What kind of institute is the NBRC
Goswami ANAND (PhD)
Intracellular deposits of mutant, misfolded proteins in the form of inclusions / aggregates are the major pathological hallmarks of several neurodegenerative diseases including Amyotropic lateral sclerosis (ALS). The major aim of our research is to understand the molecular pathomechanism (s) involved in such diseases with special focus on ALS and to subsequently design molecular targets for therapeutic interventions.
Protein biochemistry, neuropathology of human spinal cord, skeletal muscles and brain, routine histology, cell culture models, human fibroblast cell culture model, human ipSC-derived motor neuron culture, transgenic and knockout mouse models for neuromuscular diseases.
Protein aggregation, autophagy, ER chaperones, neuroprotection, disease resistant neurons, C-boutons, motor neuron excitability, synaptic plasticity, neuromuscular diseases, skeletal muscles, calcium homeostasis, ultrastructural defects of neurons.
Post doc .: Laboratory for Structural Neuropathology BSI, RIKEN, Tokyo, Japan. Head: Dr. Nobuyuki Nukina.
PhD: Laboratory for molecular neuroscience. National Brain Research Center (NBRC) Gurgaon, India. Supervisor: Prof. Nihar Ranjan Jana
Goswami A, Dikshit P, Mishra A, Mulherkar S, Nukina N, Jana NR. Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction. Biochem Biophys Res Commun. 31; 342 (1): 184-90, 2006
Goswami A, Dikshit P, Mishra A, Nukina N, Jana NR. Expression of expanded polyglutamine proteins suppresses the activation of transcription factor NFkappaB. J Biol Chem. 281 (48): 37017-24, 2006
Farmer PO, Goswami A, Wong HK, Okuno M, Kurosawa M, Yamada M, Miyazaki H, Matsumoto G, Kino Y, Nagai Y, Nukina N. Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein. Nat Biotechnol. 28 (3): 256-63, 2010
Prause J *, Goswami A *, Katona I, Roos A, Schnizler M, Bushuven E, Dreier A, Buchkremer S, Johann S, Beyer C, Deschauer M, Troost D, Weis J. Altered localization, abnormal modification and loss of function of Sigma receptor-1 in amyotrophic lateral sclerosis. Hum Mol Genet. 22 (8): 1581-1600, 2013. * Equal contr.
Vollrath JT, Sechi A, Dreser A, Katona I, Wiemuth D, Vervoorts J, Dohmen M, Chandrasekar A, Prause J, Brauers E, Jesse CM, Weis J *, Goswami A *. Loss of function of the ALS protein SigR1 leads to ER pathology associated with defective autophagy and lipid raft disturbances. Cell Death Dis. 12; 5: e1290, 2014. * Equal contr.
Goswami A, Jesse C, Chandrasekar A, Bushuven E, Vollrath J, Dreser A, Katona I, Beyer C, Johann S, Feller A, Grond M, Wagner S, Nikolin S, Troost D, Weis J. Accumulation of STIM1 is associated with the degenerative muscle fiber phenotype in ALS and other neurogenic atrophies. Neuropathol Appl Neurobiol. 41 (3): 304-18. 2014
Filézac de L'Etang A, Maharjan N, Cordeiro Braña M, Ruegsegger C, Rehmann R, Goswami A, Roos A, Troost D, Schneider BL, Weis J, Saxena S. Marinesco-Sjögren syndrome protein SIL1 regulates motor neuron subtype-selective ER stress in ALS. Nature Neurosci. 18 (2): 227-238, 2015
Ruegsegger C *, Maharjan N *, Goswami A, Filézac de L'Etang A, Weis J, Troost D, Heller M, Gut H, Saxena S. Aberrant association of misfolded SOD1 with Na (+) / K (+) ATPase-α3 impairs its activity and contributes to motor neuron vulnerability in ALS. Acta Neuropathol. 131 (3): 427-51, 2016
Jesse CM1, Bushuven E1, Drepper C2, Chandrasekar A1, Yamoah A1, Tripathi P1, Dreser A1, Katona I1, Beyer C3, Johann S3, Grond M4, Wagner S4, Nikolin S1, Aninik J5, Troost D5, Sendtner M2 & Goswami A1 *, Weis J1 * ALS-associated endoplasmic reticulum proteins in denervated skeletal muscle: Implications for motor neuron disease pathology. Brain pathol. 27 (6): 781-794, 2016. * Equal contr.
Dreser A, Vollrath JT, Sechi A, Johann S, Roos A, Yamoah A, Katona I, Boholega S, Wiemuth D, Tian Y, Schmidt A, Vervoorts-Weber J, Dohmen M, Beyer C, Anink J, Aronica E, Troost D, Weis J *, Goswami A *. The ALS-linked E102Q mutation in Sigma receptor-1 leads to ER stress-mediated defects in protein homeostasis and dysregulation of RNA binding proteins. Cell Death Differ. 10: 1655-1671, 2017. * Equal contr.
For a complete reference list please see PubMed * Link
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