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ProteomicsStructural perturbation at the N-terminal domain of human phosphoglycerate kinase 1 reduces the kinetic stability and unfolding cooperativity of a two-domain enzyme
Phosphoglycerate kinase has been a model for the stability, folding cooperativity and catalysis of a two-domain protein. The human isoform 1 (hPGK1) is associated with cancer development and rare genetic diseases that affect several of their features. To investigate how mutations affect hPGK1 foldin...
ORGANISM(S): Homo sapiens (Human) 
2022-11-03 | PXD035628 | Pride
Protein folding  structural perturbation  disease 
ProteomicsCounterintuitive structural and functional effects due to naturally-occurring mutations targeting the active site of the disease-associated NQO1 enzyme
Our knowledge on the genetic diversity of the human genome is exponentially growing. However, our capacity to establish genotype-phenotype correlations in a large-scale requires a combination of detailed experimental and computational work. This is a remarkable task in human proteins, which are typi...
ORGANISM(S): Homo sapiens (Human) 
2022-11-23 | PXD036417 | Pride
Genotype-phenotype correlations  protein structure-function  structural stability  catalytic mechanism 
ProteomicsPhenotypic divergence due to site-specific phosphorylation in the antioxidant and cancer-associated NQO1 enzyme
Aims: to evaluate the effects of site-specific phosphorylation (using phosphomimetic mutations at sites S40, S82 and T128) on multiple functional aspects of the antioxidant and disease-associated human flavoprotein NQO1. Results: in vitro biophysical studies revealed effects of phosphorylation at di...
ORGANISM(S): Homo sapiens (Human) 
2022-09-20 | PXD034600 | Pride
Flavoprotein  phosphorylation  phenotypic effects  structure-function relationships  structural stability 
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