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Publications by John Löfblom

Refereegranskade

Artiklar

[2]
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, pp. 2999, 2020.
[3]
S. S. Rinne et al., "Benefit of Later-Time-Point PET Imaging of HER3 Expression Using Optimized Radiocobalt-Labeled Affibody Molecules," International Journal of Molecular Sciences, vol. 21, no. 6, 2020.
[4]
H. Chaudhary et al., "Dissecting the structural organization of multiprotein amyloid aggregates using a bottom-up approach," ACS Chemical Neuroscience, vol. 11, no. 10, pp. 1447-1457, 2020.
[7]
S. S. Rinne et al., "Influence of Residualizing Properties of the Radiolabel on Radionuclide Molecular Imaging of HER3 Using Affibody Molecules," International Journal of Molecular Sciences, vol. 21, no. 4, 2020.
[10]
[11]
[14]
S. Meister, N. Hendrikse and J. Löfblom, "Directed evolution of the 3C protease from coxsackievirus using a novel fluorescence-assisted intracellular method," Biological chemistry (Print), vol. 400, no. 3, pp. 405-415, 2019.
[27]
S. Ståhl et al., "Affibody Molecules in Biotechnological and Medical Applications," Trends in Biotechnology, vol. 35, no. 8, pp. 691-712, 2017.
[28]
M. Rosestedt et al., "Evaluation of a radiocobalt-labelled affibody molecule for imaging of human epidermal growth factor receptor 3 expression," International Journal of Oncology, vol. 51, no. 6, pp. 1765-1774, 2017.
[32]
M. Nosrati et al., "Insights from engineering the Affibody-Fc interaction with a computational-experimental method," Protein Engineering Design & Selection, vol. 30, no. 9, pp. 593-601, 2017.
[33]
L. Sandersjöö, A. Jonsson and J. Löfblom, "Protease substrate profiling using bacterial display of self-blocking affinity proteins and flow-cytometric sorting," Biotechnology Journal, vol. 12, no. 1, 2017.
[34]
J. Löfblom et al., "Staphylococcus carnosus : from starter culture to protein engineering platform," Applied Microbiology and Biotechnology, vol. 101, no. 23-24, pp. 8293-8307, 2017.
[36]
J. Garousi et al., "Comparative Evaluation of Affibody Molecules for Radionuclide Imaging of in Vivo Expression of Carbonic Anhydrase IX," Molecular Pharmaceutics, vol. 13, no. 11, pp. 3676-3687, 2016.
[37]
M. Rosestedt et al., "Development and Evaluation of Radiocobalt-labelled Affibody Molecule for Next Day PET Imaging of HER3 Expression," European Journal of Nuclear Medicine and Molecular Imaging, vol. 43, pp. S37-S38, 2016.
[39]
B. Mitran et al., "Feasibility of in vivo imaging of VEGFR2 expression using high affinity antagonistic biparatopic affibody construct Z(VEGFR2)-Bp(2)," European Journal of Nuclear Medicine and Molecular Imaging, vol. 43, pp. S97-S98, 2016.
[40]
M. Oroujeni et al., "Imaging of EGFR Expression Using 99mTC-Labelled ZEGFR:2377 Affibody Molecule," European Journal of Nuclear Medicine and Molecular Imaging, vol. 43, pp. S238-S238, 2016.
[43]
F. Fleetwood et al., "Novel affinity binders for neutralization of vascular endothelial growth factor (VEGF) signaling," Cellular and Molecular Life Sciences (CMLS), vol. 73, no. 8, pp. 1671-1683, 2016.
[44]
J. Garousi et al., "PET imaging of epidermal growth factor receptor expression in tumours using Zr-89-labelled ZEGFR:2377 affibody molecules," International Journal of Oncology, vol. 48, no. 4, pp. 1325-1332, 2016.
[45]
M. Malm et al., "Targeting HER3 using mono- and bispecific antibodies or alternative scaffolds," mAbs, vol. 8, no. 7, pp. 1195-1209, 2016.
[46]
L. Sandersjöö, A. Jonsson and J. Löfblom, "A new prodrug form of Affibody molecules (pro-Affibody) is selectively activated by cancer-associated proteases," Cellular and Molecular Life Sciences (CMLS), vol. 72, no. 7, pp. 1405-1415, 2015.
[47]
M. Rosestedt et al., "Affibody-mediated PET imaging of HER3 expression in malignant tumours," Scientific Reports, vol. 5, 2015.
[49]
