Hoppa till huvudinnehållet
Till KTH:s startsida

Publikationer av Sophia Hober

Refereegranskade

Artiklar

[1]
M. Jönsson et al., "Cooperative folding as a molecular switch in an evolved antibody binder," Journal of Biological Chemistry, vol. 300, no. 11, 2024.
[4]
M. Dannemeyer et al., "Fast and robust recombinant protein production utilizing episomal stable pools in WAVE bioreactors," Protein Expression and Purification, vol. 221, 2024.
[5]
U. Marking et al., "Humoral immune responses to the monovalent xbb.1.5-adapted bnt162b2 mrna booster in sweden," The Lancet - Infectious diseases, vol. 24, no. 2, s. e80-e81, 2024.
[6]
A. Jernbom Falk et al., "Prevalent and persistent new-onset autoantibodies in mild to severe COVID-19," Nature Communications, vol. 15, no. 1, 2024.
[7]
A. Wisniewski et al., "Targeted HER2-positive cancer therapy using ADAPT6 fused to horseradish peroxidase," New Biotechnology, vol. 83, s. 74-81, 2024.
[8]
U. Marking et al., "7-month duration of SARS-CoV-2 mucosal immunoglobulin-A responses and protection," The Lancet - Infectious diseases, vol. 23, no. 2, s. 150-152, 2023.
[10]
J. Scheffel et al., "Calcium-dependent affinity ligands for the purification of antibody fragments at neutral pH," Journal of Chromatography A, vol. 1694, s. 463902, 2023.
[11]
M. Wolf-Watz et al., "Calcium-dependent protein folding in a designed molecular switch," Biophysical Journal, vol. 122, no. 3S1, 2023.
[14]
O. Bladh et al., "Mucosal immune responses following a fourth SARS-CoV-2 vaccine dose," The Lancet Microbe, vol. 4, no. 7, s. 488, 2023.
[16]
S. Mravinacová et al., "A cell-free high throughput assay for assessment of SARS-CoV-2 neutralizing antibodies," New Biotechnology, vol. 66, s. 46-52, 2022.
[17]
[18]
S. Havervall et al., "Anti-Spike Mucosal IgA Protection against SARS-CoV-2 Omicron Infection," New England Journal of Medicine, vol. 387, no. 14, s. 1333-1336, 2022.
[19]
K. Asplund Högelin et al., "B-cell repopulation dynamics and drug pharmacokinetics impact SARS-CoV-2 vaccine efficacy in anti-CD20-treated multiple sclerosis patients," European Journal of Neurology, vol. 29, no. 11, s. 3317-3328, 2022.
[20]
[28]
S. Havervall et al., "Impact of SARS-CoV-2 infection on vaccine-induced immune responses over time," Clinical & Translational Immunology (CTI), vol. 11, no. 4, 2022.
[32]
[34]
E. von Witting, S. Hober och S. Kanje, "Affinity-Based Methods for Site-Specific Conjugation of Antibodies," Bioconjugate chemistry, vol. 32, s. 1515-1524, 2021.
[36]
J. Dillner et al., "Antibodies to SARS-CoV-2 and risk of past or future sick leave," Scientific Reports, vol. 11, no. 1, 2021.
[39]
K. M. Elfstrom et al., "Differences in risk for SARS-CoV-2 infection among healthcare workers," Preventive Medicine Reports, vol. 24, 2021.
[41]
J. Dillner et al., "High Amounts of SARS-CoV-2 Precede Sickness Among Asymptomatic Health Care Workers," The Journal of Infectious Diseases, vol. 224, no. 1, s. 14-20, 2021.
[42]
J. Scheffel och S. Hober, "Highly selective Protein A resin allows for mild sodium chloride-mediated elution of antibodies," Journal of Chromatography A, vol. 1637, 2021.
[43]
H. Alkharaan et al., "Persisting Salivary IgG Against SARS-CoV-2 at 9 Months After Mild COVID-19 : A Complementary Approach to Population Surveys," Journal of Infectious Diseases, vol. 224, no. 3, s. 407-414, 2021.
[44]
[46]
S. Klevebro et al., "Risk of SARS-CoV-2 exposure among hospital healthcare workers in relation to patient contact and type of care," Scandinavian Journal of Public Health, vol. 49, no. 7, s. 707-712, 2021.
[47]
S. Hassan et al., "SARS-CoV-2 infections amongst personnel providing home care services for older persons in Stockholm, Sweden," Journal of Internal Medicine, vol. 290, no. 2, s. 430-436, 2021.
[50]
