Search Results - "Rawat, Anoop"
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Membranes as modulators of amyloid protein misfolding and target of toxicity
Published in Biochimica et biophysica acta. Biomembranes (01-09-2018)“…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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Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
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
Amplification of neurotoxic HTTex1 assemblies in human neurons
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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Peptide self-assembly: from toxins to amyloid fibrils and nanotubes
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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Chronic chemogenetic activation of hippocampal progenitors enhances adult neurogenesis and modulates anxiety-like behavior and fear extinction learning
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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Determinants of membrane association in the SH4 domain of Fyn: Roles of N-terminus myristoylation and side-chain thioacylation
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
Aggregation-induced conformation changes dictate islet amyloid polypeptide (IAPP) membrane affinity
Published in Biochimica et biophysica acta. Biomembranes (01-09-2018)“…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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The 17-residue-long N terminus in huntingtin controls stepwise aggregation in solution and on membranes via different mechanisms
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
Droplet and fibril formation of the functional amyloid Orb2
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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Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human β2-microglobulin
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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Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human β(2)-microglobulin
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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12
An Early Folding Contact between Phe19 and Leu34 is Critical for Amyloid‑β Oligomer Toxicity
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
Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human β 2 ‐microglobulin
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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14
Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human [beta] sub(2)-microglobulin
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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15
Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human [beta]2-microglobulin
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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16
Spontaneous Fluctuations Can Guide Drug Design Strategies for Structurally Disordered Proteins
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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Amyloid Aggregation of Amylin: Gain of Function along Aggregation Pathway?
Published in Biophysical journal (16-02-2016)Get full text
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Lipid Membrane Interaction of Amyloidogenic Peptides
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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Single Molecule Tools for Probing Protein Aggregation
Published in Proceedings of the National Academy of Sciences, India, Section A, physical sciences (01-12-2015)“…Protein aggregation poses a fundamental problem in biophysics, whose solutions have enormous potential for societal benefits. Many devastating and incurable…”
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Fluorogenic Detection of Monoamine Neurotransmitters in Live Cells
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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