Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Juan Astorga-Wells"'
Autor:
Aman Mebrahtu, Ida Laurén, Rosanne Veerman, Gözde Güclüler Akpinar, Martin Lord, Alexandros Kostakis, Juan Astorga-Wells, Leif Dahllund, Anders Olsson, Oscar Andersson, Jonathan Persson, Helena Persson, Pierre Dönnes, Johan Rockberg, Sara Mangsbo
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-20 (2024)
Abstract Current antibody-based immunotherapy depends on tumor antigen shedding for proper T cell priming. Here we select a novel human CD40 agonistic drug candidate and generate a bispecific antibody, herein named BiA9*2_HF, that allows for rapid an
Externí odkaz:
https://doaj.org/article/d469af897715422a9a5f977bb3bd08a2
Autor:
Jijing Wang, Susanna L. Lundström, Sven Seelow, Sergey Rodin, Zhaowei Meng, Juan Astorga-Wells, Qinyu Jia, Roman A. Zubarev
Publikováno v:
Molecules, Vol 26, Iss 21, p 6709 (2021)
Isoaspartate (isoAsp) is a damaging amino acid residue formed in proteins mostly as a result of spontaneous deamidation of asparaginyl residues. An association has been found between isoAsp in human serum albumin (HSA) and Alzheimer’s disease (AD).
Externí odkaz:
https://doaj.org/article/406db28c57ae42aa81e660866e97c59f
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0134293 (2015)
The opportunistic pathogen Pseudomonas aeruginosa can grow under both aerobic and anaerobic conditions. Its flexibility with respect to oxygen load is reflected by the fact that its genome encodes all three existing classes of ribonucleotides reducta
Externí odkaz:
https://doaj.org/article/28a22ff0c5b24503b09c5ebbaabcc800
Autor:
Leo, Hanke, Daniel J, Sheward, Alec, Pankow, Laura Perez, Vidakovics, Vivien, Karl, Changil, Kim, Egon, Urgard, Natalie L, Smith, Juan, Astorga-Wells, Simon, Ekström, Jonathan M, Coquet, Gerald M, McInerney, Ben, Murrell
Publikováno v:
Science advances. 8(12)
Conventional approaches to isolate and characterize nanobodies are laborious. We combine phage display, multivariate enrichment, next-generation sequencing, and a streamlined screening strategy to identify numerous anti-severe acute respiratory syndr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0be67e77a61d93e6da754f91043f2977
https://pubmed.ncbi.nlm.nih.gov/35333580
https://pubmed.ncbi.nlm.nih.gov/35333580
Autor:
Ben Murrell, Changil Kim, Leo Hanke, Laura Perez Vidakovics, Jonathan M. Coquet, Natalie L Smith, Daniel J. Sheward, Vivien Karl, Alec Pankow, Gerald M. McInerney, Egon Urgard, Juan Astorga-Wells, Simon Ekström
Conventional approaches to isolate and characterize nanobodies are laborious and cumbersome. Here we combine phage display, multivariate enrichment, and novel sequence analysis techniques to annotate an entire nanobody repertoire from an immunized al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c0281422be543615bdcd72b1b27ab578
https://doi.org/10.1101/2021.07.25.453673
https://doi.org/10.1101/2021.07.25.453673
Autor:
Qing Cheng, Tobias Karlberg, Susanna L. Lundström, Sergey Rodin, Herwig Schüler, Alexey Chernobrovkin, Christian M. Beusch, Massimiliano Gaetani, Katja Näreoja, Ákos Végvári, Roman A. Zubarev, Hassan Gharibi, Ann-Gerd Thorsell, Zhaowei Meng, Pierre Sabatier, Elias S.J. Arnér, Amir Ata Saei, Juan Astorga Wells
This protocol describes the proteomics technique called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis or SIESTA 1,2. SIESTA can be used for universal discovery of enzyme substrates that shift in thermal stabil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e73587003dc573af8183717e61841907
https://doi.org/10.21203/rs.3.pex-1327/v1
https://doi.org/10.21203/rs.3.pex-1327/v1
Autor:
Sergey Rodin, Christian M. Beusch, Katja Näreoja, Herwig Schüler, Pierre Sabatier, Hassan Gharibi, Elias S.J. Arnér, Amir Ata Saei, Alexey Chernobrovkin, Massimiliano Gaetani, Zhaowei Meng, Ann-Gerd Thorsell, Ákos Végvári, Qing Cheng, Susanna L. Lundström, Roman A. Zubarev, Tobias Karlberg, Juan Astorga Wells
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications
Nature Communications
Despite the immense importance of enzyme–substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-through
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fbc6c8284cbd513051e2785bbe3ed02
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-436138
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-436138
Autor:
Iryna Kolosenko, Matthieu Desroses, Thomas Helleday, Sander Busker, Juan Astorga-Wells, Dan Grandér, Sanaz Attarha, Roman A. Zubarev, Brent D. G. Page
Publikováno v:
Journal of Pharmaceutical and Biomedical Analysis. 160:80-88
STAT3 protein is an established target for the development of new cancer therapeutic agents. Despite lacking a traditional binding site for small molecule inhibitors, many STAT3 inhibitors have been identified and explored for their anti-cancer activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d66cd3a9e94facd5337f92370cf17253
https://doi.org/10.1016/j.jpba.2018.07.018
https://doi.org/10.1016/j.jpba.2018.07.018
Autor:
Taeyang Jung, Hyeongju Kim, Roy Jung, Alexander Leitner, Ihn Sik Seong, Ji-Joon Song, Hans Hebert, Ruedi Aebersold, Giorgio E. Tamò, Juan Astorga-Wells, Baehyun Shin, Maria J. Marcaida, Matteo Dal Peraro, Ravi Vijayvargia
The polyQ-expansion at the N-terminus of huntingtin (HTT) is the prime cause of Huntington’s disease. The recent cryo-EM structure of HTT with HAP40 provides information on the protein’s prominent HEAT-repeats. Here, we present analyses of the im
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25155d600caef7e7a92c3b52518f706d
https://doi.org/10.1101/721191
https://doi.org/10.1101/721191
Autor:
Izabela Behrendt, Martyna Prądzińska, Roman A. Zubarev, Paulina Czaplewska, Aleksandra S. Kołodziejczyk, Juan Astorga-Wells, Sylwia Rodziewicz-Motowidło, Aleksandr Manoilov
Publikováno v:
Amino Acids
Human cystatin C (hCC) is a small cysteine protease inhibitor whose oligomerization by propagated domain swapping is linked to certain neurological disorders. One of the ways to prevent hCC dimerization and fibrillogenesis is to enable its interactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2645a683fb69b9cf39cc04109222d2de
https://doi.org/10.1007/s00726-016-2316-y
https://doi.org/10.1007/s00726-016-2316-y