Muhammed Muazzam Kamil Syed

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Amyloid self-assembly of alpha-synuclein (alpha Syn) is linked to the pathogenesis of Parkinson's disease (PD). Type 2 diabetes (T2D) has recently emerged as a risk factor for PD. Cross-interactions between their amyloidogenic proteins may act as molecular ...

Increasing evidence suggests that the process of alpha-synuclein (alpha-syn) aggregation from monomers into amyloid fibrils and Lewy bodies, via oligomeric intermediates plays an essential role in the pathogenesis of different synucleinopathies, including ...

Die amyloide Selbstassemblierung von α‐Synuclein (αSyn) wird mit der Pathogenese der Parkinson‐Krankheit (PD) in Verbindung gebracht. Typ 2 Diabetes (T2D) hat sich kürzlich als Risikofaktor für PD herausgestellt. Kreuzinteraktionen zwischen den amyloidogen ...

Alpha-synuclein aggregation and mitochondrial dysfunction are main pathological hallmarks of Parkinson's disease (PD) and several other neurodegenerative diseases, collectively known as synucleinopathies. However, increasing evidence suggests that they may ...

Several lines of research point to a key role of low oxygen supply (hypoxia) in Parkinson's disease pathogenesis. Although severe hypoxia is detrimental for the brain, physiological adaptations to mild hypoxia are neuroprotective. Herein we discuss, how ne ...

Muhammed Muazzam Kamil Syed

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Multi-Targeting Macrocyclic Peptides as Nanomolar Inhibitors of Self- and Cross-Seeded Amyloid Self-Assembly of α-Synuclein

A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of alpha-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in alpha-synuclein research

Multi‐Targeting Makrozyklische Peptide als Nanomolare Inhibitoren der Selbst‐ und Kreuznukleation der Amyloiden Selbstassemblierung von α‐Synuclein

Fatal attraction-The role of hypoxia when alpha-synuclein gets intimate with mitochondria

Hypoxia Conditioning as a Promising Therapeutic Target in Parkinson's Disease?

Identification of key segments of IAPP/aSyn cross-amyloid interactions