Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Martin H Schaefer"'
Publikováno v:
eLife, Vol 11 (2022)
Aneuploidy, a state of chromosome imbalance, is a hallmark of human tumors, but its role in cancer still remains to be fully elucidated. To understand the consequences of whole-chromosome-level aneuploidies on the proteome, we integrated aneuploidy,
Externí odkaz:
https://doaj.org/article/f458247280e6471d95eb928989243348
Publikováno v:
Molecular Systems Biology, Vol 17, Iss 3, Pp n/a-n/a (2021)
Externí odkaz:
https://doaj.org/article/97fbd3d5c23248048fbde9447f822825
Autor:
Sarah A Head, Xavier Hernandez-Alias, Jae-Seong Yang, Ludovica Ciampi, Violeta Beltran-Sastre, Antonio Torres-Méndez, Manuel Irimia, Martin H Schaefer, Luis Serrano
Publikováno v:
PLoS Biology, Vol 19, Iss 2, p e3001138 (2021)
RNA splicing is widely dysregulated in cancer, frequently due to altered expression or activity of splicing factors (SFs). Microexons are extremely small exons (3-27 nucleotides long) that are highly evolutionarily conserved and play critical roles i
Externí odkaz:
https://doaj.org/article/76df6cb1b2ea420c84a74a8d5bee3d8b
Publikováno v:
Molecular Systems Biology, Vol 16, Iss 3, Pp n/a-n/a (2020)
Abstract Different tissues express genes with particular codon usage and anticodon tRNA repertoires. However, the codon–anticodon co‐adaptation in humans is not completely understood, nor is its effect on tissue‐specific protein levels. Here, w
Externí odkaz:
https://doaj.org/article/5328167fdb934cf4bd1d3f8b3a425a36
Publikováno v:
eLife, Vol 5 (2016)
Copy number alterations (CNAs) in cancer patients show a large variability in their number, length and position, but the sources of this variability are not known. CNA number and length are linked to patient survival, suggesting clinical relevance. W
Externí odkaz:
https://doaj.org/article/8b33e334a5fe48889ba953d661d83f4a
Publikováno v:
Frontiers in Genetics, Vol 6 (2015)
Protein-protein interaction (PPI) networks are associated with multiple types of biases partly rooted in technical limitations of the experimental techniques. Another source of bias are the different frequencies with which proteins have been studied
Externí odkaz:
https://doaj.org/article/b78c72c07b33496a809a2da1ab145b28
Autor:
Apichat Suratanee, Martin H Schaefer, Matthew J Betts, Zita Soons, Heiko Mannsperger, Nathalie Harder, Marcus Oswald, Markus Gipp, Ellen Ramminger, Guillermo Marcus, Reinhard Männer, Karl Rohr, Erich Wanker, Robert B Russell, Miguel A Andrade-Navarro, Roland Eils, Rainer König
Publikováno v:
PLoS Computational Biology, Vol 10, Iss 9, p e1003814 (2014)
Characterizing the activating and inhibiting effect of protein-protein interactions (PPI) is fundamental to gain insight into the complex signaling system of a human cell. A plethora of methods has been suggested to infer PPI from data on a large sca
Externí odkaz:
https://doaj.org/article/e01205940d804bc0bcc38759f7abd7ed
Publikováno v:
PLoS Computational Biology, Vol 10, Iss 6, p e1003659 (2014)
Many proteins and signaling pathways are present in most cell types and tissues and yet perform specialized functions. To elucidate mechanisms by which these ubiquitous pathways are modulated, we overlaid information about cross-cell line protein abu
Externí odkaz:
https://doaj.org/article/0d5c301790a541c5be777529a0075d78
Autor:
Martin H Schaefer, Tiago J S Lopes, Nancy Mah, Jason E Shoemaker, Yukiko Matsuoka, Jean-Fred Fontaine, Caroline Louis-Jeune, Amie J Eisfeld, Gabriele Neumann, Carol Perez-Iratxeta, Yoshihiro Kawaoka, Hiroaki Kitano, Miguel A Andrade-Navarro
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 1, p e1002860 (2013)
Interactions of proteins regulate signaling, catalysis, gene expression and many other cellular functions. Therefore, characterizing the entire human interactome is a key effort in current proteomics research. This challenge is complicated by the dyn
Externí odkaz:
https://doaj.org/article/e759ad74877144fcb8e54790c4b22681
Autor:
David Fournier, Gareth A Palidwor, Sergey Shcherbinin, Angelika Szengel, Martin H Schaefer, Carol Perez-Iratxeta, Miguel A Andrade-Navarro
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e79894 (2013)
Alpha-solenoids are flexible protein structural domains formed by ensembles of alpha-helical repeats (Armadillo and HEAT repeats among others). While homology can be used to detect many of these repeats, some alpha-solenoids have very little sequence
Externí odkaz:
https://doaj.org/article/88a72ad9995a458a8a90390d1b8e954e