Publications by John Löfblom
Refereegranskade
Artiklar
[1]
L. Parks et al., "Investigation of an AIDA-I based expression system for display of various affinity proteins on Escherichia coli," Biochemical and Biophysical Research Communications - BBRC, vol. 696, 2024.
[2]
L. C. Hjelm et al., "Affibody Molecules Intended for Receptor-Mediated Transcytosis via the Transferrin Receptor," Pharmaceuticals, vol. 16, no. 7, 2023.
[3]
C. D. Leitao et al., "Conditionally activated affibody-based prodrug targeting EGFR demonstrates improved tumour selectivity," Journal of Controlled Release, vol. 357, pp. 185-195, 2023.
[4]
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.
[5]
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, pp. 75-81, 2023.
[6]
A. Mestre Borras et al., "Generation of an anti-idiotypic affibody-based masking domain for conditional activation of EGFR-targeting," New Biotechnology, vol. 73, pp. 9-18, 2023.
[7]
O. Wegrzyniak et al., "Imaging of fibrogenesis in the liver by [18F]TZ-Z0959 : an Affibody molecule targeting platelet derived growth factor receptor β," EJNMMI Radiopharmacy and Chemistry, vol. 8, no. 1, 2023.
[8]
L. C. Hjelm, M. Hedhammar and J. Löfblom, "In vitro Blood-Brain barrier model based on recombinant spider silk protein nanomembranes for evaluation of transcytosis capability of biomolecules," Biochemical and Biophysical Research Communications - BBRC, vol. 669, pp. 77-84, 2023.
[9]
P. Cheung et al., "Preclinical evaluation of Affibody molecule for PET imaging of human pancreatic islets derived from stem cells," EJNMMI Research, vol. 13, no. 1, 2023.
[10]
S. S. Rinne et al., "Targeting Tumor Cells Overexpressing the Human Epidermal Growth Factor Receptor 3 with Potent Drug Conjugates Based on Affibody Molecules," Biomedicines, vol. 10, no. 6, 2022.
[11]
R. Faresjö et al., "Transferrin Receptor Binding BBB-Shuttle Facilitates Brain Delivery of Anti-Aβ-Affibodies," Pharmaceutical research, vol. 39, no. 7, pp. 1509-1521, 2022.
[12]
J. Persson et al., "Discovery, optimization and biodistribution of an Affibody molecule for imaging of CD69," Scientific Reports, vol. 11, no. 1, 2021.
[13]
S. S. Rinne et al., "HER3 PET Imaging : 68Ga-Labeled Affibody Molecules Provide Superior HER3 Contrast to 89Zr-Labeled Antibody and Antibody-Fragment-Based Tracers," Cancers, vol. 13, no. 19, pp. 4791-4791, 2021.
[14]
M. Oroujeni et al., "The Use of a Non-Conventional Long-Lived Gallium Radioisotope Ga-66 Improves Imaging Contrast of EGFR Expression in Malignant Tumours Using DFO-ZEGFR:2377 Affibody Molecule," Pharmaceutics, vol. 13, no. 2, 2021.
[15]
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.
[16]
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.
[17]
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.
[18]
C. D. Leitao et al., "Evaluating the Therapeutic Efficacy of Mono- and Bivalent Affibody-Based Fusion Proteins Targeting HER3 in a Pancreatic Cancer Xenograft Model," Pharmaceutics, vol. 12, no. 6, 2020.
[19]
R. Güler et al., "Increasing thermal stability and improving biodistribution of VEGFR2-binding affibody molecules by a combination of in silico and directed evolution approaches," Scientific Reports, vol. 10, no. 1, 2020.
[20]
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.
[21]
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.
[22]
B. Mitran et al., "Affibody-mediated imaging of EGFR expression in prostate cancer using radiocobalt-labeled DOTA-Z(EGFR:2377)," Oncology Reports, vol. 41, no. 1, pp. 534-542, 2019.
[23]
K. G. Andersson et al., "Autotransporter-Mediated Display of a Naive Affibody Library on the Outer Membrane of Escherichia coli," Biotechnology Journal, vol. 14, no. 4, 2019.
[24]
S. Deyev et al., "Comparative Evaluation of Two DARPin Variants : Effect of Affinity, Size, and Label on Tumor Targeting Properties," Molecular Pharmaceutics, vol. 16, no. 3, pp. 995-1008, 2019.
