4 results match your criteria: "Department of Biological Chemistry University of Michigan Medical School[Affiliation]"

Background: Specialty societies, such as the International Society on Thrombosis and Haemostasis (ISTH), are a key source of support for clinical and scientific communities, through the provision of educational activities, tools, and resources to support evidence-based care and high-quality, relevant basic science and clinical research.

Objective: The aim of this study was to identify areas where the thrombosis and hemostasis (T&H) community is facing challenges and could benefit from the support of ISTH.

Methods: A 3-phase, mixed-methods study consisting of semistructured individual interviews (phase 1), an online survey (phase 2), and discussion groups (phase 3) was conducted on the challenges experienced by the T&H community.

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This illustrated review focuses on polyphosphate as a potent modulator of the plasma clotting cascade, with possible roles in hemostasis, thrombosis, and inflammation. Polyphosphates are highly anionic, linear polymers of inorganic phosphates that are widespread throughout biology. Infectious microorganisms accumulate polyphosphates with widely varying polymer lengths (from a few phosphates to over a thousand phosphates long), while activated human platelets secrete polyphosphate with a very narrow size distribution (about 60-100 phosphates long).

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Non-histone protein lysine methyltransferases (PKMTs) represent an exceptionally diverse and large group of PKMTs. Even accepting the possibility of multiple protein substrates, if the number of different proteins with methylated lysyl residues and the number of residues modified is indicative of individual PKMTs there are well over a hundred uncharacterized PKMTs. Astoundingly, only a handful of PKMTs have been studied, and of these only a few with identifiable and well-characterized structure and biochemical properties.

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The redox active metal copper is an essential cofactor in critical biological processes such as respiration, iron transport, oxidative stress protection, hormone production, and pigmentation. A widely conserved family of high affinity copper transport proteins (Ctr proteins) mediates copper uptake at the plasma membrane. However, little is known about Ctr protein topology, structure, and the mechanisms by which this class of transporters mediates high affinity copper uptake.

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