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Shuangping Shi

Researcher at Cornell University

Publications -  8
Citations -  1088

Shuangping Shi is an academic researcher from Cornell University. The author has contributed to research in topics: Tumor necrosis factor alpha & Pyruvate dehydrogenase complex. The author has an hindex of 7, co-authored 8 publications receiving 1021 citations.

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Reprogramming of the Macrophage Transcriptome in Response to Interferon-γ and Mycobacterium tuberculosis Signaling Roles of Nitric Oxide Synthase-2 and Phagocyte Oxidase

TL;DR: Studies involving macrophages deficient in inducible nitric oxide synthase and/or phagocyte oxidase revealed that these two antimicrobial enzymes help orchestrate the profound transcriptional remodeling that underlies macrophage activation.
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MyD88 Primes Macrophages for Full-Scale Activation by Interferon-γ yet Mediates Few Responses to Mycobacterium tuberculosis

TL;DR: Analysis of the mechanism revealed that MyD88 mediates a process of self-priming by which resting macrophages produce a low level of tumor necrosis factor, which synergizes with IFN-γ for gene induction.
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Virulence of Mycobacterium tuberculosis Depends on Lipoamide Dehydrogenase, a Member of Three Multienzyme Complexes

TL;DR: Mycobacterium tuberculosis (Mtb) adapts to persist in a nutritionally limited macrophage compartment and critically requires BCKADH along with PDH and PNR/P for pathogenesis, positioning Lpd as a potential target for anti-infectives against Mtb.
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Mycobacterium tuberculosis appears to lack α-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes

TL;DR: In this paper, a peroxynitrite reductase-peroxidase complex in Mtb was identified, which included products of the genes sucB and lpd, which are annotated to encode the dihydrolipoamide succinyltransferase and lipoamide dehydrogenase (E3) components of α-ketoglutarate deacetyltransferase (KDH).
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Expression of many immunologically important genes in Mycobacterium tuberculosis-infected macrophages is independent of both TLR2 and TLR4 but dependent on IFN-alphabeta receptor and STAT1.

TL;DR: Viable Mtb elicits the expression of inducible NO synthase, RANTES, IFN-inducible protein 10, and IRG1 in macrophages that lack mannose receptor, complement receptors 3 and 4, type A scavenger receptor, or CD40.