[25]
J. Garousi et al., "Comparative evaluation of affibody- and antibody fragments-based CAIX imaging probes in mice bearing renal cell carcinoma xenografts," Scientific Reports, vol. 9, 2019.
[26]
A. Vorobyeva et al., "Comparison of tumor-targeting properties of directly and indirectly radioiodinated designed ankyrin repeat protein (DARPin) G3 variants for molecular imaging of HER2," International Journal of Oncology, vol. 54, no. 4, pp. 1209-1220, 2019.
[27]
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.
[28]
M. Rosestedt et al., "Improved contrast of affibody-mediated imaging of HER3 expression in mouse xenograft model through co-injection of a trivalent affibody for in vivo blocking of hepatic uptake," Scientific Reports, vol. 9, 2019.
[29]
S. S. Rinne et al., "Increase in negative charge of Ga-68/chelator complex reduces unspecific hepatic uptake but does not improve imaging properties of HER3-targeting affibody molecules," Scientific Reports, vol. 9, 2019.
[30]
C. Dahlsson Leitao et al., "Molecular Design of HER3-Targeting Affibody Molecules : Influence of Chelator and Presence of HEHEHE-Tag on Biodistribution of 68 Ga-Labeled Tracers," International Journal of Molecular Sciences, vol. 20, no. 5, 2019.
[31]
A. Vorobyeva et al., "Optimal composition and position of histidine-containing tags improves biodistribution of Tc-99m-labeled DARP in G3," Scientific Reports, vol. 9, 2019.
[32]
S. S. Rinne et al., "Optimization of HER3 expression imaging using affibody molecules : Influence of chelator for labeling with indium-111," Scientific Reports, vol. 9, 2019.
[33]
R. Güler et al., "VEGFR2-Specific Ligands Based on Affibody Molecules Demonstrate Agonistic Effects when Tetrameric in the Soluble Form or Immobilized via Spider Silk," ACS Biomaterials Science & Engineering, vol. 5, no. 12, pp. 6474-6484, 2019.
[34]
D. Summer et al., "Cyclic versus Noncyclic Chelating Scaffold for 89Zr-Labeled ZEGFR:2377 Affibody Bioconjugates Targeting Epidermal Growth Factor Receptor Overexpression," Molecular Pharmaceutics, vol. 15, no. 1, pp. 175-185, 2018.
[35]
A. Orlova et al., "Evaluation of the Therapeutic Potential of a HER3-Binding Affibody Construct TAM-HER3 in Comparison with a Monoclonal Antibody, Seribantumab," Molecular Pharmaceutics, vol. 15, no. 8, pp. 3394-3403, 2018.
[36]
M. Altai et al., "Influence of Molecular Design on the Targeting Properties of ABD-Fused Mono- and Bi-Valent Anti-HER3 Affibody Therapeutic Constructs," Cells, vol. 7, no. 10, 2018.
[37]
M. Oroujeni et al., "Influence of composition of cysteine-containing peptide-based chelators on biodistribution of Tc-99m-labeled anti-EGFR affibody molecules," Amino Acids, vol. 50, no. 8, pp. 981-994, 2018.
[38]
M. Oroujeni et al., "Preclinical Evaluation of [Ga-68]Ga-DFO-ZEGFR:2377 : A Promising Affibody-Based Probe for Noninvasive PET Imaging of EGFR Expression in Tumors," Cells, vol. 7, no. 9, 2018.
[39]
B. Mitran et al., "Radionuclide imaging of VEGFR2 in glioma vasculature using biparatopic affibody conjugate : proof-of-principle in a murine model," Theranostics, vol. 8, no. 16, pp. 4462-4476, 2018.
[40]
S. Ståhl et al., "Affibody Molecules in Biotechnological and Medical Applications," Trends in Biotechnology, vol. 35, no. 8, pp. 691-712, 2017.
[41]
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.
[42]
H. Lindberg et al., "Flow-cytometric screening of aggregation-inhibitors using a fluorescence-assisted intracellular method," Biotechnology Journal, vol. 12, no. 1, 2017.
[43]
E. Wahlberg et al., "Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid-β," Scientific Reports, vol. 7, no. 1, 2017.
[44]
T. Bass et al., "In vivo evaluation of a novel format of a bivalent HER3-targeting and albumin- binding therapeutic affibody construct," Scientific Reports, vol. 7, 2017.
[45]
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.
[46]
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.
[47]
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.
