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Glycosylation is a well-known post-translational modification, but identifying specific roles for the attached glycans is often challenging. The identification and investigation of a new O-GlcNAc site on the transcription factor CREB provides insights into how glycosylation works together with phosphorylation to coordinate neural function.
20(S)-hydroxycholesterol, a naturally occurring oxysterol, activates the Hedgehog signaling pathway by directly binding an allosteric site on Smoothened.
Patch-clamp fluorometry measurements of cAMP binding and channel opening combined with global kinetic fitting revealed that ligand binding to the tetrameric hyperpolarization-activated cyclic nucleotide–gated channel is favored at the second and fourth binding events.
Mucopolysaccharidoses are inherited disorders in which inactivation of lysosomal enzymes results in accumulation of glycosaminoglycans within cells, causing tissue and organ dysfunction. A method to determine the unique end structures of the accumulated glycosaminoglycans offers a new way for diagnosis.
NMR and structural analyses of DHFR complexes with inhibitors of differing affinities define a model for ligand dissociation involving conformational switching and a new excited state that mediates the dissociation.
Osmolytes act as chemical chaperones capable of directly assisting the folding of destabilizing mutations in proteins in vivo, with different osmolytes having distinct targets and thereby increasing the level of genetic variability.
20(S)-hydroxycholesterol binds to Smo at a site distinct from cyclopamine and activates signaling via an allosteric mechanism. A new alkyne oxysterol analog selectively captures Smo from membrane extracts and provides a new method for detecting protein-sterol interactions.
DNA repair proteins require efficient pathways to search for DNA damage lesions within a large genome. Kinetic trapping experiments define the rates of human uracil DNA glycosylase hopping and sliding along damaged DNA substrates and highlight the role of the phosphodiester backbone in DNA sliding.
Mucopolysaccharidoses are caused by a deficiency in GAG processing and can often be treated if the dysfunctional enzyme can be identified. A chemical derivatization strategy in combination with biochemical logic now yields a series of biomarkers that can be used to distinguish these disorders.
