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Boutajangout, A., Lindberg, H., Awwad, A., Paul, A., Baitalmal, R., Almokyad, I., . . . Wisniewski, T. (2019). Affibody-Mediated Sequestration of Amyloid beta Demonstrates Preventive Efficacy in a Transgenic Alzheimer's Disease Mouse Model. Frontiers in Aging Neuroscience, 11, Article ID 64.
Öppna denna publikation i ny flik eller fönster >>Affibody-Mediated Sequestration of Amyloid beta Demonstrates Preventive Efficacy in a Transgenic Alzheimer's Disease Mouse Model
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2019 (Engelska)Ingår i: Frontiers in Aging Neuroscience, ISSN 1663-4365, E-ISSN 1663-4365, Vol. 11, artikel-id 64Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Different strategies for treatment and prevention of Alzheimer's disease (AD) are currently under investigation, including passive immunization with anti-amyloid beta (anti-A beta) monoclonal antibodies (mAbs). Here, we investigate the therapeutic potential of a novel type of A beta-targeting agent based on an affibody molecule with fundamentally different properties to mAbs. We generated a therapeutic candidate, denoted Z(SYM73)-albumin-binding domain (ABD; 16.8 kDa), by genetic linkage of the dimeric Z(SYM73) affibody for sequestering of monomeric A beta-peptides and an ABD for extension of its in vivo half-life. Amyloid precursor protein (APP)/PS1 transgenic AD mice were administered with Z(SYM73)-ABD, followed by behavioral examination and immunohistochemistry. Results demonstrated rescued cognitive functions and significantly lower amyloid burden in the treated animals compared to controls. No toxicological symptoms or immunology-related side-effects were observed. To our knowledge, this is the first reported in vivo investigation of a systemically delivered scaffold protein against monomeric A beta, demonstrating a therapeutic potential for prevention of AD.

Ort, förlag, år, upplaga, sidor
Frontiers Media S.A., 2019
Nyckelord
Alzheimer's disease, affibody molecule, amyloid beta (A beta), behavior, histology, immunotherapy, transgenic mice
Nationell ämneskategori
Geriatrik
Identifikatorer
urn:nbn:se:kth:diva-249880 (URN)10.3389/fnagi.2019.00064 (DOI)000462530400001 ()30967771 (PubMedID)
Anmärkning

QC 20190423

Tillgänglig från: 2019-04-23 Skapad: 2019-04-23 Senast uppdaterad: 2019-04-23Bibliografiskt granskad
Andersson, K. G., Persson, J., Ståhl, S. & Löfblom, J. (2019). Autotransporter-Mediated Display of a Naive Affibody Library on the Outer Membrane of Escherichia coli. Biotechnology Journal, 14(4), Article ID 1800359.
Öppna denna publikation i ny flik eller fönster >>Autotransporter-Mediated Display of a Naive Affibody Library on the Outer Membrane of Escherichia coli
2019 (Engelska)Ingår i: Biotechnology Journal, ISSN 1860-6768, E-ISSN 1860-7314, Vol. 14, nr 4, artikel-id 1800359Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Development of new affinity proteins using combinatorial protein engineering is today established for generation of monoclonal antibodies and also essential for discovery of binders that are based on non-immunoglobulin proteins. Phage display is most frequently used, but yeast display is becoming increasingly popular, partly due to the option of utilizing fluorescence-activated cell sorting (FACS) for isolation of new candidates. Escherichia coli has several valuable properties for library applications and in particular the high transformation efficiency. The use of various autotransporters and intimins for secretion and anchoring on the outer membrane have shown promising results and particularly for directed evolution of different enzymes. Here, the authors report on display of a large naive affibody library on the outer membrane of E. coli using the autotransporter Adhesin Involved in Diffuse Adherence (AIDA-I). The expression cassette is first engineered by removing non-essential sequences, followed by introduction of an affibody library, comprising more than 10(9) variants, into the new display vector. The quality of the library and general performance of the method is assessed by FACS against five different targets, which resulted in a panel of binders with down to nanomolar affinities, suggesting that the method has potential as a complement to phage display for generation of affibody molecules.