E. von Witting et al., "Small Bispecific Affinity Proteins for Simultaneous Target Binding and Albumin-Associated Half-Life Extension," Molecular Pharmaceutics, vol. 18, no. 1, s. 328-337, 2021.
[51]
S. Havervall et al., "Symptoms and Functional Impairment Assessed 8 Months After Mild COVID-19 Among Health Care Workers," Journal of the American Medical Association (JAMA), vol. 325, s. 2015, 2021.
[52]
[55]
H. Tegel et al., "High throughput generation of a resource of the human secretome in mammalian cells," New Biotechnology, vol. 58, s. 45-54, 2020.
[56]
S. Kanje et al., "Improvements of a high-throughput protein purification process using a calcium-dependent setup," Protein Expression and Purification, vol. 175, 2020.
[58]
A.-S. Rudberg et al., "SARS-CoV-2 exposure, symptoms and seroprevalence in healthcare workers in Sweden.," Nature Communications, vol. 11, no. 1, 2020.
[59]
M. Ding et al., "Secretome-Based Screening in Target Discovery," SLAS Discovery, vol. 25, no. 6, s. 535-551, 2020.
[60]
S. Hober, S. Lindbo och J. Nilvebrant, "Bispecific applications of non-immunoglobulin scaffold binders," Methods, vol. 154, s. 143-152, 2019.
[61]
J. Garousi et al., "Comparative evaluation of dimeric and monomeric forms of ADAPT scaffold protein for targeting of HER2-expressing tumours," European journal of pharmaceutics and biopharmaceutics, vol. 134, s. 37-48, 2019.
[63]
K. Jennbacken et al., "Phenotypic Screen with the Human Secretome Identifies FGF16 as Inducing Proliferation of iPSC-Derived Cardiac Progenitor Cells," International Journal of Molecular Sciences, vol. 20, no. 23, 2019.
[65]
[66]
M. Uhlén et al., "The human secretome," Science Signaling, vol. 12, no. 609, 2019.
[67]
F. Edfors et al., "Enhanced validation of antibodies for research applications," Nature Communications, vol. 9, 2018.
[68]
S. Lindbo et al., "Optimized molecular design of ADAPT-based HER2-imaging probes labelled with 111In and 68Ga," Molecular Pharmaceutics, vol. 15, no. 7, s. 2674-2683, 2018.
[69]
S. Kanje et al., "Protein engineering allows for mild affinity-based elution of therapeutic antibodies," Journal of Molecular Biology, vol. 430, no. 18, s. 3427-3438, 2018.
[72]
M. Uhlén et al., "A pathology atlas of the human cancer transcriptome," Science, vol. 357, no. 6352, s. 660-+, 2017.
[73]
P. J. Thul et al., "A subcellular map of the human proteome," Science, vol. 356, no. 6340, 2017.
[75]
T. Boström, J. Ottosson Takanen och S. Hober, "Antibodies as means for selective mass spectrometry," Journal of chromatography. B, vol. 1021, s. 3-13, 2016.
[76]
S. Lindbo et al., "Influence of Histidine-Containing Tags on the Biodistribution of ADAPT Scaffold Proteins.," Bioconjugate chemistry, vol. 27, no. 3, s. 716-726, 2016.
[77]
[78]
J. Garousi et al., "Influence of the N-terminal amino acid sequence on imaging properties of In-111-labeled anti-HER2 scaffold protein ADAPT6," European Journal of Nuclear Medicine and Molecular Imaging, vol. 43, s. S55-S55, 2016.
[83]
X. Wang et al., "Association of chromosome 19 to lung cancer genotypes and phenotypes," Cancer Metastasis Review, vol. 34, no. 2, s. 217-226, 2015.
[84]
X. Wang et al., "Association of chromosome 19 to lung cancer genotypes and phenotypes (vol 34, pg 217, 2015)," Cancer Metastasis Review, vol. 34, no. 2, s. 227-227, 2015.
[86]
M. Uhlén et al., "Tissue-based map of the human proteome," Science, vol. 347, no. 6220, s. 1260419, 2015.
[87]
C. L. Nilsson et al., "Use of ENCODE Resources to Characterize Novel Proteoforms and Missing Proteins in the Human Proteome," Journal of Proteome Research, vol. 14, no. 2, s. 603-608, 2015.
[88]
J. Nilvebrant, M. Åstrand och S. Hober, "An orthogonal fusion tag for efficient protein purification," Methods in Molecular Biology, vol. 1129, s. 205-210, 2014.
[89]
