Publications by Magdalena Malm
Peer reviewed
Articles
[1]
H. O. Masson et al., "Deciphering the determinants of recombinant protein expression across the human secretome," Proceedings of the National Academy of Sciences of the United States of America, vol. 122, no. 41, 2025.
[2]
N. Thalén et al., "Mammalian cell display with automated oligo design and library assembly allows for rapid residue level conformational epitope mapping," Communications Biology, vol. 7, no. 1, 2024.
[3]
N. Thalén et al., "Tuning of CHO secretional machinery improve activity of secreted therapeutic sulfatase 150-fold," Metabolic engineering, vol. 81, pp. 157-166, 2024.
[4]
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.
[5]
M. Moradi et al., "Autophagy and intracellular product degradation genes identified by systems biology analysis reduce aggregation of bispecific antibody in CHO cells," New Biotechnology, vol. 68, pp. 68-76, 2022.
[6]
M. Malm et al., "Harnessing secretory pathway differences between HEK293 and CHO to rescue production of difficult to express proteins," Metabolic engineering, vol. 72, pp. 171-187, 2022.
[7]
R. Saghaleyni et al., "Report Enhanced metabolism and negative regulation of ER stress support higher erythropoietin production in HEK293 cells," Cell Reports, vol. 39, no. 11, pp. 110936, 2022.
[8]
M. Malm et al., "Evolution from adherent to suspension : systems biology of HEK293 cell line development," Scientific Reports, vol. 10, no. 1, 2020.
[9]
C. Zhan et al., "Low Shear Stress Increases Recombinant Protein Production and High Shear Stress Increases Apoptosis in Human Cells," iScience, vol. 23, no. 11, 2020.
[10]
H. Schwarz et al., "Small-scale bioreactor supports high density HEK293 cell perfusion culture for the production of recombinant Erythropoietin," Journal of Biotechnology, vol. 309, pp. 44-52, 2020.
[11]
[12]
M. Malm et al., "Targeting HER3 using mono- and bispecific antibodies or alternative scaffolds," mAbs, vol. 8, no. 7, pp. 1195-1209, 2016.
[13]
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.
[14]
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.
[15]
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.
[16]
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.
[17]
L. Göstring et al., "Cellular Effects of HER3-Specific Affibody Molecules," PLOS ONE, vol. 7, no. 6, pp. e40023, 2012.
[18]
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.
[19]
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.
Non-peer reviewed
Articles
[20]
S. Rönning et al., "Automated plasmid purification can reducemanual labour and increase titres in AAV production," Human Gene Therapy, vol. 36, no. 3-4, pp. E179-E180, 2025.
[21]
P. N. Arrías, M. R. Esnal and M. Malm, "Imaging the rAAV manufacturing process : assessing the subcellular localisation of capsids during production," Human Gene Therapy, vol. 36, no. 3-4, pp. E187-E188, 2025.
[22]
H. Thorell et al., "Selective DNA delivery through amodular AAV platform utilising Affibody binding domains," Human Gene Therapy, vol. 36, no. 3-4, pp. E211-E212, 2025.
[23]
M. R. Esnal et al., "Understanding recombinant AAV production kinetics in HEK293 cells," Human Gene Therapy, vol. 36, no. 3-4, pp. E189-E189, 2025.
[24]
M. Malm et al., "Improving targeting and yield of AAV by capsid and cell engineering," Human Gene Therapy, vol. 32, no. 19-20, pp. A119-A120, 2021.
[25]
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.
[26]
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.
[27]
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.
Theses
[28]
M. Malm, "Generation and characterization of Affibody molecules targeting HER3," Doctoral thesis Stockholm : KTH Royal Institute of Technology, TRITA-BIO-Report, 2014:1, 2013.
Other
[29]
H. Thorell et al., "A modular binding domain AAV platform for cell surface receptor-selective DNA delivery," (Manuscript).
[30]
M. Karlander et al., "Amplification and Fragmentation Free Long-read Sequencing Enables Rapid Analysis of Packaged Adeno-associated Virus ssDNA," (Manuscript).
[31]
[32]
M. Malm et al., "Harnessing secretory pathway differences between HEK293 and CHO to rescue production of difficult to express proteins," (Manuscript).
[33]
C. Zhan et al., "Hydrodynamic shear stress in hollow filter for perfusion culture of human cells," (Manuscript).
[34]
H. Schwarz et al., "Small-scale bioreactor supports high density HEK293 cell perfusion culture for the production of recombinant Erythropoietin," (Manuscript).
[35]
M. Karlander et al., "Survival of the less fit - directed evolution via deep sequencing enables selection of diverse high affinity proteins," (Manuscript).
[36]
N. Thalén et al., "Systems biology greatly improve activity of secreted therapeutic sulfatase in CHO bioprocess," (Manuscript).
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2025-11-23 00:42:31 UTC