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Michael Eschenberg

Researcher at Amgen

Publications -  10
Citations -  1211

Michael Eschenberg is an academic researcher from Amgen. The author has contributed to research in topics: Motesanib & Thyroid cancer. The author has an hindex of 8, co-authored 10 publications receiving 1137 citations.

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Journal ArticleDOI

Phase II study of safety and efficacy of motesanib in patients with progressive or symptomatic, advanced or metastatic medullary thyroid cancer

TL;DR: Although the objective response rate was low, a significant proportion of MTC patients (81%) achieved stable disease while receiving motesanib, and motesanIB trough concentrations were lower compared with differentiated thyroid cancer patients from the same study.
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Interference with bile salt export pump function is a susceptibility factor for human liver injury in drug development.

TL;DR: In this study, membrane vesicles harvested from BSEP-transfected insect cells were used to assess the activity of more than 200 benchmark compounds to thoroughly investigate the relationship between interference with BSEp function and liver injury, and suggest a relatively strong association between the pharmacological interference with bile salt export pump function and human hepatotoxicity.
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Progressive increases in bone mass and bone strength in an ovariectomized rat model of osteoporosis after 26 weeks of treatment with a sclerostin antibody.

TL;DR: Bone mass and strength increased progressively over 26 weeks of Scl-Ab treatment in adult OVX rats, and the early gains were accompanied by increased cortical and trabecular bone formation and reduced osteoclast activity, whereas later gains were attributed to residual endocortical and trABecular osteoblast stimulation and persistently low osteOClast activity.
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Beyond Glass Transitions: Studying the Highly Viscous and Elastic Behavior of Frozen Protein Formulations Using Low Temperature Rheology and Its Potential Implications on Protein Stability

TL;DR: The first application of oscillatory rheology is reported to study phase behavior of IgG2 in a sucrose-containing formulation and its correspondence with physical stability not explained by glass transition, providing a mechanism and data suggesting that protein instability occurs at the ice/water interface.