Publikationer av Hanna Lindberg
Refereegranskade
Artiklar
[1]
M. Ek et al., "An anti-sortilin affibody-peptide fusion inhibits sortilin-mediated progranulin degradation," Frontiers in Immunology, vol. 15, 2024.
[2]
S. Ståhl et al., "Cloning of Affibody Libraries for Display Methods," Cold Spring Harbor Protocols, vol. 2024, no. 11, 2024.
[3]
S. Ståhl et al., "Engineering of Affibody Molecules," Cold Spring Harbor Protocols, vol. 2024, no. 11, 2024.
[4]
C. Dahlsson Leitao et al., "Selection of Affibody Molecules Using Escherichia coli Display," Cold Spring Harbor Protocols, vol. 2024, no. 11, 2024.
[5]
L. C. Hjelm et al., "Selection of Affibody Molecules Using Phage Display," Cold Spring Harbor Protocols, vol. 2024, no. 11, 2024.
[6]
J. Löfblom et al., "Selection of Affibody Molecules Using Staphylococcal Display," Cold Spring Harbor Protocols, vol. 2024, no. 11, 2024.
[7]
L. C. Hjelm et al., "Affibody Molecules Intended for Receptor-Mediated Transcytosis via the Transferrin Receptor," Pharmaceuticals, vol. 16, no. 7, 2023.
[8]
L. C. Hjelm et al., "Construction and Validation of a New Naive Sequestrin Library for Directed Evolution of Binders against Aggregation-Prone Peptides," International Journal of Molecular Sciences, vol. 24, no. 1, 2023.
[9]
C. D. Leitao et al., "Display of a naïve affibody library on staphylococci for selection of binders by means of flow cytometry sorting," Biochemical and Biophysical Research Communications - BBRC, vol. 655, s. 75-81, 2023.
[10]
R. Faresjö et al., "Transferrin Receptor Binding BBB-Shuttle Facilitates Brain Delivery of Anti-Aβ-Affibodies," Pharmaceutical research, vol. 39, no. 7, s. 1509-1521, 2022.
[11]
S. Meister et al., "An Affibody Molecule Is Actively Transported into the Cerebrospinal Fluid via Binding to the Transferrin Receptor," International Journal of Molecular Sciences, vol. 21, no. 8, s. 2999, 2020.
[12]
A. Boutajangout et al., "Affibody-Mediated Sequestration of Amyloid beta Demonstrates Preventive Efficacy in a Transgenic Alzheimer's Disease Mouse Model," Frontiers in Aging Neuroscience, vol. 11, 2019.
[13]
H. Lindberg et al., "Flow-cytometric screening of aggregation-inhibitors using a fluorescence-assisted intracellular method," Biotechnology Journal, vol. 12, no. 1, 2017.
[14]
E. Wahlberg et al., "Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid-β," Scientific Reports, vol. 7, no. 1, 2017.
[15]
M. Malm et al., "Inhibiting HER3-Mediated Tumor Cell Growth with Affibody Molecules Engineered to Low Picomolar Affinity by Position-Directed Error-Prone PCR-Like Diversification," PLOS ONE, vol. 8, no. 5, s. e62791, 2013.
[16]
H. Lindberg et al., "Staphylococcal display for combinatorial protein engineering of a head-to-tail affibody dimer binding the Alzheimer amyloid-ss peptide," Biotechnology Journal, vol. 8, no. 1, s. 139-145, 2013.
[17]
H. Lindberg et al., "Evaluation of a HER2-targeting affibody molecule combining an N-terminal HEHEHE-tag with a GGGC chelator for Tc-99m-labelling at the C terminus," Tumor Biology, vol. 33, no. 3, s. 641-651, 2012.
Icke refereegranskade
Artiklar
[18]
J. H. Greenberg et al., "The Role of Affibody in Aged Mouse Model of Alzheimer's Disease," Journal of The American Geriatrics Society, vol. 68, s. S341-S341, 2020.
[19]
H. Lindberg et al., "A truncated and dimeric format of an Affibody library on bacteria enables FACS-mediated isolation of amyloid-beta aggregation inhibitors with subnanomolar affinity," Biotechnology Journal, vol. 10, no. 11, s. 1707-1718, 2015.
[20]
A. Orlova et al., "Feasibility of radionuclide imaging of HER3-expressing tumors using affibody molecules," Journal of labelled compounds & radiopharmaceuticals, vol. 56, s. S11-S11, 2013.
[21]
A. Orlova et al., "Feasibility of radionuclide imaging of HER3-expressing tumours using technetium-99m labeled affibody molecules," European Journal of Nuclear Medicine and Molecular Imaging, vol. 40, s. S185-S186, 2013.
Avhandlingar
[22]
H. Lindberg, "Engineering of Affibody molecules targeting the Alzheimer’s-related amyloid β peptide," Doktorsavhandling Stockholm : KTH Royal Institute of Technology, TRITA-BIO-Report, 2015:14, 2015.
Övriga
[23]
L. C. Hjelm et al., "Affibody molecules intended for receptor-mediated transcytosis via the transferrin receptor," (Manuskript).
[24]
A. Boutajangout et al., "Affibody-mediated Reduction of Amyloid Burden and Improvement of Cognitive Decline in an Animal Model of Alzheimer’s disease," (Manuskript).
[25]
H. Lindberg et al., "Development of a fluorescence-based intracellular method for function-based isolation of protein-based aggregation inhibitors," (Manuskript).
[26]
E. Wahlberg et al., "Selection of binding proteins that specifically recognize protofibrillar aggregates of amyloid-β," (Manuskript).
[27]
L. C. Hjelm et al., "Sequestrins inhibiting amyloidogenic aggregation-prone peptides," (Manuskript).
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2025-07-13 01:03:10 UTC