Ort, förlag, år, upplaga, sidor
WILEY-V C H VERLAG GMBH, 2019
Nyckelord
affibody library, AIDA-I, autodisplay, bacterial display, directed evolution
Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
urn:nbn:se:kth:diva-249806 (URN)10.1002/biot.201800359 (DOI)000462917100020 ()30179307 (PubMedID)2-s2.0-85053871994 (Scopus ID)
Anmärkning

QC 20190423

Tillgänglig från: 2019-04-23 Skapad: 2019-04-23 Senast uppdaterad: 2019-04-23Bibliografiskt granskad
Garousi, J., Huizing, F. J., Vorobyeva, A., Mitran, B., Andersson, K. G., Leitao, C. D., . . . Tolmachev, V. (2019). Comparative evaluation of affibody- and antibody fragments-based CAIX imaging probes in mice bearing renal cell carcinoma xenografts. Scientific Reports, 9, Article ID 14907.
Öppna denna publikation i ny flik eller fönster >>Comparative evaluation of affibody- and antibody fragments-based CAIX imaging probes in mice bearing renal cell carcinoma xenografts
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2019 (Engelska)Ingår i: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, artikel-id 14907Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Carbonic anhydrase IX (CAIX) is a cancer-associated molecular target for several classes of therapeutics. CAIX is overexpressed in a large fraction of renal cell carcinomas (RCC). Radionuclide molecular imaging of CAIX-expression might offer a non-invasive methodology for stratification of patients with disseminated RCC for CAIX-targeting therapeutics. Radiolabeled monoclonal antibodies and their fragments are actively investigated for imaging of CAIX expression. Promising alternatives are small non-immunoglobulin scaffold proteins, such as affibody molecules. A CAIX-targeting affibody ZCAIX:2 was re-designed with the aim to decrease off-target interactions and increase imaging contrast. The new tracer, DOTA-HE3-ZCAIX:2, was labeled with In-111 and characterized in vitro. Tumor-targeting properties of [In-111]In-DOTA-HE3-ZCAIX:2 were compared head-to-head with properties of the parental variant, [(99)mTc]Tc(CO)(3)-HE3-ZCAIX:2, and the most promising antibody fragment-based tracer, [In-111]In-DTPA-G250(Fab')(2), in the same batch of nude mice bearing CAIX-expressing RCC xenografts. Compared to the (99)mTc-labeled parental variant, [In-111]In-DOTA-HE3-ZCAIX:2 provides significantly higher tumor-to-lung, tumor-to-bone and tumor-to-liver ratios, which is essential for imaging of CAIX expression in the major metastatic sites of RCC. [In-111]In-DOTA-HE3-ZCAIX:2 offers significantly higher tumor-to-organ ratios compared with [In-111]In-G250(Fab']2. In conclusion, [In-111]In-DOTA-HE3-ZCAIX:2 can be considered as a highly promising tracer for imaging of CAIX expression in RCC metastases based on our results and literature data.

Ort, förlag, år, upplaga, sidor
NATURE PUBLISHING GROUP, 2019
Nationell ämneskategori
Radiologi och bildbehandling
Identifikatorer
urn:nbn:se:kth:diva-263340 (URN)10.1038/s41598-019-51445-w (DOI)000490702200022 ()31624303 (PubMedID)2-s2.0-85073512499 (Scopus ID)
Anmärkning

QC 20191206

Tillgänglig från: 2019-12-06 Skapad: 2019-12-06 Senast uppdaterad: 2019-12-06Bibliografiskt granskad
Garousi, J., Huizing, F., Vorobyeva, A., Mitran, B., Andersson, K., Leitao, C. D., . . . Tolmachev, V. (2019). Comparison Of Affibody- And Antibody Fragments-based Caix Imaging Probes In Mice Bearing Renal Cell Carcinoma Xenografts. Paper presented at 32nd Annual Congress of the European-Association-of-Nuclear-Medicine (EANM), OCT 12-16, 2019, Barcelona, SPAIN. European Journal of Nuclear Medicine and Molecular Imaging, 46(Suppl 1), S580-S580
Öppna denna publikation i ny flik eller fönster >>Comparison Of Affibody- And Antibody Fragments-based Caix Imaging Probes In Mice Bearing Renal Cell Carcinoma Xenografts
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2019 (Engelska)Ingår i: European Journal of Nuclear Medicine and Molecular Imaging, ISSN 1619-7070, E-ISSN 1619-7089, Vol. 46, nr Suppl 1, s. S580-S580Artikel i tidskrift, Meeting abstract (Övrigt vetenskapligt) Published
Ort, förlag, år, upplaga, sidor
SPRINGER, 2019
Nationell ämneskategori
Klinisk medicin
Identifikatorer
urn:nbn:se:kth:diva-264328 (URN)10.1007/s00259-019-04486-2 (DOI)000492444400123 ()2-s2.0-85073183616 (Scopus ID)
Konferens
32nd Annual Congress of the European-Association-of-Nuclear-Medicine (EANM), OCT 12-16, 2019, Barcelona, SPAIN
Anmärkning

