Khalid Masood

Centre of Excellence in Molecular Biology, Lāhaur, Punjab, Pakistan

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Publications (5)10.22 Total impact

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    ABSTRACT: The E glycoprotein of dengue virus is responsible for the viral binding to the receptor. The crystal structure of envelope glycoprotein has already been determined. However, where the well-defined Bcell and T-cell epitopes are located is still a question. Because of the large variations among the four dengue genotypes, it is very hard to design conserved epitopes for all of them. Therefore, we selected only one genotype (DENV3). The conserved regions were found in more than 600 DENV E glycoprotein sequences. Both the B-cell and T-cell epitopes were predicted and the hydrophobicity, antigenicity, accessibility and flexibility of the highly conserved E glycoprotein were further predicted by using different bioinformatics algorithms. The secondary structure was obtained and the predicted epitopes were pointed out in it. Binding sites on glycoprotein of DENV-3 for attachment of virus to the receptor was identified, while keeping those attachments in which new drugs for dengue related infections could not be designed.
    AFRICAN JOURNAL OF BIOTECHNOLOGY 05/2011; 10(18-18):3528-3533. · 0.57 Impact Factor
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    Abida Shehzadi · Khalid Masood ·
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    ABSTRACT: Asp66his, Asp54Lys, and Asp50Asn are mutations in connexin 26 that are observed in the clinic and give rise to autosomal dominant syndromes. They are the result of point mutations in the human gap junction gene. In order to investigate the structural mechanism of Bart-Pumphrey Syndrome, Keratitis-Ichthyosis-Deafness Syndrome, and Vohwinkel Syndrome, homology modeling was carried out. Asp66 has direct contact with Asn62 by two hydrogen bonds in the wild-type protein, and in Asp66His, the biggest change observed is a tremendous energy increase caused by hydrogen bond breakage to Asn62. Shifts in the side chain and new hydrogen bond formation are observed for Lys54 compared to the wild-type protein (Asn54) and result in closer contact to Val84. Asp50Asn causes a significant decrease in bond energy, and residual charge reversal repels the ion and metabolites and, hence, inhibits their transportation. Such perturbations are likely to be a factor contributing to abnormal functioning of ion channels, resulting cell death and disease.
    06/2010; 8(2). DOI:10.5808/GI.2010.8.2.070
  • Gulzar Niazi · Zeeshan Shaukat · Khalid Masood · Rashid Hussain ·

    Human Genetics 09/2009; 126(2):332. · 4.82 Impact Factor
  • Zeeshan Shaukat · Gulzar A Niazi · Khalid Masood · Rashid Hussain ·

    Human Genetics 08/2009; 126(2):332. · 4.82 Impact Factor
  • Source
    Nazia Nawaz · Rashid Hussain · Khalid Masood · Gulzar Niazi ·
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    ABSTRACT: Hemophilia B, an X-linked recessive bleeding disorder is caused by deficiency of clotting factor 1X protein. In an attempt to understand the molecular basis of hemophilia B which is a rare disease in Pakistan, we analyzed amplified genomic DNA from 20 patients (ages 3-36 years) with different ethnic back-grounds. Eleven mutations were identified in 15 out of 20 patients with mutation detection efficacy of 75%. Out of thes e 11mutations, 9 have been described earlier and these included: 7 missense and 2 nonsense mutations. The remaining 2 mutations are novel and are not listed in the hemophilia B mutation databases. These are: a 6bp insertion (CCTGCT) (Ser-Lys) in exon5 at codon110 in the second epidermal growth factor (EGF2) domain, which increases the length of domain by a little; and the other is a deletion of nucleotide #946(AAA_-AA) (-Lys) in exon8 at codon316, located in one of highly variable surface loops resulting in frame-shift in catalytic domain of the protein. Five SNPs in exons 6, 7 and 8, which are only one of its kinds, were present in Pakistan i hemophilia B patients.

Publication Stats

4 Citations
10.22 Total Impact Points


  • 2011
    • Centre of Excellence in Molecular Biology
      Lāhaur, Punjab, Pakistan
  • 2010
    • University of the Punjab
      • Centre for Excellence in Molecular Biology
      Lāhaur, Punjab, Pakistan