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Michael G. Klein

Researcher at Takeda Pharmaceutical Company

Publications -  101
Citations -  5960

Michael G. Klein is an academic researcher from Takeda Pharmaceutical Company. The author has contributed to research in topics: Calcium & Endoplasmic reticulum. The author has an hindex of 41, co-authored 95 publications receiving 5609 citations. Previous affiliations of Michael G. Klein include United States Department of Energy & University of Southern California.

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Two mechanisms of quantized calcium release in skeletal muscle

TL;DR: A 'dual-control' model for discrete Ca2+ release events from the sacroplasmic reticulum is proposed that unifies diverse observations about Ca2-signalling in frog skeletal muscle, and that may be applicable to other excitable cells.
Journal Article

Antisense to Cyclin D1 Inhibits the Growth and Tumorigenicity of Human Colon Cancer Cells

TL;DR: Findings provide direct evidence that increased expression of cyclin D1 in colon tumor cells contributes to their abnormal growth and tumorigenicity and suggest that cyclinD1 or its associated cyclin-dependent kinase 4 may be useful targets in the therapy of colon cancer.
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Treatment of comminuted fractures of the proximal humerus in elderly patients with the Delta III reverse shoulder prosthesis.

TL;DR: The good functional outcome and the short intervention time in the present study and not needing a sufficient rotator cuff for implementation purposes suggest the use of the Delta III reverse shoulder prosthesis as a treatment option for elderly patients with comminuted fractures of the proximal humerus.
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The APOBEC-2 crystal structure and functional implications for the deaminase AID

TL;DR: The crystal structure of APO2 is reported and it is shown that AID deamination activity is impaired by mutations predicted to interfere with oligomerization and substrate access, resulting in defective antibody maturation.
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Structure-based analysis of catalysis and substrate definition in the HIT protein family.

TL;DR: Fragile histidine triad protein and protein kinase C interacting protein were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions and may be useful in identifying structure-function relations between protein families identified through genomics.