Nameerah Saleem
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Nameerah Saleem has a total of 10 co-authors. Here are the top co-authors by number of shared publications:
- Abdullah Etezaz
Institute of Microbiology, University of Agriculture, Faisalabad, Pakistan
1 shared publication - Farzana Rashid
Department of Zoology, Lahore College for Women University, Lahore, Pakistan
1 shared publication - Hafiz Ishfaq Ahmad
Department of Animal Breeding and Genetics, Faculty of Veterinary and Animal Sciences, The Islamia University of Bahawalpur, Bahawalpur, Pakistan
1 shared publication - Haiba Kaul
Department of Animal Breeding and Genetics, University of Veterinary and Animal Sciences (UVAS), Lahore–54000, Punjab, Pakistan., Pakistan
1 shared publication - Muhammad Bilal Bin Majeed
CRISPR Lab, Section Genetics, Department of Animal Breeding and Genetics, University of Veterinary and Animal Sciences, Lahore (Ravi Campus, Pattoki), Pakistan
1 shared publication - Muhammad Shakil
Department of Biochemistry, King Edward Medical University (KEMU), Lahore, Pakistan
1 shared publication
Latest Publications
- 9 May 2025
- Published by Springer Nature in Biochemical Genetics
- Vol. 64 (2) , 2048-2065
Molecular Characterization of Oculocutaneous Albinism in Consanguineous Pakistani Families: Unraveling Disease-Causing Pathogenic Variants in OCA2 and TYR Genes for Precision Diagnosis
Oculocutaneous albinism is a rare genetic disorder characterized by the absence or reduction of melanin pigment in the skin, hair, and eyes, leading to various visual and dermatological challenges. To shed light on the molecular pathology of OCA in consanguineous Pakistani families, we conducted whole-exome sequencing on affected individuals from two families. We identified disease-causing homozygous mutations in the TYR (NM_000372) and OCA2 (NM_000275.3) genes that segregated within their respective pedigrees. In family AL01, we identified a novel mutation in the TYR gene, resulting in a missense change, c.1280T>C, leading to p.V427A. In family AL02, we detected a splice site variant, c.1045-15T>G in OCA2 gene. Protein model of the V427A mutation within the tyrosinase protein predicted that as the mutant amino acid was considerably smaller in size than the wild type, it might have created a potential gap in protein’s core structure. The V427A mutation is positioned centrally within the Lumenal melanosome repeat domain raises concerns about potential structural alterations in this domain due to disparities between the wild-type and mutant residue, potentially leading to a loss of function in this repeated region. Our study provides a deeper understanding of the molecular basis of OCA in consanguineous Pakistani families by identifying disease-causing mutations in the TYR and OCA2 genes. The novel TYR mutation, V427A, offers insights on the structural consequences of this mutation, which could have implications for understanding the pathology of OCA and potentially effecting future diagnostic and therapeutic approaches for individuals affected by this rare genetic disorder.
- 9 May 2025
- Published by Springer Nature in Biochemical Genetics
- Vol. 64 (2) , 2048-2065
Molecular Characterization of Oculocutaneous Albinism in Consanguineous Pakistani Families: Unraveling Disease-Causing Pathogenic Variants in OCA2 and TYR Genes for Precision Diagnosis
Oculocutaneous albinism is a rare genetic disorder characterized by the absence or reduction of melanin pigment in the skin, hair, and eyes, leading to various visual and dermatological challenges. To shed light on the molecular pathology of OCA in consanguineous Pakistani families, we conducted whole-exome sequencing on affected individuals from two families. We identified disease-causing homozygous mutations in the TYR (NM_000372) and OCA2 (NM_000275.3) genes that segregated within their respective pedigrees. In family AL01, we identified a novel mutation in the TYR gene, resulting in a missense change, c.1280T>C, leading to p.V427A. In family AL02, we detected a splice site variant, c.1045-15T>G in OCA2 gene. Protein model of the V427A mutation within the tyrosinase protein predicted that as the mutant amino acid was considerably smaller in size than the wild type, it might have created a potential gap in protein’s core structure. The V427A mutation is positioned centrally within the Lumenal melanosome repeat domain raises concerns about potential structural alterations in this domain due to disparities between the wild-type and mutant residue, potentially leading to a loss of function in this repeated region. Our study provides a deeper understanding of the molecular basis of OCA in consanguineous Pakistani families by identifying disease-causing mutations in the TYR and OCA2 genes. The novel TYR mutation, V427A, offers insights on the structural consequences of this mutation, which could have implications for understanding the pathology of OCA and potentially effecting future diagnostic and therapeutic approaches for individuals affected by this rare genetic disorder.