QC 20191202

Tillgänglig från: 2019-12-02 Skapad: 2019-12-02 Senast uppdaterad: 2020-01-10Bibliografiskt granskad
Vorobyeva, A., Schulga, A., Konovalova, E., Güler, R., Mitran, B., Garousi, J., . . . Tolmachev, V. (2019). 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, 54(4), 1209-1220
Öppna denna publikation i ny flik eller fönster >>Comparison of tumor-targeting properties of directly and indirectly radioiodinated designed ankyrin repeat protein (DARPin) G3 variants for molecular imaging of HER2
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2019 (Engelska)Ingår i: International Journal of Oncology, ISSN 1019-6439, Vol. 54, nr 4, s. 1209-1220Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Evaluation of human epidermal growth factor receptor 2 (HER2) expression levels in breast and gastroesophageal cancer is used for the stratification of patients for HER2-targeting therapies. The use of radionuclide molecular imaging may facilitate such evaluation in a non-invasive way. Designed ankyrin repeat proteins (DARPins) are engineered scaffold proteins with high potential as probes for radionuclide molecular imaging. DARPin G3 binds with high affinity to HER2 and may be used to visualize this important therapeutic target. Studies on other engineered scaffold proteins have demonstrated that selection of the optimal labeling approach improves the sensitivity and specificity of radionuclide imaging. The present study compared two methods of labeling G3, direct and indirect radioiodination, to select an approach providing the best imaging contrast. G3-H6 was labeled with iodine-124, iodine-125 and iodine-131 using a direct method. A novel construct bearing a C-terminal cysteine, G3-GGGC, was site-specifically labeled using [125I]I-iodo-[(4-hydroxyphenyl)ethyl]maleimide (HPEM). The two radiolabeled G3 variants preserved binding specificity and high affinity to HER2-expressing cells. The specificity of tumor targeting in vivo was demonstrated. Biodistribution comparison of [131I]I-G3-H6 and [125I]I-HPEM-G3-GGGC in mice, bearing HER2-expressing SKOV3 xenografts, demonstrated an appreciable contribution of hepatobiliary excretion to the clearance of [125I]I-HPEM-G3-GGGC and a decreased tumor uptake compared to [131I]I-G3-H6. The direct label provided higher tumor-to-blood and tumor-to-organ ratios compared with the indirect label at 4 h post-injection. The feasibility of high contrast PET/CT imaging of HER2 expression in SKOV3 xenografts in mice using [124I]I-G3-H6 was demonstrated. In conclusion, direct radioiodination is the preferable approach for labeling DARPin G3 with iodine-123 and iodine-124 for clinical single photon emission computed tomography and positron emission tomography imaging.

Ort, förlag, år, upplaga, sidor
SPANDIDOS PUBL LTD, 2019
Nyckelord
DARPin, HER2, imaging, radionuclide, iodine, radioiodination
Nationell ämneskategori
Cancer och onkologi
Identifikatorer
urn:nbn:se:kth:diva-248065 (URN)10.3892/ijo.2019.4712 (DOI)000461097600006 ()30968147 (PubMedID)2-s2.0-85062653493 (Scopus ID)
Anmärkning

