Alvaro Mallagaray

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Ternured-Track Assistant Professor

University of Luebeck

Germany

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About

Dr. Alvaro Mallagaray is a Tenured-Track Assistant Professor at the University of Luebeck in Germany. His research focuses on NMR-based techniques in the assessment of glycosylations related to cancer and metabolic traits, as well as studies on protein interactions and immune evasion mechanisms. Recent publications include investigations into the binding dynamics of glycan interactions and the structural properties of viral proteins.

Recent Grants

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Glycans Controlling Non-Enveloped Virus Infections

Open Date: 2016-04-01

Close Date:

Grant: Close

Targeting Norovirus Receptor Interactions at Atomic Resolution

Open Date: 2013-04-01

Close Date: 2015-04-01

Grant: Close

NMR characterization of the interaction between natural and synthetic TLR4-active compounds and the innate immunity receptor MD-2

Open Date: 2013-01-01

Close Date: 2013-03-01

Grant: Close

Síntesis de moléculas con actividad biológica basada en procesos dominó catalizadas por metales de transición

Open Date: 2005-09-01

Close Date: 2009-09-01

Articles (16)

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2025

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2025

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2023

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2022

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2022

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2021

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2021

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University of Lübeck

GERMANY

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Marc Ehlers

Professor and Head of the Laboratories of Immunology and Antibody Glycan Analysis

GERMANY

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Alvaro Mallagaray

Research Interests

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About

Recent Grants

Articles (16)

PNPLA3 I148M variant links to adverse metabolic traits in MASLD during fasting and feeding

Fast NMR-Based Assessment of Cancer-Associated Protein Glycosylations from Serum Samples

Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein

Towards a Precise NMR Quantification of Acute Phase Inflammation Proteins from Human Serum

Towards a Precise NMR Quantification of Acute Phase Inflammation Proteins from Human Serum

Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases

Binding of Glycans to the SARS CoV‐2 Spike Protein, an Open Question: NMR Data on Binding Site Localization, Affinity, and Selectivity

Distinct dissociation rates of murine and human norovirus P-domain dimers suggest a role of dimer stability in virus-host interactions

Norovirus–glycan interactions — how strong are they really?

Assignment of Ala, Ile, LeuproS, Met, and ValproS methyl groups of the protruding domain of murine norovirus capsid protein VP1 using methyl–methyl NOEs, site directed mutagenesis, and pseudocontact shifts

Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins

Generation of glycan-specific nanobodies

Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry

Glycan-Induced Protein Dynamics in Human Norovirus P Dimers Depend on Virus Strain and Deamidation Status

NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins

Complete assignment of Ala, Ile, LeuProS, Met and ValProS methyl groups of the protruding domain from human norovirus GII.4 Saga

Collaborators (11)

Felix Goerdeler

Matthias Stein

Mario Schubert

Charlotte Uetrecht

Marcelo Guerin

Thomas Peters

Gergő Péter Szekeres

Georg Wallmann

Jonathan Du

Svenja Meyhöfer

Marc Ehlers

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