Search Results - "Rawat, Anoop"

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  1. 1

    Membranes as modulators of amyloid protein misfolding and target of toxicity by Rawat, Anoop, Langen, Ralf, Varkey, Jobin

    “…Abnormal protein aggregation is a hallmark of various human diseases. α-Synuclein, a protein implicated in Parkinson's disease, is found in aggregated form…”
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  2. 2

    Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted by Mario Isas, J., Pandey, Nitin K., Xu, Hui, Teranishi, Kazuki, Okada, Alan K., Fultz, Ellisa K., Rawat, Anoop, Applebaum, Anise, Meier, Franziska, Chen, Jeannie, Langen, Ralf, Siemer, Ansgar B.

    Published in Nature communications (13-07-2021)
    “…The first exon of the huntingtin protein (HTTex1) important in Huntington’s disease (HD) can form cross-β fibrils of varying toxicity. We find that the…”
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  3. 3

    Amplification of neurotoxic HTTex1 assemblies in human neurons by Chongtham, Anjalika, Isas, J. Mario, Pandey, Nitin K., Rawat, Anoop, Yoo, Jung Hyun, Mastro, Tara, Kennedy, Mary B., Langen, Ralf, Khoshnan, Ali

    Published in Neurobiology of disease (01-11-2021)
    “…Huntington’s disease (HD) is a genetically inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) repeat in the exon-1 of…”
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  4. 4

    Peptide self-assembly: from toxins to amyloid fibrils and nanotubes by Rawat, Anoop, Nagaraj, Ramakrishnan

    Published in Current topics in medicinal chemistry (01-03-2014)
    “…The process of self-assembly is universal and lies at the heart of biological structures and function. Peptide aggregation, while considered a nuisance in…”
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  5. 5

    Chronic chemogenetic activation of hippocampal progenitors enhances adult neurogenesis and modulates anxiety-like behavior and fear extinction learning by Maheshwari, Megha, Singla, Aastha, Rawat, Anoop, Banerjee, Toshali, Pati, Sthitapranjya, Shah, Sneha, Maiti, Sudipta, Vaidya, Vidita A.

    Published in IBRO neuroscience reports (01-06-2024)
    “…Adult hippocampal neurogenesis is a lifelong process that involves the integration of newborn neurons into the hippocampal network, and plays a role in…”
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  6. 6

    Determinants of membrane association in the SH4 domain of Fyn: Roles of N-terminus myristoylation and side-chain thioacylation by Rawat, Anoop, Nagaraj, Ramakrishnan

    Published in Biochimica et biophysica acta (01-10-2010)
    “…The SH4 domain of Fyn, a member of the Src family of tyrosine kinases, though rich in polar amino acid residues, anchors to the cytosolic face of membranes…”
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  7. 7

    Aggregation-induced conformation changes dictate islet amyloid polypeptide (IAPP) membrane affinity by Rawat, Anoop, Maity, Barun Kumar, Chandra, Bappaditya, Maiti, Sudipta

    “…Islet amyloid polypeptide (IAPP) is a 37 residue intrinsically disordered protein whose aggregation is associated with Type II diabetes. Like most amyloids, it…”
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  8. 8

    The 17-residue-long N terminus in huntingtin controls stepwise aggregation in solution and on membranes via different mechanisms by Pandey, Nitin K., Isas, J. Mario, Rawat, Anoop, Lee, Rachel V., Langen, Jennifer, Pandey, Priyatama, Langen, Ralf

    Published in The Journal of biological chemistry (16-02-2018)
    “…Aggregation of huntingtin protein arising from expanded polyglutamine (polyQ) sequences in the exon-1 region of mutant huntingtin plays a central role in the…”
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  9. 9

    Droplet and fibril formation of the functional amyloid Orb2 by Ashami, Kidist, Falk, Alexander S., Hurd, Connor, Garg, Samridhi, Cervantes, Silvia A., Rawat, Anoop, Siemer, Ansgar B.

