Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Geri F, Moolenaar"'
Autor:
Ramon A van der Valk, Jocelyne Vreede, Liang Qin, Geri F Moolenaar, Andreas Hofmann, Nora Goosen, Remus T Dame
Publikováno v:
eLife, Vol 6 (2017)
Bacteria frequently need to adapt to altered environmental conditions. Adaptation requires changes in gene expression, often mediated by global regulators of transcription. The nucleoid-associated protein H-NS is a key global regulator in Gram-negati
Externí odkaz:
https://doaj.org/article/7e8de8306837484288f8eca19e55465f
Autor:
Kassiani Kytidou, Thomas J. M. Beenakker, Lotte B. Westerhof, Cornelis H. Hokke, Geri F. Moolenaar, Nora Goosen, Mina Mirzaian, Maria J. Ferraz, Mark de Geus, Wouter W. Kallemeijn, Herman S. Overkleeft, Rolf G. Boot, Arjen Schots, Dirk Bosch, Johannes M. F. G. Aerts
Publikováno v:
Frontiers in Plant Science, Vol 8 (2017)
Deficiency of α-galactosidase A (α-GAL) causes Fabry disease (FD), an X-linked storage disease of the glycosphingolipid globtriaosylcerammide (Gb3) in lysosomes of various cells and elevated plasma globotriaosylsphingosine (Lyso-Gb3) toxic for podo
Externí odkaz:
https://doaj.org/article/65d83c0c2ed34ed3bbeb8805c99ee953
Autor:
Mia Urem, Teunke van Rossum, Giselda Bucca, Geri F. Moolenaar, Emma Laing, Magda A. Świątek-Połatyńska, Joost Willemse, Elodie Tenconi, Sébastien Rigali, Nora Goosen, Colin P. Smith, Gilles P. van Wezel
Publikováno v:
mSystems, Vol 1, Iss 3 (2016)
ABSTRACT Two-component regulatory systems allow bacteria to respond adequately to changes in their environment. In response to a given stimulus, a sensory kinase activates its cognate response regulator via reversible phosphorylation. The response re
Externí odkaz:
https://doaj.org/article/d0d85a81b67a4222a27d115c79c8e771
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1837
DNA looping is important for genome organization in all domains of life. The basis of DNA loop formation is the bridging of two separate DNA double helices. Detecting DNA bridge formation generally involves the use of complex single-molecule techniqu
Autor:
Maxime A. Siegler, Vincent H. S. van Rixel, Luigi Messori, Geri F. Moolenaar, Sylvestre Bonnet
Publikováno v:
Dalton Transactions, 47(2), 507-516
Dalton Transactions
Dalton Transactions
Three new trans-ruthenium(ii) complexes coordinated to tetrapyridyl ligands, namely [Ru(bapbpy)(dmso)Cl]Cl ([2]Cl), [Ru(bapbpy)(Hmte)2](PF6)2 ([3](PF6)2), and [Ru(biqbpy)(Hmte)2](PF6)2 ([4](PF6)2), were prepared as analogues of [Ru(biqbpy)(dmso)Cl]Cl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::629a4464029a4c2857a60eedf941c0d2
https://doi.org/10.1039/c7dt03613b
https://doi.org/10.1039/c7dt03613b
Autor:
Cornelis H. Hokke, Rebecca Katzy, Herman S. Overkleeft, Marta Artola, Johannes M. F. G. Aerts, Maria J. Ferraz, Navraj S. Pannu, Patrick Voskamp, Jules Beekwilder, Eline van Meel, Dirk Bosch, Ruud H. P. Wilbers, Geri F. Moolenaar, Kassiani Kytidou, Nora Goosen, Bogdan I. Florea, Arjen Schots
Publikováno v:
Journal of biological chemistry, 293(26), 10042-10058. American Society for Biochemistry and Molecular Biology Inc.
Journal of Biological Chemistry, 293(26), 10042-10058
Journal of Biological Chemistry
Journal of Biological Chemistry 293 (2018) 26
Journal of Biological Chemistry, 293(26), 10042-10058
Journal of Biological Chemistry
Journal of Biological Chemistry 293 (2018) 26
α-Galactosidases (EC 3.2.1.22) are retaining glycosidases that cleave terminal α-linked galactose residues from glycoconjugate substrates. α-Galactosidases take part in the turnover of cell wall–associated galactomannans in plants and in the lys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afbf72531e93112cd14695721f20b43d
https://pure.amc.nl/en/publications/nicotiana-benthamianagalactosidase-a11-can-functionally-complement-human-galactosidase-a-deficiency-associated-with-fabry-disease(a85b5a1d-6e87-4656-92d3-f2955ae41ea9).html
https://pure.amc.nl/en/publications/nicotiana-benthamianagalactosidase-a11-can-functionally-complement-human-galactosidase-a-deficiency-associated-with-fabry-disease(a85b5a1d-6e87-4656-92d3-f2955ae41ea9).html
Autor:
Anjali Pandit, Karthick Babu Sai Sankar Gupta, Maithili Krishnan, Geri F. Moolenaar, Nora Goosen
Publikováno v:
Scientific Reports
Scientific Reports, 7, 15200
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports, 7, 15200
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Plants adapt to fluctuating light conditions by a process called non-photochemical quenching (NPQ), where membrane protein PsbS plays a crucial role and transforms a change in the pH-gradient across the thylakoid membrane under excess light condition
Autor:
Liang Qin, Geri F. Moolenaar, Jocelyne Vreede, R.A. van der Valk, Remus T. Dame, Andreas Hofmann, Nora Goosen
Publikováno v:
eLife
eLife, 6:e27369. eLife Sciences Publications
ELIFE, 6, e27369
eLife, Vol 6 (2017)
ELIFE
eLife, 6:e27369. eLife Sciences Publications
ELIFE, 6, e27369
eLife, Vol 6 (2017)
ELIFE
Bacteria frequently need to adapt to altered environmental conditions. Adaptation requires changes in gene expression, often mediated by global regulators of transcription. The nucleoid-associated protein H-NS is a key global regulator in Gram-negati
Autor:
Gerrit Sitters, Niels Laurens, Geri F. Moolenaar, Remus T. Dame, Gijs J.L. Wuite, Nora Goosen, Rosalie P. C. Driessen
Publikováno v:
Biochemistry
Driessen, R P C, Sitter, G, Moolenaar, G F, Wuite, G J L, Goosen, N & Dame, R T 2014, ' Effect of Temperature on the Intrinsic Flexibility of DNA and Its Interaction with Architectural Proteins ', Biochemistry, vol. 2014, no. 53, pp. 6430-6438 . https://doi.org/10.1021/bi500344j
Biochemistry, 2014(53), 6430-6438. American Chemical Society
Driessen, R P C, Sitter, G, Moolenaar, G F, Wuite, G J L, Goosen, N & Dame, R T 2014, ' Effect of Temperature on the Intrinsic Flexibility of DNA and Its Interaction with Architectural Proteins ', Biochemistry, vol. 2014, no. 53, pp. 6430-6438 . https://doi.org/10.1021/bi500344j
Biochemistry, 2014(53), 6430-6438. American Chemical Society
The helical structure of double-stranded DNA is destabilized by increasing temperature. Above a critical temperature (the melting temperature), the two strands in duplex DNA become fully separated. Below this temperature, the structural effects are l