Nikolaos Louros

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Assistant Professor

University of Texas Southwestern Medical Center

United States

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Nikolaos Louros is an Assistant Professor at the University of Texas Southwestern Medical Center in the United States. His research focuses on protein misfolding, amyloid pathology, and the development of novel therapeutic strategies for neurodegenerative diseases such as Alzheimer's. He has contributed significantly to the field through recent publications exploring amyloid interactions, single-cell infrared spectroscopy, and the protective mechanisms against protein aggregation.

Recent Grants

Grant: Close

Microfluidics-based counting of individual amyloid seeding particles in Alzheimer’s disease

Open Date: 2023-01-01

Close Date: 2025-01-01

Grant: Close

Een high-throughput platform voor het screenen van amyloïdstammen en hun seedingcapaciteit met moleculaire resolutie

Open Date: 2021-10-01

Close Date: 2024-09-30

Grant: Close

Investigating the role of proteomic context in Alzheimer's disease

Open Date: 2020-01-01

Close Date: 2022-01-01

Grant: Close

Principes van specificiteit in kruis-aggregatie interacties

Open Date: 2018-10-01

Close Date: 2021-09-30

Articles (17)

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2022

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2022

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2022

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2022

Collaborators (13)

Wim Versées

Vrije Universiteit Brussel

BELGIUM

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Joost Schymkowitz

Professor

Katholieke Universiteit Leuven

BELGIUM

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Vita Sereikaite

Københavns Universitet

DENMARK

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Frédéric A Meunier

AUSTRALIA

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Christine Helsen

Vrije Universiteit Brussel

BELGIUM

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Sam D'Haeyer

Vlaams Instituut voor Biotechnologie

BELGIUM

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Lary Walker

Marie and E.R. Snelling Professor

Emory University

UNITED STATES

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Deborah Kronenberg-Versteeg

University of Tübingen

GERMANY

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Jillian Madine

Lecturer

University of Liverpool

UNITED KINGDOM

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Morten Kam Dahl Dueholm

Aalborg University

DENMARK

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Ella Martin

Vrije Universiteit Brussel

BELGIUM

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Kristian Strømgaard

Københavns Universitet

DENMARK

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Katrien Princen

Head in vitro drug development

reMYND NV

BELGIUM

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Nikolaos Louros

Research Interests

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About

Recent Grants

Articles (17)

Interactions between pathological and functional amyloid: A match made in Heaven or Hell?

An end-to-end approach for single-cell infrared absorption spectroscopy of bacterial inclusion bodies: from AFM-IR measurement to data interpretation of large sample sets

Pharmacological modulation of septins restores calcium homeostasis and is neuroprotective in models of Alzheimer’s disease

CORDAX web server: an online platform for the prediction and 3D visualization of aggregation motifs in protein sequences

Local structural preferences in shaping tau amyloid polymorphism

N-glycosylation as a eukaryotic protective mechanism against protein aggregation

Mechanisms and pathology of protein misfolding and aggregation

Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation

Enhanced therapeutic window for antimicrobial Pept-ins by investigating their structure-activity relationship

Enhanced therapeutic window for antimicrobial Pept-ins by investigating their structure-activity relationship

EndophilinA-dependent coupling between activity-induced calcium influx and synaptic autophagy is disrupted by a Parkinson-risk mutation.

Exploiting the intrinsic misfolding propensity of the KRAS oncoprotein.

Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation

Medin co-aggregates with vascular amyloid-β in Alzheimer’s disease

Exploiting Ligand-binding Domain Dimerization for Development of Novel Androgen Receptor Inhibitors

Tau amyloid polymorphism is shaped by local structural propensities of its protein sequence

Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study.

Collaborators (13)

Wim Versées

Joost Schymkowitz

Vita Sereikaite

Frédéric A Meunier

Christine Helsen

Sam D'Haeyer

Lary Walker

Deborah Kronenberg-Versteeg

Jillian Madine

Morten Kam Dahl Dueholm

Ella Martin

Kristian Strømgaard

Katrien Princen

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