B. Fallon,Martin R. Farlow,Steven H. Ferris,Tatiana Foroud,Paul Gallins,Mary Ganguli,Daniel H. Geschwind,John R. Gilbert,Sid Gilman,Bruno Giordani,Jonathan D. Glass,Alison Goate,Neil Graff-Radford,Robert C. Green,John H. Growdon,Hakon Hakonarson,Ronald L. Hamilton,John Hardy,Lindy E. Harrell,Elizabeth Head,Lawrence S. Honig,Matthew J. Huentelman,Christine M. Hulette,Bradley T. Hyman,Gail P. Jarvik,Gregory A. Jicha,Lee-Way Jin,Nancy Johnson,Gyungah Jun,M. Ilyas Kamboh,Jason Karlawish,A. Karydas,John S. K. Kauwe,Jeffrey Kaye,Ronald C. Kim,Edward H. Koo,Neil W. Kowall,Patricia L. Kramer,Walter A. Kukull,James J. Lah,Eric B. Larson,Oscar L. Lopez,Kathryn L. Lunetta,Wendy J. Mack,Daniel C. Marson,Eden R. Martin,Frank Martiniuk,Deborah C. Mash,Wayne C. McCormick,Susan M. McCurry,Andrew McDavid,Ann C. McKee,M.-Marsel Mesulam,Bruce L. Miller,Carol A. Miller,Joshua W. Miller,Thomas J. Montine,John C. Morris,Amanda J. Myers,Adam C. Naj,Petra Nowotny,Joseph E. Parisi,Daniel P. Perl,Elaine R. Peskind,Wayne W. Poon,Huntington Potter,Joseph F. Quinn,Ashok Raj,Ruchita Rajbhandary,Murray A. Raskind,Eric M. Reiman,Barry Reisberg,Christiane Reitz,Erik D. Roberson,Ekaterina Rogaeva,Roger N. Rosenberg,Mary Sano,Andrew J. Saykin,Andrew J. Saykin,Julie A. Schneider,Lon S. Schneider,William W. Seeley,Michael L. Shelanski,Michael A. Slifer,Charles D. Smith,Joshua A. Sonnen,Peter St George-Hyslop,Peter St George-Hyslop,Robert S. Stern,Rudolph E. Tanzi,Debby W. Tsuang,Badri N. Vardarajan,Harry V. Vinters,Jean Paul G. Vonsattel,Sandra Weintraub,Kathleen A. Welsh-Bohmer,Jennifer Williamson,Randall L. Woltjer,Steven G. Younkin,Owen A. Ross,Rosa Rademakers,Gerard D. Schellenberg,Eckhard Mandelkow +211 more
TL;DR: These data provide the first genetic evidence and functional studies supporting the role of MAPT p.A152T as a rare risk factor for both FTD-s and AD and the concept that rare variants can increase the risk for relatively common, complex neurodegenerative diseases is suggested.
Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of
Sadasivam Jeganathan,Antje Hascher,Subashchandrabose Chinnathambi,Jacek Biernat,Eva-Maria Mandelkow,Eckhard Mandelkow +5 more
TL;DR: Jeganathan et al. as mentioned in this paper showed that the paperclip conformation becomes tighter or looser, depending on the pseudo-phosphorylation state of the protein. And they provided a framework for the global folding of Tau dependent on proline-directed phosphorylation in the domains flanking the repeats.
Journal ArticleDOI
β-sheet core of Tau paired helical filaments revealed by solid-state NMR
Venita Daebel,Subashchandrabose Chinnathambi,Jacek Biernat,Martin Schwalbe,Birgit Habenstein,Antoine Loquet,Elias Akoury,Katharina Tepper,Henrik Müller,Marc Baldus,Christian Griesinger,Markus Zweckstetter,Markus Zweckstetter,Eckhard Mandelkow,Vinesh Vijayan,Adam Lange +15 more
TL;DR: Solid-state nuclear magnetic resonance spectroscopy is applied to investigate in vitro assembled PHFs from a truncated three-repeat tau isoform (K19) that represents the core of PHFs and finds that the rigid core of the fibrils is formed by amino acids V306 to S324, only 18 out of 99 residues, and comprises three β-strands connected by two short kinks.
Journal ArticleDOI
Human Tau Isoforms Assemble into Ribbon-like Fibrils That Display Polymorphic Structure and Stability
Susanne Wegmann,Yu Jin Jung,Subashchandrabose Chinnathambi,Eva-Maria Mandelkow,Eckhard Mandelkow,Daniel J. Müller +5 more
TL;DR: Th thin and thick fibrils assembled from different human Tau isoforms challenge current structural models of paired helical filaments and, upon exposure to mechanical stress or hydrophobic surfaces, disassemble into uniform fragments that remain connected by thin thread-like structures.