Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Helen, Hoffmeister"'
Autor:
Kristina Kovač, Anja Sauer, Igor Mačinković, Stephan Awe, Florian Finkernagel, Helen Hoffmeister, Andreas Fuchs, Rolf Müller, Christina Rathke, Gernot Längst, Alexander Brehm
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
ATP-dependent chromatin remodelers are often found mutated in human cancers. Here, the authors characterize the nucleosome remodelling properties of cancer-associated mutants of the Drosophila Chd4 homolog dMi-2.
Externí odkaz:
https://doaj.org/article/4b4ca0b894bf4df581150e361275c81e
Autor:
Helen Hoffmeister, Simon Holzinger, Marie-Sofie Dürr, Astrid Bruckmann, Susanne Schindler, Regina Gröbner-Ferreira, Reinhard Depping, Gernot Längst
Publikováno v:
Journal of Cell Science. 136
Chromatin remodeling enzymes form large multiprotein complexes that play central roles in regulating access to the genome. Here, we characterize the nuclear import of the human CHD4 protein. We show that CHD4 enters the nucleus by means of several im
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::780a3c3d2c0b915ac83af16c2247104a
https://doi.org/10.1242/jcs.260724
https://doi.org/10.1242/jcs.260724
Autor:
Leonhard Heizinger, Andreas Fuchs, Stefan Dove, Regina Groebner-Ferreira, Helen Hoffmeister, Laura Strobl, Elizabeth A. Komives, Julian Nazet, Gernot Längst, Rainer Merkl
Publikováno v:
The FEBS Journal. 288:4000-4023
Chromatin remodelers use the energy of ATP hydrolysis to regulate chromatin dynamics. Their impact for development and disease requires strict enzymatic control. Here, we address the differential regulability of the ATPase domain of hSNF2H and hCHD3,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d986b534418131a9ad7695620d566ab2
https://doi.org/10.1111/febs.15699
https://doi.org/10.1111/febs.15699
Autor:
Alexander Brehm, Andreas Fuchs, Igor Mačinković, Gernot Längst, Anja Sauer, Christina Rathke, Kristina Kovač, Rolf Müller, Helen Hoffmeister, Stephan Awe, Florian Finkernagel
Publikováno v:
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
ATP-dependent chromatin remodellers are mutated in more than 20% of human cancers. The consequences of these mutations on enzyme function are poorly understood. Here, we characterise the effects of CHD4 mutations identified in endometrial carcinoma o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc2fd05b07ec6ed2e938103f934aea7a
https://pubmed.ncbi.nlm.nih.gov/29844320
https://pubmed.ncbi.nlm.nih.gov/29844320
Autor:
Raphael Hubrich, Helen Hoffmeister, Claudia Steinem, Michaela Schatz, Anya Krefft, Daniela Morick, Ralph Witzgall
Publikováno v:
Biochemical and Biophysical Research Communications. 437:532-537
Polycystin-2 (PC2) trafficking has been proposed to be a result of the interaction of PIGEA14 with PC2 as a function of the phosphorylation state of PC2. Here, we investigated the interaction of PIGEA14 with the C-terminal part of polycystin-2 wild t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25a3533faa5c28294ef39bd440b039b7
https://doi.org/10.1016/j.bbrc.2013.06.105
https://doi.org/10.1016/j.bbrc.2013.06.105
Autor:
Helen, Hoffmeister, Andreas, Fuchs, Fabian, Erdel, Sophia, Pinz, Regina, Gröbner-Ferreira, Astrid, Bruckmann, Rainer, Deutzmann, Uwe, Schwartz, Rodrigo, Maldonado, Claudia, Huber, Anne-Sarah, Dendorfer, Karsten, Rippe, Gernot, Längst
Publikováno v:
Nucleic Acids Research
CHD3 and CHD4 (Chromodomain Helicase DNA binding protein), two highly similar representatives of the Mi-2 subfamily of SF2 helicases, are coexpressed in many cell lines and tissues and have been reported to act as the motor subunit of the NuRD comple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::1cffcb0b7cff717d2f5b4f9a8d2b4e4c
Autor:
Helen Hoffmeister, Frank Schumann, Ralph Witzgall, M Schmidt, Reto Bader, Hans Robert Kalbitzer
Publikováno v:
Journal of Biological Chemistry. 284:24372-24383
The PKD1 and PKD2 genes are the genes that are mutated in patients suffering from autosomal dominant polycystic kidney disease. The human PKD2 gene codes for a 968-amino acid long membrane protein called polycystin-2 that represents a cation channel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3db6e0d1ba398827ceaad9992eadb41a
https://doi.org/10.1074/jbc.m109.025635
https://doi.org/10.1074/jbc.m109.025635
Autor:
Thu-Hang, Pham, Julia, Minderjahn, Christian, Schmidl, Helen, Hoffmeister, Sandra, Schmidhofer, Wei, Chen, Gernot, Längst, Christopher, Benner, Michael, Rehli
Publikováno v:
Nucleic Acids Research
The transcription factor PU.1 is crucial for the development of many hematopoietic lineages and its binding patterns significantly change during differentiation processes. However, the ‘rules’ for binding or not-binding of potential binding sites
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::36433dc9a1c753bd53adb3054dd4fb92
https://pubmed.ncbi.nlm.nih.gov/23658224
https://pubmed.ncbi.nlm.nih.gov/23658224
Autor:
Karin Babinger, Larissa Osten, Anne Rascle, Karin Schadendorf, Sonja Gürster, Uwe de Vries, Helen Hoffmeister, Anna Cedzich, Ralph Witzgall, Christine Meese
Publikováno v:
The Journal of Cell Biology
Polycystin-2 goes through the Golgi apparatus when going to the plasma membrane, but bypasses it en route to the ciliary membrane.
Polycystin-2 (also called TRPP2), an integral membrane protein mutated in patients with cystic kidney disease, is
Polycystin-2 (also called TRPP2), an integral membrane protein mutated in patients with cystic kidney disease, is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dcb8dea0f8d5747f51b670f137bbe1d
https://pubmed.ncbi.nlm.nih.gov/21321097
https://pubmed.ncbi.nlm.nih.gov/21321097
Publikováno v:
The Biochemical journal. 433(2)
PKD2 is one of the two genes mutated in ADPKD (autosomal-dominant polycystic kidney disease). The protein product of PKD2, polycystin-2, functions as a non-selective cation channel in the endoplasmic reticulum and possibly at the plasma membrane. Hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed44b9a4a5afc808b5e7f707c6a4bc80
https://pubmed.ncbi.nlm.nih.gov/21044049
https://pubmed.ncbi.nlm.nih.gov/21044049