C. Älgenäs et al., "Antibody performance in western blot applications is context- dependent," Biotechnology Journal, vol. 9, no. 3, s. 435-445, 2014.
[90]
J. Garousi et al., "Development of ADAPT6 as a new scaffold protein for radionuclide molecular imaging," European Journal of Nuclear Medicine and Molecular Imaging, vol. 41, s. S309-S309, 2014.
[92]
F. Edfors et al., "Immunoproteomics using polyclonal antibodies and stable isotope-labeled affinity-purified recombinant proteins," Molecular & Cellular Proteomics, vol. 13, no. 6, s. 1611-1624, 2014.
[93]
C. F. Lichti et al., "Integrated Chromosome 19 Transcriptomic and Proteomic Data Sets Derived from Glioma Cancer Stem-Cell Lines," Journal of Proteome Research, vol. 13, no. 1, s. 191-199, 2014.
[95]
M. Hedhammar, J. Nilvebrant och S. Hober, "Zbasic: a purification tag for selective ion-exchange recovery," Methods in Molecular Biology, vol. 1129, s. 197-204, 2014.
[96]
S. Andersson et al., "Antibodies Biotinylated Using a Synthetic Z-domain from Protein A Provide Stringent In Situ Protein Detection," Journal of Histochemistry and Cytochemistry, vol. 61, no. 11, s. 773-784, 2013.
[97]
C. L. Nilsson et al., "Chromosome 19 Annotations with Disease Speciation : A First Report from the Global Research Consortium," Journal of Proteome Research, vol. 12, no. 1, s. 134-149, 2013.
[98]
L. Fagerberg et al., "Contribution of antibody-based protein profiling to the human chromosome-centric proteome project (C-HPP)," Journal of Proteome Research, vol. 12, no. 6, s. 2439-2448, 2013.
[99]
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, s. 3973-3985, 2013.
[100]
J. Malm et al., "Developments in biobanking workflow standardization providing sample integrity and stability," Journal of Proteomics, vol. 95, no. SI, s. 38-45, 2013.
[101]
J. Nilvebrant och S. Hober, "The albumin-binding domain as a scaffold for protein engineering," Computational and Structural Biotechnology Journal, vol. 6, no. 7, s. a5, 2013.
[102]
B. Adler et al., "Miniaturized and Automated High-Throughput Verification of Proteins in the ISET Platform with MALDI MS," Analytical Chemistry, vol. 84, no. 20, s. 8663-8669, 2012.
[103]
J. Nilvebrant, T. Alm och S. Hober, "Orthogonal protein purification facilitated by a small bispecific affinity tag," Journal of Visualized Experiments, no. 59, s. 1-5, 2012.
[104]
K. Colwill et al., "A roadmap to generate renewable protein binders to the human proteome," Nature Methods, vol. 8, no. 7, s. 551-8, 2011.
[105]
A. Konrad, A. Eriksson Karlström och S. Hober, "Covalent Immunoglobulin Labeling through a Photoactivable Synthetic Z Domain," Bioconjugate chemistry, vol. 22, no. 12, s. 2395-2403, 2011.
[106]
J. Nilvebrant et al., "Engineering Bispecificity into a Single Albumin-Binding Domain," PLOS ONE, vol. 6, no. 10, s. e25791, 2011.
[107]
H. Tegel, J. Ottosson och S. Hober, "Enhancing the protein production levels in Escherichia coli with a strong promoter," The FEBS Journal, vol. 278, no. 5, s. 729-739, 2011.
[108]
B. Hjelm et al., "High nuclear RBM3 expression is associated with an improved prognosis in colorectal cancer," Proteomics. Clinical applications, vol. 5, no. 11-12, s. 624-35, 2011.
[109]
K. Larsson et al., "Novel antigen design for the generation of antibodies to G-protein-coupled receptors," JIM - Journal of Immunological Methods, vol. 370, no. 1-2, s. 14-23, 2011.
[110]
H. Tegel et al., "Parallel production and verification of protein products using a novel high-throughput screening method," Biotechnology Journal, vol. 6, no. 8, s. 1018-1025, 2011.
[111]
E. Gustavsson et al., "Surrogate antigens as targets for proteome-wide binder selection," New Biotechnology, vol. 28, no. 4, s. 302-311, 2011.
[112]
R. Falk et al., "Targeted protein pullout from human tissue samples using competitive elution," Biotechnology Journal, vol. 6, no. 1, s. 28-37, 2011.
[114]
