Publications by authors named "Dlzar D Ghafoor"

This is the first study in Iraq to integrate socioeconomic, genetic, and oxidative stress markers in MS patients, revealing unique associations between HLA-DRB1 polymorphisms and relapsing-remitting MS (RRMS). This work investigated the demographic, clinical, oxidative stress, and molecular aspects influencing quality of life in multiple sclerosis patients in Sulaymaniyah, Iraq. A cross-sectional study was undertaken with 63 MS patients and 20 healthy controls to evaluate quality of life using the Multiple Sclerosis Quality of Life-54 (MSQoL-54) questionnaire.

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Recent research has revealed the role of metalloproteinases in a number of severe pathological illnesses, including cardiac, cartilage, neurological, and cancer-related diseases that are fatal to humans. Metalloproteinases are a subclass of endopeptidases that comprise structurally identical enzymes known as Matrix Metalloproteinases (MMPs) that are solely involved in extracellular matrix degradation and play a significant regulatory function in tissue remodeling. Improper regulation and expression of MMPs have been linked to several life-threatening pathological conditions in humans.

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This study aims to estimate the level of malondialdehyde (MDA) as oxidative stress marker and reduced glutathione (GSH) as antioxidant and correlate them to different inflammatory markers as interleukins (IL-6, IL-8, IL-10) and tumor necrosis factor alpha (TNF-α) in different stages of breast cancer (BC). For the purpose of comparisons, 35 healthy subjects matched for age, sex and ethnic background were selected who have no history or clinical evidence of BC or any chronic disease and obvious abnormalities as a control group and 35 patients of different stages of BC were participated in the study. The cancer patients were diagnosed by specialists.

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Proximal distal heme-NO coordination is a novel strategy for selective gas response in heme-based NO-sensors. In the case of cytochrome c' (AXCP), formation of a transient distal 6cNO complex is followed by scission of the Fe-His bond and conversion to a proximal 5cNO product a putative dinitrosyl species. Here we show that replacement of the AXCP distal Leu16 residue with smaller or similar sized residues (Ala, Val or Ile) traps the distal 6cNO complex, whereas Leu or Phe residues lead to a proximal 5cNO product with a transient or non-detectable distal 6cNO precursor.

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Cytochromes c', that occur in methanotrophic, denitrifying and photosynthetic bacteria, form unusual proximal penta-coordinate NO complexes via a hexa-coordinate distal NO intermediate. Their NO binding properties are similar to those of the eukaryotic NO sensor, soluble guanylate cyclase, for which they provide a valuable structural model. Previous studies suggested that hydrogen bonding between the displaced proximal histidine (His120) ligand (following its dissociation from heme due to trans effects from the distally bound NO) and a conserved aspartate residue (Asp121) could play a key role in allowing proximal NO binding to occur.

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