L. Sandersjöö et al., "A protease substrate profiling method that links site-specific proteolysis with antibiotic resistance," Biotechnology Journal, vol. 9, no. 1, pp. 155-162, 2014.
[50]
J. Seijsing et al., "An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein," Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 48, pp. 17110-17115, 2014.
[54]
A. Orlova et al., "Imaging of HER3-expressing xenografts in mice using a Tc-99m(CO)(3)-HEHEHE-Z(HER3:08699) affibody molecule," European Journal of Nuclear Medicine and Molecular Imaging, vol. 41, no. 7, pp. 1450-1459, 2014.
[55]
M. Altai et al., "Re-188-Z(HER2:V2), a Promising Affibody-Based Targeting Agent Against HER2-Expressing Tumors : Preclinical Assessment," Journal of Nuclear Medicine, vol. 55, no. 11, pp. 1842-1848, 2014.
[56]
M. Altai et al., "Selection of an optimal cysteine-containing peptide-based chelator for labeling of affibody molecules with (188)Re.," European Journal of Medicinal Chemistry, vol. 87, pp. 519-28, 2014.
[58]
S. Ståhl et al., "Affinity proteins and their generation," Journal of chemical technology and biotechnology (1986), vol. 88, no. 1, pp. 25-38, 2013.
[59]
J. Nilvebrant et al., "Development and characterization of small bispecific albumin-binding domains with high affinity for ErbB3," Cellular and Molecular Life Sciences (CMLS), vol. 70, no. 20, pp. 3973-3985, 2013.
[63]
F. Fleetwood et al., "Surface display of a single-domain antibody library on Gram-positive bacteria," Cellular and Molecular Life Sciences (CMLS), vol. 70, no. 6, pp. 1081-1093, 2013.
[64]
L. Göstring et al., "Cellular Effects of HER3-Specific Affibody Molecules," PLOS ONE, vol. 7, no. 6, pp. e40023, 2012.
[65]
S. Schlegel et al., "Optimizing Membrane Protein Overexpression in the Escherichia coli strain Lemo21(DE3)," Journal of Molecular Biology, vol. 423, no. 4, pp. 648-659, 2012.
[67]
J. Löfblom, "Bacterial display in combinatorial protein engineering," Biotechnology Journal, vol. 6, no. 9, pp. 1115-1129, 2011.
[68]
N. Kronqvist et al., "Combining phage and staphylococcal surface display for generation of ErbB3-specific Affibody molecules," Protein Engineering Design & Selection, vol. 24, no. 4, pp. 385-396, 2011.
[69]
J. Nilvebrant et al., "Engineering Bispecificity into a Single Albumin-Binding Domain," PLOS ONE, vol. 6, no. 10, pp. e25791, 2011.
[70]
J. Löfblom, F. Y. Frejd and S. Ståhl, "Non-immunoglobulin based protein scaffolds," Current Opinion in Biotechnology, vol. 22, no. 6, pp. 843-848, 2011.
[71]
J. Löfblom et al., "Affibody molecules : Engineered proteins for therapeutic, diagnostic and biotechnological applications," FEBS Letters, vol. 584, no. 12, pp. 2670-2680, 2010.
[72]
J. Rockberg et al., "Epitope mapping using gram-positive surface display," Current Protocols in Immunology, no. SUPPL. 90, pp. 9.9.1-9.9.17, 2010.
[73]
B. Hjelm et al., "Exploring epitopes of antibodies toward the human tryptophanyl-tRNA synthetase," NEW BIOTECHNOL, vol. 27, no. 2, pp. 129-137, 2010.
[74]
N. Kronqvist et al., "Staphylococcal surface display in combinatorial protein engineering and epitope mapping of antibodies," Recent Patents on Biotechnology, vol. 4, no. 3, pp. 171-182, 2010.
[76]
N. Kronqvist et al., "A novel affinity protein selection system based on staphylococcal cell surface display and flow cytometry," Protein Engineering Design & Selection, vol. 21, no. 4, pp. 247-255, 2008.
[77]
J. Rockberg et al., "Epitope mapping of antibodies using bacterial surface display," Nature Methods, vol. 5, no. 12, pp. 1039-1045, 2008.
[80]
J. Löfblom et al., "Optimization of electroporation-mediated transformation : Staphylococcus carnosus as model organism," Journal of Applied Microbiology, vol. 102, no. 3, pp. 736-747, 2007.
[81]
J. Löfblom, H. Wernérus and S. Ståhl, "Fine affinity discrimination by normalized fluorescence activated cell sorting in staphylococcal surface display," FEMS Microbiology Letters, vol. 248, no. 2, pp. 189-198, 2005.