[48]
J. Garousi et al., "The use of radiocobalt as a label improves imaging of EGFR using DOTA-conjugated Affibody molecule," Scientific Reports, vol. 7, 2017.
[49]
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.
[50]
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.
[51]
K. G. Andersson et al., "Feasibility of imaging of epidermal growth factor receptor expression with ZEGFR:2377 affibody molecule labeled with Tc-99m using a peptide-based cysteine-containing chelator," International Journal of Oncology, vol. 49, no. 6, pp. 2285-2293, 2016.
[52]
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.
[53]
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.
[54]
A. Orlova et al., "In vivo evaluation of pharmacokinetics, tumors targeting and therapeutic efficacy of a novel format of HER3-targeting affibody molecule with prolonged blood circulation," European Journal of Nuclear Medicine and Molecular Imaging, vol. 43, pp. S237-S237, 2016.
[55]
M. Åstrand et al., "Investigating affinity-maturation strategies and reproducibility of fluorescence-activated cell sorting using a recombinant ADAPT library displayed on staphylococci," Protein Engineering Design & Selection, vol. 29, no. 5, pp. 187-195, 2016.
[56]
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.
[57]
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.
[58]
M. Malm et al., "Targeting HER3 using mono- and bispecific antibodies or alternative scaffolds," mAbs, vol. 8, no. 7, pp. 1195-1209, 2016.
[59]
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.
[60]
M. Rosestedt et al., "Affibody-mediated PET imaging of HER3 expression in malignant tumours," Scientific Reports, vol. 5, 2015.
[61]
K. G. Andersson et al., "Comparative evaluation of 111In-labeled NOTA‑conjugated affibody molecules for visualization of HER3 expression in malignant tumors," Oncology Reports, vol. 34, no. 2, pp. 1042-8, 2015.
[62]
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.
[63]
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.
[64]
F. Fleetwood et al., "An engineered autotransporter-based surface expression vector enables efficient display of Affibody molecules on OmpT-negative E. coli as well as protease-mediated secretion in OmpT-positive strains," Microbial Cell Factories, vol. 13, pp. 179, 2014.
[65]
J. Nilvebrant et al., "Engineering of Bispecific Affinity Proteins with High Affinity for ERBB2 and Adaptable Binding to Albumin," PLOS ONE, vol. 9, no. 8, pp. e103094, 2014.
[66]
M. Malm et al., "Engineering of a bispecific affibody molecule towards HER2 and HER3 by addition of an albumin-binding domain allows for affinity purification and in vivo half-life extension," Biotechnology Journal, vol. 9, no. 9, pp. 1215-1222, 2014.
[67]
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.
[68]
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.
[69]
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.
[70]
F. Fleetwood et al., "Simultaneous targeting of two ligand-binding sites on VEGFR2 using biparatopic Affibody molecules results in dramatically improved affinity," Scientific Reports, vol. 4, pp. 7518, 2014.
[71]
S. Ståhl et al., "Affinity proteins and their generation," Journal of chemical technology and biotechnology (1986), vol. 88, no. 1, pp. 25-38, 2013.
[72]
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.
[73]
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, pp. e62791, 2013.
[74]
J. Seijsing et al., "Robust Expression of the Human Neonatal Fc Receptor in a Truncated Soluble Form and as a Full-Length Membrane-Bound Protein in Fusion with eGFP," PLOS ONE, vol. 8, no. 11, pp. e81350, 2013.
[75]
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, pp. 139-145, 2013.
[76]
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.
[77]
L. Göstring et al., "Cellular Effects of HER3-Specific Affibody Molecules," PLOS ONE, vol. 7, no. 6, pp. e40023, 2012.
[78]
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.
[79]
B. Hjelm et al., "Parallel Immunizations of Rabbits Using the Same Antigen Yield Antibodies with Similar, but Not Identical, Epitopes," PLOS ONE, vol. 7, no. 12, pp. e45817, 2012.
[80]
J. Löfblom, "Bacterial display in combinatorial protein engineering," Biotechnology Journal, vol. 6, no. 9, pp. 1115-1129, 2011.
[81]
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.
[82]
J. Nilvebrant et al., "Engineering Bispecificity into a Single Albumin-Binding Domain," PLOS ONE, vol. 6, no. 10, pp. e25791, 2011.
[83]
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.
[84]
J. Löfblom et al., "Affibody molecules : Engineered proteins for therapeutic, diagnostic and biotechnological applications," FEBS Letters, vol. 584, no. 12, pp. 2670-2680, 2010.