T. Alm et al., "A small bispecific protein selected for orthogonal affinity purification," BIOTECHNOL J, vol. 5, no. 6, s. 605-617, 2010.
[116]
L. Paavilainen et al., "The Impact of Tissue Fixatives on Morphology and Antibody-based Protein Profiling in Tissues and Cells," Journal of Histochemistry and Cytochemistry, vol. 58, no. 3, s. 237-246, 2010.
[117]
M. Uhlén et al., "Towards a knowledge-based Human Protein Atlas," Nature Biotechnology, vol. 28, no. 12, s. 1248-1250, 2010.
[118]
F. Ponten et al., "A global view of protein expression in human cells, tissues, and organs," Molecular Systems Biology, vol. 5, 2009.
[119]
J. Steen et al., "Automated sample preparation method for mass spectrometry analysis on recombinant proteins," Journal of Chromatography A, vol. 1216, no. 20, s. 4457-4464, 2009.
[120]
K. Larsson et al., "Characterization of PrEST-based antibodies towards human Cytokeratin-17," JIM - Journal of Immunological Methods, vol. 342, s. 20-32, 2009.
[121]
M. Ramström et al., "Development of affinity columns for the removal of high-abundance proteins in cerebrospinal fluid," Biotechnology and applied biochemistry, vol. 52, no. 2, s. 159-166, 2009.
[122]
M. Uhlén och S. Hober, "Generation and validation of affinity reagents on a proteome-wide level," Journal of Molecular Recognition, vol. 22, no. 2, s. 57-64, 2009.
[123]
[124]
J. Mulder et al., "Tissue Profiling of the Mammalian Central Nervous System Using Human Antibody-based Proteomics," Molecular & Cellular Proteomics, vol. 8, no. 7, s. 1612-1622, 2009.
[125]
L. Berglund et al., "A genecentric human protein atlas for expression profiles based on antibodies," Molecular & Cellular Proteomics, vol. 7, no. 10, s. 2019-2027, 2008.
[126]
E. Björling et al., "A web-based tool for in silico biomarker discovery based on tissue-specific protein profiles in normal and cancer tissues," Molecular & Cellular Proteomics, vol. 7, no. 5, s. 825-844, 2008.
[127]
L. Paavilainen et al., "Evaluation of monospecific antibodies : A comparison study with commercial analogs using immunohistochemistry on tissue microarrays," Applied immunohistochemistry & molecular morphology (Print), vol. 16, no. 5, s. 493-502, 2008.
[128]
S. Hober och M. Uhlén, "Human protein atlas and the use of microarray technologies," Current Opinion in Biotechnology, vol. 19, no. 1, s. 30-35, 2008.
[130]
C. Grönwall et al., "Affibody-mediated transferrin depletion for proteomics applications," Biotechnology Journal, vol. 2, no. 11, s. 1389-1398, 2007.
[131]
R. Falk et al., "Approaches for systematic proteome exploration," Biomolecular Engineering, vol. 24, no. 2, s. 155-168, 2007.
[133]
S. Hober, K. Nord och M. Linhult, "Protein A chromatography for antibody purification," Journal of chromatography. B, vol. 848, no. 1, s. 40-47, 2007.
[135]
M. Lerner et al., "The RBCC gene RFP2 (leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD," Molecular Biology of the Cell, vol. 18, no. 5, s. 1670-1682, 2007.
[136]
M. Hedhammar och S. Hober, "Z(basic) - A novel purification tag for efficient protein recovery," Journal of Chromatography A, vol. 1161, no. 1-2, s. 22-28, 2007.
[137]
A. Persson, S. Hober och M. Uhlén, "A human protein atlas based on antibody proteomics," Current opinion in molecular therapeutics (Print), vol. 8, no. 3, s. 185-190, 2006.
[138]
M. Hedhammar, H. R. Jung och S. Hober, "Enzymatic cleavage of fusion proteins using immobilised protease 3C," Protein Expression and Purification, vol. 47, no. 2, s. 422-426, 2006.
[140]
J. Steen et al., "High-throughput protein purification using an automated set-up for high-yield affinity chromatography," Protein Expression and Purification, vol. 46, no. 2, s. 173-178, 2006.
[141]
C. Eriksson et al., "Microfluidic analysis of antibody specificity in a compact disk format," Journal of Proteome Research, vol. 5, no. 7, s. 1568-1574, 2006.