    Published in The Journal of biological chemistry (01-07-2021)
    “…The functional amyloid Orb2 belongs to the cytoplasmic polyadenylation element binding (CPEB) protein family and plays an important role in long-term memory…”
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  10. 10

    Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human β2-microglobulin by Rawat, Anoop, Nagaraj, Ramakrishnan

    Published in Journal of peptide science (01-12-2013)
    “…Aggregation of a polypeptide chain into highly ordered amyloid aggregates is a complex process. Various factors, both extrinsic and intrinsic to the…”
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  11. 11

    Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human β(2)-microglobulin by Rawat, Anoop, Nagaraj, Ramakrishnan

    Published in Journal of peptide science (01-12-2013)
    “…Aggregation of a polypeptide chain into highly ordered amyloid aggregates is a complex process. Various factors, both extrinsic and intrinsic to the…”
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    Journal Article
  12. 12

    An Early Folding Contact between Phe19 and Leu34 is Critical for Amyloid‑β Oligomer Toxicity by Das, Anand K, Rawat, Anoop, Bhowmik, Debanjan, Pandit, Rucha, Huster, Daniel, Maiti, Sudipta

    Published in ACS chemical neuroscience (19-08-2015)
    “…Small hydrophobic oligomers of aggregation-prone proteins are thought to be generically toxic. Here we examine this view by perturbing an early folding contact…”
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  13. 13

    Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human β 2 ‐microglobulin by Rawat, Anoop, Nagaraj, Ramakrishnan

    Published in Journal of peptide science (01-12-2013)
    “…Aggregation of a polypeptide chain into highly ordered amyloid aggregates is a complex process. Various factors, both extrinsic and intrinsic to the…”
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    Journal Article
  14. 14

    Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human [beta] sub(2)-microglobulin by Rawat, Anoop, Nagaraj, Ramakrishnan

    Published in Journal of peptide science (01-12-2013)
    “…Aggregation of a polypeptide chain into highly ordered amyloid aggregates is a complex process. Various factors, both extrinsic and intrinsic to the…”
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    Journal Article
  15. 15

    Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human [beta]2-microglobulin by Rawat, Anoop, Nagaraj, Ramakrishnan

    Published in Journal of peptide science (01-12-2013)
    “…Aggregation of a polypeptide chain into highly ordered amyloid aggregates is a complex process. Various factors, both extrinsic and intrinsic to the…”
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    Journal Article
  16. 16

    Spontaneous Fluctuations Can Guide Drug Design Strategies for Structurally Disordered Proteins by Maity, Barun Kumar, Vishvakarma, Vicky, Surendran, Dayana, Rawat, Anoop, Das, Anirban, Pramanik, Shreya, Arfin, Najmul, Maiti, Sudipta

    Published in Biochemistry (Easton) (17-07-2018)
    “…Structure-based “rational” drug design strategies fail for diseases associated with intrinsically disordered proteins (IDPs). However, structural disorder…”
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  17. 17
  18. 18

    Lipid Membrane Interaction of Amyloidogenic Peptides by Dey, Simli, Gupta, Ankur, Bhowmik, Debanjan, Das, Anirban, Rawat, Anoop, Maiti, Sudipta

    Published in The FASEB journal (01-04-2018)
    “…Membrane interaction appears to be a key step in the toxic pathway of many amyloidogenic proteins, such as Amyloidβ (Aβ40/42, associated with Alzheimer's…”
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  19. 19

    Single Molecule Tools for Probing Protein Aggregation by Rawat, Anoop, Maiti, Sudipta

    “…Protein aggregation poses a fundamental problem in biophysics, whose solutions have enormous potential for societal benefits. Many devastating and incurable…”
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  20. 20

    Fluorogenic Detection of Monoamine Neurotransmitters in Live Cells by Bera, Kallol, Das, Anand Kant, Rakshit, Ananya, Sarkar, Bidyut, Rawat, Anoop, Maity, Barun Kumar, Maiti, Sudipta

    Published in ACS chemical neuroscience (21-03-2018)
    “…Monoamine neurotransmission is key to neuromodulation, but imaging monoamines in live neurons has remained a challenge. Here we show that externally added…”
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