Sidra Islam
Aligarh Muslim University
13 Papers
29 Citations
Sidra Islam is an academic researcher from Aligarh Muslim University. The author has contributed to research in topics: Chemistry & Glycation. The author has an hindex of 8, co-authored 11 publications. Previous affiliations of Sidra Islam include Case Western Reserve University & Jawaharlal Nehru Medical College, Aligarh.
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Papers
Biophysical and biochemical studies on glycoxidatively modified human low density lipoprotein.
Minhal Abidi,M. Salman Khan,Saheem Ahmad,Tasneem Kausar,Shahid M. Nayeem,Sidra Islam,Asif Ali,Khursheed Alam,Moinuddin +8 more
TL;DR: The structural perturbations in LDL upon modification with MGO which could obstruct its normal physiological functions and hence contribute to disease pathogenesis and associated complications are reported.
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Glycation, oxidation and glycoxidation of IgG: a biophysical, biochemical, immunological and hematological study.
Sidra Islam,Moinuddin,Abdul Rouf Mir,Abdul Rouf Mir,Alok Raghav,Safia Habib,Khursheed Alam,Asif Ali +7 more
TL;DR: The glycoxidative modification of IgG caused maximum alteration in the IgG as compared to the glycatively and oxidatively modified protein, and led to activation of inflammatory pathways.
24
Studies on glycoxidatively modified human IgG: Implications in immuno-pathology of type 2 diabetes mellitus.
TL;DR: Methylglyoxal modified human immunoglobulin G (MG-IgG) was found to perturb the structural integrity of IgG, affect its aromatic micro-environment and cause the generation of advanced glycation end products (AGEs) and aggregate adducts.
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Immunochemical studies on HNE-modified HSA: Anti-HNE-HSA antibodies as a probe for HNE damaged albumin in SLE.
TL;DR: The experimentally induced anti-HNE-HSA antibodies appreciably recognized HNE modified epitopes on the HSA obtained from SLE patients and form a good immunochemical probe to detect such damages in lupus patients.
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Methylglyoxal modified IgG generates autoimmune response in rheumatoid arthritis.
TL;DR: The IgG modification in RA patients under alter carbonyl concentrations is established and suggests that the interaction of the methylglyoxal with the IgG has consequences in the autoimmunopathology of rheumatoid arthritis.
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