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Shobini Jayaraman

Researcher at Boston University

Publications -  35
Citations -  892

Shobini Jayaraman is an academic researcher from Boston University. The author has contributed to research in topics: Lipoprotein & Apolipoprotein B. The author has an hindex of 20, co-authored 35 publications receiving 805 citations. Previous affiliations of Shobini Jayaraman include Massachusetts Institute of Technology.

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Journal ArticleDOI

Dipolar assisted rotational resonance NMR of tryptophan and tyrosine in rhodopsin

TL;DR: DARR is shown to be more effective than RFDR in recoupling long-range dipolar interactions in model systems and 13C-13C correlations can be obtained in non-crystalline integral membrane proteins reconstituted into lipid membranes containing less than 150 nmoles of protein.
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Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis

TL;DR: It is suggested that high structural stability and resistance to proteolysis of SAA oligomers at pH 3.5–4.5 help them escape lysosomal degradation, promote SAA accumulation in lysOSomes, and ultimately damage cellular membranes and liberate intracellular amyloid.
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Amyloidogenic mutations in human apolipoprotein A‐I are not necessarily destabilizing – a common mechanism of apolipoprotein A‐I misfolding in familial amyloidosis and atherosclerosis

TL;DR: The results suggest that structural perturbations in the amyloid‐prone segments trigger α‐helix to β‐sheet conversion in the N‐terminal ~ 75 residues forming theAmyloid core, a novel mechanism that suggests potential therapeutic interventions for apoA‐I isyloidosis.
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Effects of salt on the thermal stability of human plasma high-density lipoprotein.

TL;DR: Analysis of the effects of various salts, sucrose, and pH suggests that HDL destabilization by salt results from ionic screening of favorable short-range electrostatic interactions such as salt bridges, which significantly contribute to the high thermostability of HDL in low-salt solutions.
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Role of apolipoprotein A-II in the structure and remodeling of human high-density lipoprotein (HDL): protein conformational ensemble on HDL.

TL;DR: An ensemble of apolipoprotein conformations on various HDL is postulate, hypothesizing that endogenous apoA-II helps confer lipid surface curvature during conversion of nascent discoidal HDL and HDL containing either apo-I or apo a-II to mature spherical HDL containing both proteins, and hinders remodeling of HDL by hindering the expansion of the apo A-I conformation.