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parD toxin-antitoxin system of plasmid R1 - basic contributions, biotechnological applications and relationships with closely-related toxin-antitoxin systems

Autor: Elizabeth Diago-Navarro, Ana J. Muñoz-Gómez, Marc Lemonnier, Rolf Boelens, Ana M. Hernández-Arriaga, Juan López-Villarejo, Monique B. Kamphuis, Ramón Díaz-Orejas

Publikováno v: FEBS Journal. 277:3097-3117

Toxin–antitoxin systems, as found in bacterial plasmids and their host chromosomes, play a role in the maintenance of genetic information, as well as in the response to stress. We describe the basic biology of the parD/kiskid toxin–antitoxin syst

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::79a78d7712c670f57705fcfa8bb60250
https://doi.org/10.1111/j.1742-4658.2010.07722.x

The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates

Autor: Carlo P. M. van Mierlo, Monique B. Kamphuis, Yves J. M. Bollen

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America 103 (2006) 11
Proceedings of the National Academy of Sciences of the United States of America, 103(11), 4095-4100
Proceedings of the National Academy of Sciences of the United States of America, 103, 4095-4100. National Acad Sciences
Bollen, Y J M, Kamphuis, M B & Van Mierlo, C P M 2006, ' The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates. ', Proceedings of the National Academy of Sciences of the United States of America, vol. 103, pp. 4095-4100 . https://doi.org/10.1073/pnas.0509133103

Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and NMR spectroscopy. Knowledge about these metastable states is required to better understand the onset of folding-related d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0179b28241d433ec79d8be1472d4abf2
https://doi.org/10.1073/pnas.0509133103

The CXCR3 Binding Chemokine IP-10/CXCL10: Structure and Receptor Interactions

Autor: Ian Clark-Lewis, Valerie Booth, David W. Keizer, B.D. Sykes, Monique B Kamphuis

Publikováno v: Biochemistry. 41:10418-10425

The structure of IP-10 was solved by NMR spectroscopy and represents the first structure from the class of agonists toward the receptor CXCR3. CXCR3 binding chemokines are unique in their ability to bind receptors from both the CC and CXC classes of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1f3ed7b054fb7d1ab2460b81bc39cf5
https://doi.org/10.1021/bi026020q

A mutagenic analysis of the RNase mechanism of the bacterial Kid toxin by mass spectrometry

Autor: Elizabeth, Diago-Navarro, Monique B, Kamphuis, Rolf, Boelens, Arjan, Barendregt, Albert J, Heck, Robert H, van den Heuvel, Ramón, Díaz-Orejas

Publikováno v: The FEBS journal. 276(17)

Kid, the toxin of the parD (kis, kid) maintenance system of plasmid R1, is an endoribonuclease that preferentially cleaves RNA at the 5' of A in the core sequence 5'-UA(A/C)-3'. A model of the Kid toxin interacting with the uncleavable mimetic 5'-AdU

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6ab84f06859e40760b1c0b3e017fd34a
https://pubmed.ncbi.nlm.nih.gov/19694809