[142]
K. Larsson et al., "Multiplexed PrEST immunization for high-throughput affinity proteomics," JIM - Journal of Immunological Methods, vol. 315, s. 110-120, 2006.
[143]
A. Ahmadian, M. Ehn och S. Hober, "Pyrosequencing : History, biochemistry and future," Clinica Chimica Acta, vol. 363, no. 02-jan, s. 83-94, 2006.
[146]
M. Uhlén et al., "A human protein atlas for normal and cancer tissues based on antibody proteomics," Molecular & Cellular Proteomics, vol. 4, no. 12, s. 1920-1932, 2005.
[147]
M. Linhult, S. Gulich och S. Hober, "Affinity ligands for industrial protein purification," Protein peptide letters, vol. 12, no. 4, s. 305-310, 2005.
[148]
M. Boström et al., "Effect of substrate feed rate on recombinant protein secretion, degradation and invlusion body formation in Escherichia coli," Applied Microbiology and Biotechnology, vol. 68, no. 1, s. 82-90, 2005.
[149]
M. Stenvall et al., "High-throughput solubility assay for purified recombinant protein immunogens," Biochimica et Biophysica Acta - Proteins and Proteomics, vol. 1752, no. 1, s. 6-10, 2005.
[150]
M. Hedhammar, T. Gräslund och S. Hober, "Protein engineering strategies for selective protein purification," Chemical Engineering & Technology, vol. 28, no. 11, s. 1315-1325, 2005.
[152]
C. Agaton, M. Uhlén och S. Hober, "Genome-based proteomics," Electrophoresis, vol. 25, no. 9, s. 1280-1288, 2004.
[153]
M. Linhult et al., "Improving the tolerance of a protein a analogue to repeated alkaline exposures using a bypass mutagenesis approach," Proteins : Structure, Function, and Bioinformatics, vol. 55, no. 2, s. 407-416, 2004.
[154]
M. Hedhammar et al., "Negatively charged purification tags for selective anion-exchange recovery," Protein Engineering Design & Selection, vol. 17, no. 11, s. 779-786, 2004.
[155]
C. Agaton et al., "Selective enrichment of monospecific polyclonal antibodies for antibody-based proteomics efforts," Journal of Chromatography A, vol. 1043, s. 33-40, 2004.
[156]
[157]
R. Falk et al., "An improved dual-expression concept, generating high-quality antibodies for proteomics research," Biotechnology and applied biochemistry, vol. 38, s. 231-239, 2003.
[159]
[160]
S. Gulich et al., "Engineering streptococcal protein G for increased alkaline stability," Protein Engineering, vol. 15, no. 10, s. 835-842, 2002.
[165]
T. Gräslund et al., "Strategy for highly selective ion-exchange capture using a charge-polarizing fusion partner," Journal of Chromatography A, vol. 942, no. 1-2, s. 157-166, 2002.
[166]
M. U. Johansson et al., "Structure, specificity, and mode of interaction for bacterial albumin-binding modules," Journal of Biological Chemistry, vol. 277, no. 10, s. 8114-8120, 2002.
[167]
M. Ehn et al., "Overexpression, rapid isolation, and biochemical characterization of Escherichia coli single-stranded DNA-binding protein," Protein Expression and Purification, vol. 22, no. 1, s. 120-127, 2001.
[168]
T. Gräslund et al., "Charge engineering of a protein domain to allow efficient ion-exchange recovery," Protein Engineering, vol. 13, no. 10, s. 703-709, 2000.
[169]
S. Gulich, M. Uhlén och S. Hober, "Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatography," Journal of Biotechnology, vol. 76, no. 03-feb, s. 233-244, 2000.
[170]
S. Gulich et al., "Stability towards alkaline conditions can be engineered into a protein ligand," Journal of Biotechnology, vol. 80, no. 2, s. 169-178, 2000.
[172]
K. Andersson et al., "Kinetic characterization of the interaction of the Z-fragment of protein A with mouse-IgG3 in a volume in chemical space.," Proteins : Structure, Function, and Bioinformatics, vol. 37, no. 3, 1999.
[174]
S. Hober et al., "Disulfide exchange folding of insulin-like growth factor I.," Biochemistry, vol. 31, no. 6, 1992.

