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Victoria L. Robinson

Researcher at University of Connecticut

Publications -  42
Citations -  5124

Victoria L. Robinson is an academic researcher from University of Connecticut. The author has contributed to research in topics: Response regulator & Metastasis. The author has an hindex of 22, co-authored 42 publications receiving 4830 citations. Previous affiliations of Victoria L. Robinson include Howard Hughes Medical Institute & Center for Advanced Biotechnology and Medicine.

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Two-component signal transduction

TL;DR: Detailed analyses of a relatively small number of representative proteins provide a foundation for understanding this large family of signaling proteins, which consists of two conserved components, a histidine protein kinase and a response regulator protein.
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A tale of two components: a novel kinase and a regulatory switch

TL;DR: Structures of the core domains of histidine kinases reveal a protein kinase fold different from that of the Ser/Thr/Tyr protein kinases family, but similar to that of other ATP binding domains.
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Metastasis Suppression: The Evolving Role of Metastasis Suppressor Genes for Regulating Cancer Cell Growth at the Secondary Site

TL;DR: Clinical assessment of metastasis suppressor gene product status in disseminated cancer cells may improve the accuracy of predicting the prognosis in patients with clinically localized disease and support growth at the secondary site as a clinical target for metastasis treatment and prevention.
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EGFR Signals Downregulate Tumor Suppressors miR-143 and miR-145 in Western Diet–Promoted Murine Colon Cancer: Role of G1 Regulators

TL;DR: Western diet unmasks the tumor suppressor roles of these EGFR-regulated microRNAs that contribute to diet-promoted colonic tumorigenesis in murine models of colon cancer.
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Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily

TL;DR: The 1.8-A resolution crystal structure of Thermotoga maritima DrrB is determined, providing a second structure of a multidomain response regulator of the OmpR/PhoB subfamily, implying that conformational changes associated with phosphorylation will influence these intramolecular contacts.