QC 20190429

Tillgänglig från: 2019-04-29 Skapad: 2019-04-29 Senast uppdaterad: 2020-03-09Bibliografiskt granskad
Meister, S., Hendrikse, N. & Löfblom, J. (2019). Directed evolution of the 3C protease from coxsackievirus using a novel fluorescence-assisted intracellular method. Biological chemistry (Print), 400(3), 405-415
Öppna denna publikation i ny flik eller fönster >>Directed evolution of the 3C protease from coxsackievirus using a novel fluorescence-assisted intracellular method
2019 (Engelska)Ingår i: Biological chemistry (Print), ISSN 1431-6730, E-ISSN 1437-4315, Vol. 400, nr 3, s. 405-415Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Proteases are crucial for regulating biological processes in organisms through hydrolysis of peptide bonds. Recombinant proteases have moreover become important tools in biotechnological, and biomedical research and as therapeutics. We have developed a label-free high-throughput method for quantitative assessment of proteolytic activity in Escherichia coli. The screening method is based on co-expression of a protease of interest and a reporter complex. This reporter consists of an aggregation-prone peptide fused to a fluorescent protein via a linker that contains the corresponding substrate sequence. Cleavage of the substrate rescues the fluorescent protein from aggregation, resulting in increased fluorescence that correlates to proteolytic activity, which can be monitored using flow cytometry. In one round of flow-cytometric cell sorting, we isolated an efficiently cleaved tobacco etch virus (TEV) substrate from a 1:100 000 background of non-cleavable sequences, with around 6000-fold enrichment. We then engineered the 3C protease from coxsackievirus B3 (CVB3 3C(pro)) towards improved proteolytic activity on the substrate LEVLFQ down arrow GP. We isolated highly proteolytic active variants from a randomly mutated CVB3 3C(pro) library with up to 4-fold increase in activity. The method enables simultaneous measurement of proteolytic activity and protease expression levels and can therefore be applied for protease substrate profiling, as well as directed evolution of proteases.

Ort, förlag, år, upplaga, sidor
WALTER DE GRUYTER GMBH, 2019
Nyckelord
Coxsackievirus B3, FACS, GFP-fusion, intracellular assay, protease engineering, protease substrate profiling
Nationell ämneskategori
Biokemi och molekylärbiologi
Identifikatorer
urn:nbn:se:kth:diva-245129 (URN)10.1515/hsz-2018-0362 (DOI)000458628400014 ()30521472 (PubMedID)2-s2.0-85058219114 (Scopus ID)
Anmärkning

QC 20190313

Tillgänglig från: 2019-03-13 Skapad: 2019-03-13 Senast uppdaterad: 2019-03-18Bibliografiskt granskad
Rosestedt, M., Andersson, K. G., Rinne, S. S., Leitao, C. D., Mitran, B., Vorobyeva, A., . . . Orlova, A. (2019). 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, 9, Article ID 6779.
Öppna denna publikation i ny flik eller fönster >>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
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2019 (Engelska)Ingår i: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, artikel-id 6779Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Human epidermal growth factor receptor type 3 (HER3) plays a crucial role in the progression of many cancer types. In vivo radionuclide imaging could be a reliable method for repetitive detection of HER3-expression in tumors. The main challenge of HER3-imaging is the low expression in tumors together with endogenous receptor expression in normal tissues, particularly the liver. A HER3-targeting affibody molecule labeled with radiocobalt via a NOTA chelator [Co-57]Co-NOTA-Z(08699) has demonstrated the most favorable biodistribution profile with the lowest unspecific hepatic uptake and high activity uptake in tumors. We hypothesized that specific uptake of labeled affibody monomer might be selectively blocked in the liver but not in tumors by a co-injection of non-labeled corresponding trivalent affibody (Z(08699))(3). Biodistribution of [Co-57]Co-NOTA-Z(08699) and [In-111]ln-DOTA-(Z(08699))(3) was studied in BxPC-3 xenografted mice. [Co-57]Co-NOTA-Z(08699) was co-injected with unlabeled trivalent affibody DOTA-(Z(08699))(3) at different monomer:trimer molar ratios. HER3-expression in xenografts was imaged using [Co-57]Co-NOTA-Z(08699) and [Co-57]Co-NOTA-Z(08699): DOTA-(Z(08699))(3). Hepatic activity uptake of [Co-57] Co-NOTA-Z(08699): DOTA-(Z(08699))(3) decreased with increasing monomer:trimer molar ratio. The tumor activity uptake and tumor-to-liver ratios were the highest for the 1:3 ratio. SPECT/CT images confirmed the biodistribution data. Imaging of HER3 expression can be improved by co-injection of a radiolabeled monomeric affi body-based imaging probe together with a trivalent affibody.

