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Shajna Begum

Researcher at Imperial College London

Publications -  35
Citations -  2178

Shajna Begum is an academic researcher from Imperial College London. The author has contributed to research in topics: Proteome & Biotinylation. The author has an hindex of 26, co-authored 35 publications receiving 2090 citations.

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Oxidant-induced Activation of Type I Protein Kinase A Is Mediated by RI Subunit Interprotein Disulfide Bond Formation

TL;DR: It is demonstrated that type I protein kinase A is redoxactive, forming an interprotein disulfide bond between its two regulatory RI subunits in response to cellular hydrogen peroxide, which causes a subcellular translocation and activation of the kinase, resulting in phosphorylation of established substrate proteins.
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Detection and Mapping of Widespread Intermolecular Protein Disulfide Formation during Cardiac Oxidative Stress Using Proteomics with Diagonal Electrophoresis

TL;DR: The observation of widespread protein-protein disulfides indicates that these oxidative associations are likely to be fundamental in how cells respond to redox changes.
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Protein Sulfenation as a Redox Sensor Proteomics Studies Using a Novel Biotinylated Dimedone Analogue

TL;DR: A novel biotinylated derivative of dimedone is synthesized, keeping the dione cassette required for sulfenate reactivity but adding the functionality of a biotin tag, highlighting the protein sulfenates as oxygen sensors in hearts loaded and subjected to hypoxia.
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Proteomic analysis of articular cartilage shows increased type II collagen synthesis in osteoarthritis and expression of inhibin betaA (activin A), a regulatory molecule for chondrocytes.

TL;DR: Type II collagen synthesis in articular cartilage is down-regulated at skeletal maturity and reactivated in osteoarthritis in attempted repair and that activin A may be an anabolic factor in cartilage.
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The Human Muscle Proteome in Aging

TL;DR: The differences observed in the elderly group included down-regulation of regulatory myosin light chains, particularly the phosphorylated isoforms, a higher proportion of myOSin heavy chain isoforms 1 and 2A, and enhanced oxidative and reduced glycolytic capacity.