Author

K. Sahin

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Pharmacology & Toxicology· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:drug response / drug discovery· 2 Organism:mouse· 2 Research Focus:host-pathogen & immune response· 1 Organism:rat· 1 Assay:structural biology· 1 Organism:virus· 1

Frequent Co-Authors

F. Uckun· 3 shared c. orhan· 2 shared I. Ozercan· 2 shared M. Gitterle· 2 shared M. Volk· 2 shared A. B. Peksen· 1 shared A. Barty· 1 shared A. Batyuk· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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3 shared papersPharmacology & Toxicology

F. Uckun

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Non-clinical safety profile and pharmacodynamics of two formulations of the anti-sepsis drug candidate Rejuveinix

F. Uckun, c. orhan, J. Powell, E. Sahin, I. Ozercan, M. Volk, K. Sahin

This study shows two Rejuveinix formulations have a favorable safety profile in rats and similarly increase antioxidant levels in tissues, indicating bioequivalence.

bioRxiv · Jan 3, 2021Pharmacology & Toxicology

Rejuveinix Mitigates Sepsis-Associated Oxidative Stress in the Brain of Mice: Clinical Impact Potential in COVID-19 and Nervous System Disorders

F. Uckun, M. Tuzcu, M. Gitterle, M. Volk, K. Sahin

Rejuveinix improves survival in sepsis model mice by reducing brain oxidative stress, suggesting potential for neuroprotective use in sepsis and COVID-19.

bioRxiv · Jan 3, 2021 · PreprintPharmacology & Toxicology

Rejuveinix Reverses Severe Inflammatory Lung Damage in a Mouse Model of Fatal Sepsis

F. Uckun, I. Ozercan, C. Orhan, M. Gitterle, K. Sahin

This study shows that Rejuveinix reduces severe inflammatory lung damage and improves survival in a mouse model of sepsis at a low dose.

bioRxiv · Dec 31, 2020 · PreprintPharmacology & Toxicology

Near-Physiological-Temperature Serial Femtosecond X-ray Crystallography Reveals Novel Conformations of SARS-CoV-2 Main Protease Active Site for Improved Drug Repurposing

S. Durdagi, C. Dag, B. Dogan, M. Yigin, T. Avsar, C. Buyukdag, I. Erol, F. B. Ertem, S. Calis, G. Yildirim, M. Orhan, O. Guven, B. Aksoydan, E. Destan, K. Sahin, , Sn

The paper determines two apo structures of SARS-CoV-2 main protease at near-physiological temperature using SFX and uses molecular simulations to analyze inhibitor binding for drug repurposing.

bioRxiv · Sep 9, 2020Biophysics