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Aruna Basu

Researcher at University of Pennsylvania

Publications -  14
Citations -  1430

Aruna Basu is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Protein subunit & Cytochrome c oxidase. The author has an hindex of 13, co-authored 14 publications receiving 1419 citations.

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Journal Article

Bcl2 Is the Guardian of Microtubule Integrity

TL;DR: Prevention of polymerization or depolymerization of cellular microtubules by this class of cancer therapeutic drugs causes phosphorylation of bcl2, abrogating the normal antiapoptotic function of bCl2 and initiating the apoptotic program in the cycling cancer cells; these results are consistent with a normal physiological role of b cl2 as "guardian of microtubule integrity."
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Binding of an antagonistic monoclonal antibody to an intact and fragmented EGF-receptor polypeptide☆

TL;DR: The results of antibody binding studies indicate that the epitope is closely linked to the EGF binding active site, and is common to both high- and low-affinity EGF-receptors.
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Identification of a transcriptional initiator element in the cytochrome c oxidase subunit Vb promoter which binds to transcription factors NF-E1 (YY-1, delta) and Sp1.

TL;DR: It is demonstrated that NF-E1 is necessary for transcription activation of both the 17Inr and the 13Inr initiator templates, which appears to be important for basal promoter function of the mouse COXVb gene.
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The isoforms of yeast cytochrome c oxidase subunit V alter the in vivo kinetic properties of the holoenzyme

TL;DR: Findings support the conclusion that the isoforms of subunit V modulate cytochrome c oxidase activity in vivo and suggest that they do so by altering the rates of one or more intramolecular electron transfer reactions.
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The basal promoter elements of murine cytochrome c oxidase subunit IV gene consist of tandemly duplicated ets motifs that bind to GABP-related transcription factors.

TL;DR: The ets-related protein found in COS nuclear extracts is shown to be identical or closely related to the GA-binding protein (GABP) by comparison of electrophoretic mobilities and immunological reactivities of DNA-protein complexes formed with purified recombinant expressed GABP alpha and beta subunits.