Dag Sehlin

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Associate professor

Uppsala Universitet Medicinska fakulteten

Sweden

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About

Dag Sehlin is an Associate Professor at Uppsala Universitet Medicinska fakulteten in Sweden. His research focuses on neurodegenerative diseases, particularly Alzheimer's, with recent articles exploring bispecific antibodies, PET imaging techniques, and lipid analysis in brain tissues. His work contributes to understanding amyloid-beta pathology and the blood-brain barrier's interactions with therapeutic agents.

Recent Grants

Grant: Close

Hjärnpenetrerande antikroppar för behandling av neurodegenerativa sjukdomar

Open Date: 2022-01-01

Close Date: 2024-12-31

Grant: Close

Utveckling av en neuroimaging-biomarkör för att identifiera ett pro-koagulatoriskt tillstånd vid Alzheimers sjukdom

Open Date: 2021-01-01

Close Date: 2023-12-31

Grant: Close

Ökat hjärnupptag av antikroppar för effektiv behandling av neurodegenerativa sjukdomar

Open Date: 2019-01-01

Close Date: 2021-12-31

Articles (26)

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Collaborators (8)

Anna Erlandsson

Senior University Lecturer

Uppsala University

SWEDEN

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Gunnar Schröder

Technische Universität Dortmund Fakultät Physik

GERMANY

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Enrica Cerilli

Uppsala University

SWEDEN

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Jonas Eriksson

Uppsala University

SWEDEN

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Stina Syvänen

Associate Professor

Uppsala University

SWEDEN

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Vladimir Shalgunov

Københavns Universitet

DENMARK

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Greta Hultqvist

Senior Lecturer/ docent

Uppsala University

SWEDEN

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Matthias Herth

Associate Professor

Københavns Universitet

DENMARK

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Dag Sehlin

Research Interests

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About

Recent Grants

Articles (26)

Bispecific brain-penetrant antibodies for treatment of Alzheimer’s disease

PET imaging of TREM2 in amyloid-beta induced neuroinflammation

Comprehensive Approach for Sequential MALDI-MSI Analysis of Lipids, N-Glycans, and Peptides in Fresh-Frozen Rodent Brain Tissues

Fluorine-18 ImmunoPET Imaging of Antibody Brain Kinetics and Amyloid-Beta Pathology

Dual-ligand fluorescence microscopy enables chronological and spatial histological assignment of distinct amyloid-β deposits

Reducing neonatal Fc receptor binding enhances clearance and brain-to-blood ratio of TfR-delivered bispecific amyloid-β antibody

Indium-111 radiolabelling of a brain-penetrant Aβ antibody for SPECT imaging

Antibody engagement with amyloid‐beta does not inhibit [11C]PiB binding for PET imaging

Synthesis and evaluation of fluorine-18 labelled tetrazines as pre-targeting imaging agents for PET

Amyloid-β deposits in human astrocytes contain truncated and highly resistant proteoforms

Comparing in vitro affinity measurements of antibodies to TfR1: Surface plasmon resonance versus on-cell affinity

Altered amyloid-β structure markedly reduces gliosis in the brain of mice harboring the Uppsala APP deletion

Single domain antibody-scFv conjugate targeting amyloid β and TfR penetrates the blood–brain barrier and interacts with amyloid β

Cryo-EM of Aβ fibrils from mouse models find tg-APP<sub>ArcSwe</sub> fibrils resemble those found in patients with sporadic Alzheimer’s disease

Synaptic density in aging mice measured by [<sup>18</sup>F]SynVesT-1 PET

Age, dose, and binding to TfR on blood cells influence brain delivery of a TfR-transported antibody

Functionalization of Radiolabeled Antibodies to Enhance Peripheral Clearance for High Contrast Brain Imaging

PET Imaging in Preclinical Anti-Aβ Drug Development

Reduction of αSYN Pathology in a Mouse Model of PD Using a Brain-Penetrating Bispecific Antibody

In vivo imaging of alpha-synuclein with antibody-based PET.

Pretargeted Imaging beyond the Blood–Brain Barrier

ImmunoPET imaging of amyloid-beta in a rat model of Alzheimer’s disease with a bispecific, brain-penetrating fusion protein

Transferrin Receptor Binding BBB-Shuttle Facilitates Brain Delivery of Anti-Aβ-Affibodies

Passive and receptor mediated brain delivery of an anti-GFAP nanobody.

Novel multivalent design of a monoclonal antibody improves binding strength to soluble aggregates of amyloid beta.

The <i>Uppsala APP</i> deletion causes early onset autosomal dominant Alzheimer's disease by altering APP processing and increasing amyloid β fibril formation.

Collaborators (8)

Anna Erlandsson

Gunnar Schröder

Enrica Cerilli

Jonas Eriksson

Stina Syvänen

Vladimir Shalgunov

Greta Hultqvist

Matthias Herth

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