Ort, förlag, år, upplaga, sidor
NATURE PUBLISHING GROUP, 2019
Nationell ämneskategori
Radiologi och bildbehandling
Identifikatorer
urn:nbn:se:kth:diva-270659 (URN)10.1038/s41598-019-43145-2 (DOI)000466358700048 ()31043683 (PubMedID)2-s2.0-85065179852 (Scopus ID)
Anmärkning

QC 20200325

Tillgänglig från: 2020-03-25 Skapad: 2020-03-25 Senast uppdaterad: 2020-03-25Bibliografiskt granskad
Rinne, S. S., Leitao, C. D., Gentry, J., Mitran, B., Abouzayed, A., Tolmachev, V., . . . Orlova, A. (2019). 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, 9, Article ID 17710.
Öppna denna publikation i ny flik eller fönster >>Increase in negative charge of Ga-68/chelator complex reduces unspecific hepatic uptake but does not improve imaging properties of HER3-targeting affibody molecules
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2019 (Engelska)Ingår i: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, artikel-id 17710Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Upregulation of the human epidermal growth factor receptor type 3 (HER3) is a common mechanism to bypass HER-targeted cancer therapy. Affibody-based molecular imaging has the potential for detecting and monitoring HER3 expression during treatment. In this study, we compared the imaging properties of newly generated Ga-68-labeled anti-HER3 affibody molecules (HE)(3)-Z(HER3)-DOTA and (HE)(3)-Z(HER3)-DOTAGA with previously reported [Ga-68]Ga-(HE)(3)-Z(HER3)-NODAGA. We hypothesized that increasing the negative charge of the gallium-68/chelator complex would reduce hepatic uptake, which could lead to improved contrast of anti-HER3 affibody-based PET-imaging of HER3 expression. (HE)(3)-Z(HER3)-X (X = DOTA, DOTAGA) were produced and labeled with gallium-68. Binding of the new conjugates was specific in HER3 expressing BxPC-3 and DU145 human cancer cells. Biodistribution and in vivo specificity was studied in BxPC-3 xenograft bearing Balb/c nu/nu mice 3 h pi. DOTA- and DOTAGA-containing conjugates had significantly higher concentration in blood than [Ga-68]Ga-(HE)(3)-Z(HER3)-NODAGA. Presence of the negatively charged Ga-68-DOTAGA complex reduced the unspecific hepatic uptake, but did not improve overall biodistribution of the conjugate. [Ga-68]Ga-(HE)(3)-Z(HER3)-DOTAGA and [Ga-68]Ga-(HE)(3)-Z(HER3)-NODAGA had similar tumor-to-liver ratios, but [Ga-68]Ga-(HE)(3)-Z(HER3)-NODAGA had the highest tumor uptake and tumor-to-blood ratio among the tested conjugates. In conclusion, [Ga-68] Ga-(HE)(3)-Z(HER3)-NODAGA remains the favorable variant for PET imaging of HER3 expression.

Ort, förlag, år, upplaga, sidor
Nature Publishing Group, 2019
Nationell ämneskategori
Kemi
Identifikatorer
urn:nbn:se:kth:diva-265481 (URN)10.1038/s41598-019-54149-3 (DOI)000499205900001 ()31776413 (PubMedID)2-s2.0-85075755842 (Scopus ID)
Anmärkning

