Structure and Enzymatic Activity of an Intellectual Disability-Associated Ornithine Decarboxylase Variant, G84R
Por um escritor misterioso
Last updated 25 março 2025


Sequence comparison of amino acids 111–150 of AZ1 and AZ2 and

Amino acid residues at the dimer interface of human ornithine

Structural analysis of the human AzIN-Az 110-228 1 heterodimer. (A

Structure and Enzymatic Activity of an Intellectual Disability

ODC G84R crystal structure. (A) ODC G84R homodimer in the presence

Modeling the phosphopyridoxylornithine analogues in the active

AZ1 and AZ2 both bind ODC, but only AZ1 causes degradation . A

Chad SCHULTZ, Lab Manager, Michigan State University, MI

ODC is primed for proteasome recognition by associating with Az 1

Amino acid residues at the dimer interface of human ornithine

Crystal structure of ODC-cAZ1 complex.: (a) ODC-cAZ1 complex forms

Irving VEGA, Professor (Associate), PhD

The basic AUC experimental setup. The sector-shaped cell is loaded
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