[85]
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.
[86]
B. Hjelm et al., "Exploring epitopes of antibodies toward the human tryptophanyl-tRNA synthetase," NEW BIOTECHNOL, vol. 27, no. 2, pp. 129-137, 2010.
[87]
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.
[88]
N. Kronqvist et al., "New Ways for Discovery of Biopharmaceuticals : Emerging Techniques using Surface Display on Gram-positive Bacteria for Combinatorial Protein Engineering and Characterization," Bioforum Europe, vol. 13, no. 6-7, pp. 022, 2009.
[89]
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.
[90]
J. Rockberg et al., "Epitope mapping of antibodies using bacterial surface display," Nature Methods, vol. 5, no. 12, pp. 1039-1045, 2008.
[91]
N. Kronqvist et al., "Simplified characterization through site-specific protease-mediated release of affinity proteins selected by staphylococcal display," FEMS Microbiology Letters, vol. 278, no. 1, pp. 128-136, 2008.
[92]
J. Löfblom et al., "Evaluation of staphylococcal cell surface display and flow cytometry for postselectional characterization of affinity proteins in combinatorial protein engineering applications," Applied and Environmental Microbiology, vol. 73, no. 21, pp. 6714-6721, 2007.
[93]
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.
[94]
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
[95]
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
[96]
S. Rinne et al., "HER3-targeted drug delivery : Preclinical characterization of (HE)3-ZHER3-ABD-mcDM1 using Tc-99m," European Journal of Nuclear Medicine and Molecular Imaging, vol. 49, no. SUPPL 1, pp. S654-S655, 2022.
[97]
S. Rinne et al., "HER3 targeting Ga-68-labeled affibody provides superior PET imaging contrast compared with Zr-89-labeled antibody and antibody-fragment based tracers," European Journal of Nuclear Medicine and Molecular Imaging, vol. 48, no. SUPPL 1, pp. S20-S20, 2021.
[98]
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.
[99]
S. Rinne et al., "Optimizing radiocobalt labeled HER3-targeting affibody molecules for next day PET-imaging of HER3 expression," Journal of Nuclear Medicine, vol. 61, 2020.
[100]
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.
[101]
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.
[102]
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.
[103]
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.
[104]
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.
[105]
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.
[106]
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.
[107]
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.
[108]
B. Mitran et al., "In vivo imaging of vascular endothelial growth factor receptor-2 (VEGFR2) expression using biparatopic affibody construct," Journal of labelled compounds & radiopharmaceuticals, vol. 60, pp. S178-S178, 2017.
[109]
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.
[110]
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.
[111]
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.
[112]
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.
[113]
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, pp. 1707-1718, 2015.
[114]
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.
[115]
F. Fleetwood et al., "Development And Optimization Of An e.Coli-based Display Platform For Selection Of Affinity Proteins," Protein Science, vol. 23, pp. 135-135, 2014.
[116]
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.
[117]
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.
[118]
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.
[119]
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.
[120]
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.
[121]
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.
[122]
J. Löfblom, "Bacterial display in directed evolution for generation of new biopharmaceuticals," Biotech International, vol. 23, no. June, pp. 26-29, 2011.
[123]
J. Löfblom et al., "Affibody molecules : engineered proteins for therapeutic, diagnostic and biotechnological applications," The FEBS Journal, vol. 277, pp. 31-31, 2010.
Kapitel i böcker
[124]
C. D. Leitao, S. Ståhl and J. Löfblom, "Bacterial Cell Display for Selection of Affibody Molecules," in Genotype Phenotype Coupling, Stefan Zielonka, Simon Krah Ed., : Springer Nature, 2023, pp. 99-112.
Avhandlingar
[125]
J. Löfblom, "Staphylococcal surface display for protein engineering and characterization," Doctoral thesis Stockholm : KHT, 2007.
Övriga
[126]
L. C. Hjelm, M. Hedhammar and J. Löfblom, "In vitro Blood–Brain Barrier Model based on Recombinant Spider Silk Protein Nanomembranes for Evaluation of Transcytosis capability of biomolecules," (Manuscript).
[127]
L. C. Hjelm et al., "Affibody molecules intended for receptor-mediated transcytosis via the transferrin receptor," (Manuscript).
[128]
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Patent
Patent
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Senaste synkning med DiVA:
2024-04-21 04:38:45