QC 20191213

Tillgänglig från: 2019-12-13 Skapad: 2019-12-13 Senast uppdaterad: 2020-01-09Bibliografiskt granskad
Dahlsson Leitao, C., Rinne, S. S., Mitran, B., Vorobyeva, A., Andersson, K. G., Tolmachev, V., . . . Orlova, A. (2019). 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, 20(5)
Öppna denna publikation i ny flik eller fönster >>Molecular Design of HER3-Targeting Affibody Molecules: Influence of Chelator and Presence of HEHEHE-Tag on Biodistribution of 68 Ga-Labeled Tracers
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2019 (Engelska)Ingår i: International Journal of Molecular Sciences, ISSN 1422-0067, E-ISSN 1422-0067, Vol. 20, nr 5Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Affibody-based imaging of HER3 is a promising approach for patient stratification. We investigated the influence of a hydrophilic HEHEHE-tag ((HE)₃-tag) and two different gallium-68/chelator-complexes on the biodistribution of Z08698 with the aim to improve the tracer for PET imaging. Affibody molecules (HE)₃-Z08698-X and Z08698-X (X = NOTA, NODAGA) were produced and labeled with gallium-68. Binding specificity and cellular processing were studied in HER3-expressing human cancer cell lines BxPC-3 and DU145. Biodistribution was studied 3 h p.i. in Balb/c nu/nu mice bearing BxPC-3 xenografts. Mice were imaged 3 h p.i. using microPET/CT. Conjugates were stably labeled with gallium-68 and bound specifically to HER3 in vitro and in vivo. Association to cells was rapid but internalization was slow. Uptake in tissues, including tumors, was lower for (HE)₃-Z08698-X than for non-tagged variants. The neutral [68Ga]Ga-NODAGA complex reduced the hepatic uptake of Z08698 compared to positively charged [68Ga]Ga-NOTA-conjugated variants. The influence of the chelator was more pronounced in variants without (HE)3-tag. In conclusion, hydrophilic (HE)₃-tag and neutral charge of the [68Ga]Ga-NODAGA complex promoted blood clearance and lowered hepatic uptake of Z08698. [68Ga]Ga-(HE)₃-Z08698-NODAGA was considered most promising, providing the lowest blood and hepatic uptake and the best imaging contrast among the tested variants.

Ort, förlag, år, upplaga, sidor
NLM (Medline), 2019
Nyckelord
affibody, gallium-68, HER3, molecular imaging, NODAGA, NOTA, PET
Nationell ämneskategori
Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)
Identifikatorer
urn:nbn:se:kth:diva-246490 (URN)10.3390/ijms20051080 (DOI)000462542300079 ()30832342 (PubMedID)2-s2.0-85062394960 (Scopus ID)
Anmärkning

QC 20190326

Tillgänglig från: 2019-03-26 Skapad: 2019-03-26 Senast uppdaterad: 2019-04-23Bibliografiskt granskad
Vorobyeva, A., Schulga, A., Konovalova, E., Güler, R., Löfblom, J., Sandstrom, M., . . . Deyev, S. M. (2019). N-terminal position of histidine-glutamate-containing tag improves biodistribution of [Tc-99m]Tc-labeled DARPin G3. Paper presented at 32nd Annual Congress of the European-Association-of-Nuclear-Medicine (EANM), OCT 12-16, 2019, Barcelona, SPAIN. European Journal of Nuclear Medicine and Molecular Imaging, 46(SUPPL 1), S749-S749
Öppna denna publikation i ny flik eller fönster >>N-terminal position of histidine-glutamate-containing tag improves biodistribution of [Tc-99m]Tc-labeled DARPin G3
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2019 (Engelska)Ingår i: European Journal of Nuclear Medicine and Molecular Imaging, ISSN 1619-7070, E-ISSN 1619-7089, Vol. 46, nr SUPPL 1, s. S749-S749Artikel i tidskrift, Meeting abstract (Övrigt vetenskapligt) Published
Ort, förlag, år, upplaga, sidor
SPRINGER, 2019
Nationell ämneskategori
Klinisk medicin
Identifikatorer
urn:nbn:se:kth:diva-264318 (URN)000492444407025 ()
Konferens
32nd Annual Congress of the European-Association-of-Nuclear-Medicine (EANM), OCT 12-16, 2019, Barcelona, SPAIN
Anmärkning

QC 20191202

Tillgänglig från: 2019-12-02 Skapad: 2019-12-02 Senast uppdaterad: 2019-12-02Bibliografiskt granskad
Organisationer
Identifikatorer
ORCID-id: ORCID iD iconorcid.org/0000-0001-9423-0541

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