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The functional consequence of these modifications is discussed in the next section.
As a consequence of these modifications the heme is distorted and these peroxidases exhibit unique spectral and redox properties [29].
As a consequence of these modifications, an increased recruitment of NF-κB to the promoter of several cytokines and chemokines could be observed [ 79].
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Several recent biochemical and molecular studies have provided new information regarding the potential physiological consequences of these modifications.
We monitored the consequences of these modifications on Ca2+ binding by isothermal titration calorimetry, thermal stability and conformational and crystal structure analyses.
Here, we review various oxidative modifications of fibrinogen and the consequences of these modifications on protein structure and the ability to form fibrin and how the resulting alterations affect fibrin architecture and viscoelastic and biochemical properties that may contribute to disease.
However, no comprehensive, genome-wide analysis of the biological consequences of these modifications exists.
In particular, the pathways by which NO metabolism leads to protein S-nitrosation and the physiological consequences of these modifications remain obscure [ 4, 5].
Consequently, there is still considerable uncertainty regarding the majority of mitochondrial proteins affected by S-nitrosation and the functional consequences of these modifications.
By investigating the functional consequences of these modifications, we provide mechanistic insights into mitochondrial protein S-nitrosation and its potential contribution to mitochondrial physiology and pathology.
8 At rest, the clinical consequences of these modifications remain minor for a long time, mostly involving only an increase in arterial pressure.
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