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Supplementary Materials, Table 1-6, Figures 1-10 from Efficient Tumor Targeting with High-Affinity Designed Ankyrin Repeat Proteins: Effects of Affinity and Molecular Size

Autor: Andreas Plückthun, Robert Waibel, H. Kaspar Binz, Roger Schibli, Birgit Dreier, Gabriela Nagy-Davidescu, Rastislav Tamaskovic, Christine de Pasquale, Michael T. Stumpp, Martin Kawe, Christian Zahnd

Supplementary Materials, Table 1-6, Figures 1-10 from Efficient Tumor Targeting with High-Affinity Designed Ankyrin Repeat Proteins: Effects of Affinity and Molecular Size

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::285a929f6f45cc62b35a0d4b774e9ce3
https://doi.org/10.1158/0008-5472.22387148.v1

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Efficient tumor targeting with high-affinity designed ankyrin repeat proteins: effects of affinity and molecular size

Autor: Robert Waibel, Christian Zahnd, Martin Kawe, H. Kaspar Binz, Christine de Pasquale, Andreas Plückthun, Roger Schibli, Gabriela Nagy-Davidescu, Rastislav Tamaskovic, Michael T. Stumpp, Birgit Dreier

Slow-clearing, tumor-targeting proteins such as monoclonal antibodies typically exhibit high tumor accumulation but low tissue contrast, whereas intermediate-sized proteins such as scFvs show faster clearance but only moderate tumor accumulation. For

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47be495da71e3096094dd63a8719801e
https://www.zora.uzh.ch/id/eprint/39967/

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Facile promoter deletion in Escherichia coli in response to leaky expression of very robust and benign proteins from common expression vectors

Autor: Martin Kawe, Uwe Horn, Andreas Plückthun

Publikováno v: Microbial Cell Factories, Vol 8, Iss 1, p 8 (2009)
Microbial Cell Factories

Background Overexpression of proteins in Escherichia coli is considered routine today, at least when the protein is soluble and not otherwise toxic for the host. We report here that the massive overproduction of even such "benign" proteins can cause

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40f80a8c9c2c28f401d5f47d30baab00
http://www.microbialcellfactories.com/content/8/1/8

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Isolation of intracellular proteinase inhibitors derived from designed ankyrin repeat proteins by genetic screening

Autor: Andreas Plückthun, Patrik Forrer, Patrick Amstutz, Martin Kawe

Publikováno v: The Journal of biological chemistry. 281(52)

The specific intracellular inhibition of protein activity at the protein level is a highly valuable tool for the validation or modulation of cellular processes. We demonstrate here the use of designed ankyrin repeat proteins (DARPins) as tailor-made

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fbac11bebb4ba63cefa8df7ff1e8cff
https://pubmed.ncbi.nlm.nih.gov/17050543

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GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening

Autor: Martin Kawe, Andreas Plückthun

Publikováno v: Journal of molecular biology. 357(2)

While support in protein folding by molecular chaperones is extremely efficient for endogenous polypeptides, it often fails for recombinant proteins in a bacterial host, thus constituting a major hurdle for protein research and biotechnology. To unde

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9f0f20300ce38f08a6f22fc8c7f68f7
https://pubmed.ncbi.nlm.nih.gov/16427651

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AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal 'living' calibration sample

Autor: Martin Kawe, J. A. Derose, Francesco Valle, Giorgio Semenza, Giovanni Dietler, Andreas Plückthun

Publikováno v: Ultramicroscopy (Amst.) 93 (2002): 83–89. doi:10.1016/S0304-3991(02)00149-3
info:cnr-pdr/source/autori:Valle, F; DeRose, JA; Dietler, G; Kawe, M; Pluckthun, A; Semenza, G/titolo:AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal "living" calibration sample/doi:10.1016%2FS0304-3991(02)00149-3/rivista:Ultramicroscopy (Amst.)/anno:2002/pagina_da:83/pagina_a:89/intervallo_pagine:83–89/volume:93

Supramolecular complexes, such as chaperonins, are suitable samples for atomic force microscope structural studies because they have a very well defined shape. High-resolution images can be made using tapping mode in liquid under native conditions. D

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74773ad3dd873ff6e77f2aa899799532

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Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy

Autor: Francesco Valle, Andreas Plückthun, Giorgio Semenza, J. A. Derose, Giovanni Dietler, Martin Kawe

Publikováno v: Journal of microscopy
203 (2001): 195–198. doi:10.1046/j.1365-2818.2001.00891.x
info:cnr-pdr/source/autori:Valle, F; Derose, JA; Dietler, G; Kawe, M; Pluckthun, A; Semenza, G/titolo:Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy/doi:10.1046%2Fj.1365-2818.2001.00891.x/rivista:Journal of microscopy (Print)/anno:2001/pagina_da:195/pagina_a:198/intervallo_pagine:195–198/volume:203

Most sample preparation methods for scanning probe or electron microscopy require that biomolecules, such as proteins, be fixed. Fixation destroys the molecular functionality and can possibly affect the true molecular structure. Here we report sample

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d90f663951b1aec1007407e1dc17492f
https://infoscience.epfl.ch/record/109092

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