Publikationer av Magdalena Malm
Refereegranskade
Artiklar
[1]
N. Thalén et al., "Tuning of CHO secretional machinery improve activity of secreted therapeutic sulfatase 150-fold," Metabolic engineering, vol. 81, s. 157-166, 2024.
[2]
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.
[3]
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, s. 68-76, 2022.
[4]
M. Malm et al., "Harnessing secretory pathway differences between HEK293 and CHO to rescue production of difficult to express proteins," Metabolic engineering, vol. 72, s. 171-187, 2022.
[5]
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, s. 110936, 2022.
[6]
M. Malm et al., "Evolution from adherent to suspension : systems biology of HEK293 cell line development," Scientific Reports, vol. 10, no. 1, 2020.
[7]
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.
[8]
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, s. 44-52, 2020.
[9]
[10]
M. Malm et al., "Targeting HER3 using mono- and bispecific antibodies or alternative scaffolds," mAbs, vol. 8, no. 7, s. 1195-1209, 2016.
[11]
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, s. 1042-8, 2015.
[12]
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, s. 1215-1222, 2014.
[13]
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, s. 1450-1459, 2014.
[14]
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.
[15]
L. Göstring et al., "Cellular Effects of HER3-Specific Affibody Molecules," PLOS ONE, vol. 7, no. 6, s. e40023, 2012.
[16]
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, s. 385-396, 2011.
[17]
N. Kronqvist et al., "Staphylococcal surface display in combinatorial protein engineering and epitope mapping of antibodies," Recent Patents on Biotechnology, vol. 4, no. 3, s. 171-182, 2010.
Icke refereegranskade
Artiklar
[18]
M. Malm et al., "Improving targeting and yield of AAV by capsid and cell engineering," Human Gene Therapy, vol. 32, no. 19-20, s. A119-A120, 2021.
[19]
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, s. S311-S311, 2014.
[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]
M. Malm, "Generation and characterization of Affibody molecules targeting HER3," Doktorsavhandling Stockholm : KTH Royal Institute of Technology, TRITA-BIO-Report, 2014:1, 2013.
Övriga
[23]
[24]
M. Malm et al., "Harnessing secretory pathway differences between HEK293 and CHO to rescue production of difficult to express proteins," (Manuskript).
[25]
C. Zhan et al., "Hydrodynamic shear stress in hollow filter for perfusion culture of human cells," (Manuskript).
[26]
H. Schwarz et al., "Small-scale bioreactor supports high density HEK293 cell perfusion culture for the production of recombinant Erythropoietin," (Manuskript).
[27]
N. Thalén et al., "Systems biology greatly improve activity of secreted therapeutic sulfatase in CHO bioprocess," (Manuskript).
Senaste synkning med DiVA:
2024-04-28 01:43:41