Kapitel i böcker

[176]
J. Nilvebrant, M. Åstrand och S. Hober, "An orthogonal fusion tag for efficient protein purification," i Methods in Molecular Biology, NaN. uppl. : Springer Nature, 2021, s. 159-166.
[177]
J. Scheffel, S. Kanje och S. Hober, "ZCa : A protein A-derived domain with calcium-dependent affinity for mild antibody purification," i Methods in Molecular Biology, NaN. uppl. : Humana Press Inc., 2021, s. 245-249.
[178]
M. Hedhammar, J. Nilvebrant och S. Hober, "Zbasic : A Purification Tag for Selective Ion-Exchange Recovery," i Protein Downstream Processing : Design, Development, and Application of High and Low-Resolution Methods, : Humana Press, 2021, s. 149-158.
[179]
T. Boström, J. Nilvebrant och S. Hober, "Purification systems based of bacterial surface proteins," i Protein Purification, Rizwan Ahmad red., : InTech, 2012, s. 89-136.

Icke refereegranskade

Artiklar

[180]
M. Jönsson et al., "The multifaceted usefulness of calcium-regulated affinity molecules," Journal of Peptide Science, vol. 30, 2024.
[181]
K. A. Hogelin et al., "Impact of B-cell depleting treatments on development of humoral and cellular immunological memory against SARS-CoV-2," Multiple Sclerosis Journal, vol. 27, no. 2_SUPPL, s. 348-348, 2021.
[182]
O. Bragina et al., "Phase I study of 99mTc-ADAPT6, a scaffold protein-based probe for visualization of HER2 expression in breast cancer," European Journal of Nuclear Medicine and Molecular Imaging, vol. 47, no. SUPPL 1, s. S9-S9, 2020.
[183]
J. Garousi et al., "Radionuclide Therapy Using Lu-177-labeled ABD-fused ADAPT6 Scaffold Protein," European Journal of Nuclear Medicine and Molecular Imaging, vol. 47, no. SUPPL 1, s. S649-S650, 2020.
[184]
V. Tolmachev et al., "First-in-humans Evaluation of [Tc-99m]-ADAPT6, a Novel Scaffold Protein for Visualizationof HER2 Expression," European Journal of Nuclear Medicine and Molecular Imaging, vol. 46, no. SUPPL 1, s. S166-S166, 2019.
[185]
J. Garousi et al., "Selection Of The Optimal Macrocyclic Chelators For Labelling With In-111 And Ga-68 Improves Contrast Of Her2 Imaging Using Engineered Scaffold Protein Adapt6," European Journal of Nuclear Medicine and Molecular Imaging, vol. 46, no. SUPPL 1, s. S131-S131, 2019.
[186]
[187]
J. Garousi et al., "Selection of the most optimal ADAPT6-based probe for imaging of HER2 using PET and SPECT," European Journal of Nuclear Medicine and Molecular Imaging, vol. 45, s. S77-S78, 2018.
[188]
J. Garousi et al., "Radionuclide tumor targeting using ADAPT scaffold proteins : aspects of label positioning and residualizing properties of the label," European Journal of Nuclear Medicine and Molecular Imaging, vol. 44, s. S228-S229, 2017.
[189]
S. Hober, "Biotech reviews on plants, lignocellulose, sequencing, genome engineering and Aspergilli," Biotechnology Journal, vol. 7, no. 9, s. 1057-1057, 2012.
[190]
