Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Large-scale proteomics and phosphoproteomics of urinary exosomes.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Structure and expression of human dihydropteridine reductase.
-
DHPR (EC 1.5.1.34; historically 1.6.99.7) catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin and is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems.
"Dihydropteridine reductase (DHPR; EC 1.6.99.7) catalyzes the NADH-mediated
reduction of quinonoid dihydrobiopterin and is an essential component of the
pterin-dependent aromatic amino acid hydroxylating systems."
-
Recombinant human DHPR expressed in COS cells produces DHPR enzymatic activity, confirming the cloned cDNA encodes an active enzyme.
"Gene transfer of the recombinant human DHPR into COS cells
leads to expression of DHPR enzymatic activity."
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue.
-
The human DHPR enzyme was purified to homogeneity with kinetic identity to the natural enzyme and crystallized (PDB 1HDR), providing the first complete structural characterization.
"and kinetic identity to the naturally occurring enzyme has been proven."
q-dihydrobiopterin + NADH + H+ => tetrahydrobiopterin + NAD+