scispace - formally typeset
K

Khalid Iqbal

Researcher at COMSATS Institute of Information Technology

Publications -  295
Citations -  13428

Khalid Iqbal is an academic researcher from COMSATS Institute of Information Technology. The author has contributed to research in topics: Phosphorylation & Tau protein. The author has an hindex of 62, co-authored 276 publications receiving 12115 citations. Previous affiliations of Khalid Iqbal include Islamia University & Shaheed Zulfiqar Ali Bhutto Institute of Science and Technology.

Papers
More filters
Journal ArticleDOI

Distribution of Active Glycogen Synthase Kinase 3β (GSK-3β) in Brains Staged for Alzheimer Disease Neurofibrillary Changes

TL;DR: Direct in situ evidence is found that neurons with tangle-like inclusions positive for active, but not inactive, GSK-3β appear initially in the Pre-α layer of the entorhinal cortex and extend to other brain regions, coincident with the sequence of the development of neurofibrillary changes.
Journal ArticleDOI

Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau.

TL;DR: It is suggested that the abnormally phosphorylated tau can sequester both normal tau and HMW-MAPs and disassemble microtubules but, under physiological conditions, can form tangles of filaments only from tau.
Journal ArticleDOI

Phosphorylation of Microtubule-associated Protein Tau Is Regulated by Protein Phosphatase 2A in Mammalian Brain IMPLICATIONS FOR NEUROFIBRILLARY DEGENERATION IN ALZHEIMER'S DISEASE

TL;DR: It is suggested that protein phosphatase 2A participates in regulation of tau phosphorylation, processing, and function in vivo and can lead to Alzheimer-like abnormal hyperphosphorylated tau.
Journal ArticleDOI

Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain.

TL;DR: It is found that GSK-3 is prominently present in neuronal cell bodies and their processes and co-localizes with neurofibrillary changes in AD brain and is significantly increased in the postsynaptosomal supernatant from AD brains as compared to the controls.