S. Hober, "Biotech reviews : keeping up with current developments," Biotechnology Journal, vol. 6, 2011.
[191]
S. Hober, "Global biotech challenges," Biotechnology Journal, vol. 5, 2010.
[192]
S. Hober, "Progress in production and purification of proteins," The FEBS Journal, vol. 277, s. 15-15, 2010.
[193]
S. Hober, "Biotech in the post genomic era," Biotechnology Journal, vol. 4, s. 1631, 2009.
[194]
H. Tegel et al., "Flow cytometry-based analysis of promoter effects on solubility of recombinantly expressed proteins," Journal of Biotechnology, vol. 131, no. 2, s. S9-S9, 2007.
[195]
J. Ottosson et al., "High throughput protein production and purification in the Human Protein Atlas program," Molecular & Cellular Proteomics, vol. 5, no. 10, s. S40-S40, 2006.
[196]
C. Eriksson et al., "Microfluidic analysis of antibodies in a compact disc format," Molecular & Cellular Proteomics, vol. 4, no. 8, s. S47-S47, 2005.
[197]
H. Tegel et al., "Novel flow cytometry-based method for analysis of protein production in Escherichia coli," Molecular & Cellular Proteomics, vol. 4, no. 8, s. S66-S66, 2005.
[198]
J. Ottosson et al., "High throughput protein expression and purification for antibody proteomics," Molecular & Cellular Proteomics, vol. 3, no. 10, s. S169-S169, 2004.
[199]
R. Falk et al., "Selective enrichment of monospecific polyclonal antibodies for antibody-based proteomics efforts - Abstracts," Molecular & Cellular Proteomics, vol. 3, no. 10, s. S1-S1, 2004.

Kapitel i böcker

[200]
S. Kanje et al., "Engineering of Protein A for improved purification of antibodies and Fc-fused proteins," i Approaches to the Purification, Analysis and Characterization of Antibody-Based Therapeutics, : Elsevier, 2020, s. 35-54.

Övriga

[227]
J. Steen, S. Hober och J. Ottosson, "The correlation between antigen solubility and immunogenicity," (Manuskript).

Patent

Patent

[229]
J. Nilvebrant, S. Hober och S. Kanje, "Ligand and use thereof," us 11820802 (2023-11-21), 2023.
[230]
C. Ekblad et al., "Polypeptides based on a scaffold," us 11505576 (2022-11-22), 2022.
[231]
S. Hober och H. j. Johansson, "Mutant protein," us US9296791B2 (2016-03-29), 2016.
[232]
S. Hober, "Mutated immunoglobulin-binding protein," us US9156892B2 (2015-10-13), 2015.
[233]
S. Hober, A. Eriksson Karlström och A. Konrad, "Method for labeling of compounds," us 8916689B2 (2014-12-23), 2010.
[234]
S. Hober, H. J. Johansson och T. Bjorkman, "Protein ligands," us 7709209 (2010-05-04), 2002.
[235]
M. Uhlén och S. Hober, "Method of affinity separation and ligands for use therein," us 6831161B1 (2004-12-14), 1998.
[236]
M. Uhlen och S. Hober, "Method of affinity separation and ligands for use therein," au 773368-B2 (2004-05-20), 1998.
[237]
S. Hober och B. Nilsson, "Use of IGF-BP for refolding of IGF," us 5683980A (1997-11-04), 1996.
Senaste synkning med DiVA:
2024-11-24 00:15:00