Kapitel i böcker

[82]
J. Löfblom and F. Frejd, "Alternative Scaffolds as Bispecific Antibody Mimetics," in Bispecific Antibodies, Roland Kontermann Ed., Berlin Heidelberg : Springer-Verlag, 2011.

Icke refereegranskade

Artiklar

[83]
A. Orlova et al., "Affibody-based Theranostics for HER3-expressing cancers : tumor growth inhibition, and PET-imaging of HER3 for therapy monitoring in a preclinical model," European Journal of Nuclear Medicine and Molecular Imaging, vol. 47, no. SUPPL 1, pp. S13-S14, 2020.
[85]
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, pp. S341-S341, 2020.
[86]
J. Garousi et al., "Comparison Of Affibody- And Antibody Fragments-based Caix Imaging Probes In Mice Bearing Renal Cell Carcinoma Xenografts," European Journal of Nuclear Medicine and Molecular Imaging, vol. 46, no. Suppl 1, pp. S580-S580, 2019.
[87]
A. Vorobyeva et al., "N-terminal position of histidine-glutamate-containing tag improves biodistribution of [Tc-99m]Tc-labeled DARPin G3," European Journal of Nuclear Medicine and Molecular Imaging, vol. 46, no. SUPPL 1, pp. S749-S749, 2019.
[88]
S. Rinne et al., "Optimizing affibody-mediated PET imaging of HER3 expression using long-lived radiocobalt for the next day PET image," European Journal of Nuclear Medicine and Molecular Imaging, vol. 46, no. SUPPL 1, pp. S436-S436, 2019.
[89]
S. Rinne et al., "Optimizing the molecular design of Ga-68-labeled affibody molecules for in vivo PET imaging of HER3 expression," Journal of labelled compounds & radiopharmaceuticals, vol. 62, pp. S468-S470, 2019.
[90]
M. Oroujeni et al., "Comparative evaluation of anti-EFGR affibody molecules labelled with gallium-68 and zirconium-89 using desferrioxamine B as a chelator," European Journal of Nuclear Medicine and Molecular Imaging, vol. 45, pp. S674-S675, 2018.
[91]
A. Orlova et al., "Imaging contrast of HER3 expression using monomeric affibody-based imaging probe can be improved by co-injection of affibody trimer," European Journal of Nuclear Medicine and Molecular Imaging, vol. 45, pp. S673-S673, 2018.
[92]
S. Rinne et al., "Optimization of molecular design of Ga-68-labeled affibody molecule for PET imaging of HER3 expression," European Journal of Nuclear Medicine and Molecular Imaging, vol. 45, pp. S109-S109, 2018.
[93]
M. Oroujeni et al., "Influence of composition of cysteine-containing peptide based chelators on biodistribution of Tc-99m-labelled anti-EGFR affibody molecules," European Journal of Nuclear Medicine and Molecular Imaging, vol. 44, pp. S347-S348, 2017.
[94]
B. Mitran et al., "Novel high affinity affibody for radionuclide imaging of VEGFR2 in glioma vasculature : proof-of-principle in murine model," European Journal of Nuclear Medicine and Molecular Imaging, vol. 44, pp. S239-S239, 2017.
[95]
S. S. Rinne et al., "Optimization of affibody molecule for imaging of HER3 expression : negatively charged metal-chelator complex increases imaging contrast," European Journal of Nuclear Medicine and Molecular Imaging, vol. 44, pp. S539-S540, 2017.
[96]
B. Mitran et al., "Radiocobalt-labeled anti-HER1 affibody molecule DOTA-Z(EGFR:2377) for imaging of low HER1 expression in prostate cancer pre-clinical model," European Journal of Nuclear Medicine and Molecular Imaging, vol. 44, pp. S145-S145, 2017.
[98]
K. G. Andersson et al., "111In-labeled NOTA-conjugated Affibody molecules for visualization of HER3 expression in malignant tumors," European Journal of Nuclear Medicine and Molecular Imaging, vol. 41, pp. S311-S311, 2014.
[99]
[100]
M. Rosestedt et al., "PET Imaging of HER3-Expression in Tumours Using a 68Ga-Labeled Affibody Molecule," European Journal of Nuclear Medicine and Molecular Imaging, vol. 41, pp. S310-S310, 2014.
[101]
J. Nilvebrant et al., "Engineering bispecificity into a single albumin-binding domain aimed for drug targeting and in vivo half-life extension," Current Opinion in Biotechnology, vol. 24, pp. S35-S35, 2013.
[102]
A. Orlova et al., "Feasibility of radionuclide imaging of HER3-expressing tumors using affibody molecules," Journal of labelled compounds & radiopharmaceuticals, vol. 56, pp. S11-S11, 2013.
[103]
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, pp. S185-S186, 2013.
[104]
M. Altai et al., "Re-188-Z(HER2 : V2), a promising targeting agent against HER2-expressing tumors: in vitro and in vivo assessment," European Journal of Nuclear Medicine and Molecular Imaging, vol. 40, pp. S119-S119, 2013.
[105]
M. Altai et al., "Selection of an optimal cysteine-containing peptide-based chelator for labeling of Affibody molecules with Re-188," European Journal of Nuclear Medicine and Molecular Imaging, vol. 40, pp. S219-S220, 2013.
[106]
J. Löfblom, "Bacterial display in directed evolution for generation of new biopharmaceuticals," Biotech International, vol. 23, no. June, pp. 26-29, 2011.

Avhandlingar

[107]

Övriga

Senaste synkning med DiVA:
2021-10-15 01:48:31