Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Andreas O. Helbig"'
Autor:
Cristina Velázquez-Suárez, Benjamin L. Springstein, Mercedes Nieves-Morión, Andreas O. Helbig, Ann-Katrin Kieninger, Iris Maldener, Dennis J. Nürnberg, Karina Stucken, Ignacio Luque, Tal Dagan, Antonia Herrero
Publikováno v:
mBio, Vol 14, Iss 5 (2023)
ABSTRACT Anabaena sp. PCC 7120 grows by forming filaments of communicating cells and is considered a paradigm of bacterial multicellularity. Molecular exchanges between contiguous cells in the filament take place through multiprotein channels that tr
Externí odkaz:
https://doaj.org/article/7f4f866a4ccd4189876f1721362a01ec
Autor:
Rosalia Fernandez-Alonso, Francisco Bustos, Manon Budzyk, Pankaj Kumar, Andreas O. Helbig, Jens Hukelmann, Angus I. Lamond, Fredrik Lanner, Houjiang Zhou, Evangelia Petsalaki, Greg M. Findlay
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Fgf4 is a critical signal driving embryonic stem cell (ESC) exit from pluripotency and differentiation. Here the authors identify EPHA2 as a target of FGF4 signalling in ESCs, and show that EPHA2-EFNA1 signalling promotes pluripotent gene expression
Externí odkaz:
https://doaj.org/article/df268364679f47c9817b1c300c169406
Autor:
Andreas O. Helbig, Andreas Tholey
Publikováno v:
Analytical Chemistry. 92:5023-5032
Due to mechanisms such as proteolytic processing or alternative translation starts, in vivo proteoforms do not necessarily correspond directly to those encoded in the genome. Therefore, the knowledge of protein termini is an indispensable prerequisit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01e6fefbde6f13c8aad3ffdad3bad853
https://doi.org/10.1021/acs.analchem.9b05288
https://doi.org/10.1021/acs.analchem.9b05288
Autor:
Karina Stucken, Andreas O. Helbig, Benjamin L. Springstein, Tal Dagan, Enrique Flores, Antonia Herrero, Sergio Arévalo
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Cyanobacteria are unique among the eubacteria as they possess a hybrid Gram phenotype, having an outer membrane but also a comparably thick peptidoglycan sheet. Furthermore, the cyanobacterial divisome includes proteins specific for both the Gram typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c94aefb97311e0ade53de39260f05f0d
https://doi.org/10.1111/mmi.14483
https://doi.org/10.1111/mmi.14483
Publikováno v:
Journal of Proteome Research. 18:2954-2964
The proteome wide, mass spectrometry based identification of protein C-termini is hampered by factors such as poor ionization efficiencies, low yielding labeling strategies, or the need for enrichment procedures. We present a bottom-up proteomics wor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae58cccfb3d78f56f3f6654619bd1e99
https://doi.org/10.1021/acs.jproteome.9b00264
https://doi.org/10.1021/acs.jproteome.9b00264
Autor:
Britta Jordan, Andreas Tholey, Katrin Weidenbach, Claudia Kiessling, Mirja Gudzuhn, Harald Schwalbe, Nina Kubatova, Liam Cassidy, Miriam Gutt, Ruth A. Schmitz, Dennis J. Pyper, Andreas O. Helbig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3306ef1e960286ea015514191f712fd
https://doi.org/10.1111/febs.15799/v2/response1
https://doi.org/10.1111/febs.15799/v2/response1
Autor:
Britta Jordan, Nina Kubatova, Harald Schwalbe, Ruth A. Schmitz, Andreas Tholey, Claudia Kiessling, Dennis J. Pyper, Miriam Gutt, Mirja Gudzuhn, Katrin Weidenbach, Liam Cassidy, Andreas O. Helbig
Publikováno v:
The FEBS journalReferences. 288(18)
Small ORF (sORF)-encoded small proteins have been overlooked for a long time due to challenges in prediction and distinguishing between coding- and noncoding-predicted sORFs and in their biochemical detection and characterization. We report on the fi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abb07b5f4ba45deb781de4f47cef3767
https://pubmed.ncbi.nlm.nih.gov/33660383
https://pubmed.ncbi.nlm.nih.gov/33660383
Autor:
Julia Weissenbach, Marius L. Theune, Iris Maldener, Andreas O. Helbig, Benjamin L. Springstein, Christian Woehle, Dennis J. Nürnberg, Tal Dagan, Karina Stucken
Publikováno v:
The FEBS journalReferences. 288(10)
Polymerizing and filament-forming proteins are instrumental for numerous cellular processes such as cell division and growth. Their function in stabilization and localization of protein complexes and replicons is achieved by a filamentous structure.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03fd49ce4146c2670a6831748bb107e2
https://pubmed.ncbi.nlm.nih.gov/33205554
https://pubmed.ncbi.nlm.nih.gov/33205554
Autor:
Anushka Deshpande, Manju Kumari, Nesrin Schmiedel, Samuel Sossalla, Norbert Frey, Derk Frank, Lynn Christen, Andreas O. Helbig, Andreas Tholey, Andreas Jungmann, Alexander Bernt, Ashraf Yusuf Rangrez, Ankush Borlepawar, Oliver Müller, Anca Remes
Publikováno v:
Communications Biology
Communications Biology, Vol 3, Iss 1, Pp 1-15 (2020)
Communications Biology, Vol 3, Iss 1, Pp 1-15 (2020)
Myocardial inflammation has recently been recognized as a distinct feature of cardiac hypertrophy and heart failure. HectD3, a HECT domain containing E3 ubiquitin ligase has previously been investigated in the host defense against infections as well
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17eea95c4a375f79d3f0dcf00fdac9be
https://doi.org/10.1038/s42003-020-01289-2
https://doi.org/10.1038/s42003-020-01289-2
Autor:
Ruth A. Schmitz, Andreas O. Helbig, Kathrin Weidenbach, Philipp T. Kaulich, Andreas Tholey, Liam Cassidy
Publikováno v:
Journal of proteomics. 230
Short open reading frame-encoded peptides (SEP) represent a widely undiscovered part of the proteome. The detailed analysis of SEP has, despite inherent limitations such as incomplete sequence coverage, challenges encountered with protein inference,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6a32d15dd1f903749f2a5ac29a48cf8
https://pubmed.ncbi.nlm.nih.gov/32949814
https://pubmed.ncbi.nlm.nih.gov/32949814