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Liza D. Morales

Researcher at University of Texas at Austin

Publications -  21
Citations -  724

Liza D. Morales is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Protein kinase B & Protein tyrosine phosphatase. The author has an hindex of 11, co-authored 21 publications receiving 584 citations. Previous affiliations of Liza D. Morales include Baylor College of Medicine & University of Cincinnati Academic Health Center.

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GFRA1 promotes cisplatin-induced chemoresistance in osteosarcoma by inducing autophagy

TL;DR: It is demonstrated that GFRA1/GFRα1 (GDNF family receptor α 1), contributes to cisplatin-induced chemoresistance by regulating autophagy in osteosarcoma, and it is suggested thatGFRA1-mediated autophileagy is a promising novel target for overcoming cisPlatin resistance in ostea.
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Protein Tyrosine Phosphatases as Potential Regulators of STAT3 Signaling.

TL;DR: There are seven PTPs that have been shown to dephosphorylate STAT3 and, thereby, regulate STAT3 signaling and have great potential as targets for the development of more effective therapies against human disease, including cancer.
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Purified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibalpha.

TL;DR: The recombinant A2 domain polypeptide specifically binds to the active conformation of the A1 domain in VWF and effectively blocks the interaction with platelet GPIbα under high‐flow conditions.
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Stress-Induced β-Lactam Antibiotic Resistance Mutation and Sequences of Stationary-Phase Mutations in the Escherichia coli Chromosome

TL;DR: It is demonstrated that real-world stressors, such as starvation, can induce clinically relevant resistance mutations, and the ampD system is used to observe the true forward-mutation sequence spectrum of DSBR-associated stress-induced mutagenesis, for which previously only frameshift reversions were studied.
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The platelet glycoprotein Ib - von Willebrand Factor interaction activates the collagen receptor α2β1 to bind collagen: activation-dependent conformational change of the α2-I domain

TL;DR: Results strongly suggest that the interaction of platelet GP Ib with von Willebrand factor (VWF) mediates the activation of α2β1, increasing its affinity for collagen.