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Journal of Physiology and Pharmacology: An Official Journal of the Polish Physiological Society, 60 Suppl 7, 191196

10.21203/rs.3.rs-3958974/v1

[5] Structure of dihydrolipoyl transacetylase Three functionally distinct domains can be identified in the structure of dihydrolipoyl transacetylase: an N-terminal lipoyl domain, a peripheral subunit-binding domain, and a C-terminal catalytic (or acyltransferase) domain

At the same time, it has become evident that currently available pharmacological tools are not sufficiently specific or versatile to elucidate the precise role of H 2 S in biology

Matrix stiffening and EGFR cooperate to promote the collective invasion of cancer cells

However, when this continues, and they are insufficient to contain the inflammation, they also continually release additional inflammatory mediators