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Sandra W. Leung

Researcher at Johns Hopkins University School of Medicine

Publications -  9
Citations -  9170

Sandra W. Leung is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Hypoxia-Inducible Factor 1 & Transcription factor. The author has an hindex of 8, co-authored 9 publications receiving 8631 citations. Previous affiliations of Sandra W. Leung include Johns Hopkins University & University of Maryland, Baltimore.

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Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1.

TL;DR: HIF-1 is implicate in the activation of VEGF transcription in hypoxic cells and this work demonstrates the involvement of Hif-1 in theactivation of V EGF transcription.
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Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1α

TL;DR: It is demonstrated that HIF-1alpha is a master regulator of cellular and developmental O2 homeostasis in Hif1a-/- embryos that manifested neural tube defects, cardiovascular malformations, and marked cell death within the cephalic mesenchyme.
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Hypoxia Response Elements in the Aldolase A, Enolase 1, and Lactate Dehydrogenase A Gene Promoters Contain Essential Binding Sites for Hypoxia-inducible Factor 1

TL;DR: It is demonstrated that functional hypoxia response elements in the promoters of the ALDA, ENO1, and Ldha genes consist of a pair of contiguous transcription factor binding sites at least one of which contains the core sequence 5′-RCGTG-3′ and is recognized by HIF-1.
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Transactivation and Inhibitory Domains of Hypoxia-inducible Factor 1α MODULATION OF TRANSCRIPTIONAL ACTIVITY BY OXYGEN TENSION

TL;DR: It is demonstrated that HIF-1α contains two transactivation domains located between amino acids 531 and 826, which indicate that increased transcriptional activity mediated by Hif-1 in hypoxic cells results from both increased H IF-1 α protein levels and increased activity of HIF -1α trans activation domains.
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Structural and functional analysis of hypoxia-inducible factor 1

TL;DR: Structural analysis of Hif-1 alpha revealed that dimerization with HIF-1 beta (ARNT) requires the HLH and PAS domains, DNA binding is mediated by the basic domain, and that HIF -1 alpha contains a carboxyl-terminal transactivation domain.