De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus

Autor: Daniëlle G. M. Bosch, Nicole Corsten-Janssen, Colin A Ellis, Dirk Lefeber, Alfredo Brusco, Irene Bagnasco, Andrea Accogli, Ellen Macnamara, Carlo Di Bonaventura, Giovanna Zorzi, Scott Demarest, Erik A. Eklund, Noëlle Mercier, Carlo Marcelis, Rong Zhang, Ban H Edani, Camilo Toro, Ziv Gan-Or, Simone Pizzi, Kariona A. Grabińska, Nienke E. Verbeek, Karen W. Gripp, Simone Martinelli, Caterina Caputi, Luca Pannone, Marco Tartaglia, Felix Distelmaier, Louise Amlie-Wolf, Luisa Averdunk, Anne-Sophie Alaix, Renzo Guerrini, Laura Masuelli, Marwan Shinawi, Sunita Venkateswaran, Joseph Peeden, Hana Hansikova, Lucie Zdrazilova, William C. Sessa, Serena Galosi, Renske Oegema, Patricia G Wheeler, Kristin W. Barañano, Vincenzo Leuzzi, Frances Elmslie, Fadi F. Hamdan, Roberto Bei, Jean-Marc Good, Isis Atallah, Myriam Srour, Erik-Jan Kamsteeg

Publikováno v: Brain, 145, 1, pp. 208-223
Brain
Brain, 145(1), 208-223. Oxford University Press
Brain, vol. 145, no. 1, pp. 208-223
Brain, 145, 208-223

Subcellular membrane systems are highly enriched in dolichol, whose role in organelle homeostasis and endosomal-lysosomal pathway remains largely unclear besides being involved in protein glycosylation. DHDDS encodes for the catalytic subunit (DHDDS)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::012cb40531119a7d00e4415b8540c52c
https://research.rug.nl/en/publications/50de5bd9-24f7-4573-b0f2-fed69db9588d

Structural elucidation of the heterodimeric cis-prenyltransferase NgBR/DHDDS complex reveals novel insights in regulation of protein glycosylation

Autor: Benjamin Siciliano, Ban H Edani, Liliana Surmacz, Bill Sessa, Kariona A Grabinsko, Eon Joo Park, Ya Ha, Rong Zhang

SummaryCis-prenyltransferase (cis-PTase) catalyzes the rate-limiting step in the synthesis of glycosyl carrier lipids required for protein glycosylation in the lumen of endoplasmic reticulum. Here we report the crystal structure of the human NgBR/DHD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::76a09b21b572342708a5b43ce478dd20
https://doi.org/10.1101/2020.06.03.132209

A conserved C-terminal R

Autor: Kariona A, Grabińska, Ban H, Edani, Eon Joo, Park, Jan R, Kraehling, William C, Sessa

Publikováno v: The Journal of biological chemistry. 292(42)

cis-Prenyltransferases (cis-PTs) constitute a large family of enzymes conserved during evolution and present in all domains of life. In eukaryotes and archaea, cis-PT is the first enzyme committed to the synthesis of dolichyl phosphate, an obligate l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f79a0b4a41f787a2c4f33bd4cdb3a6c4
https://pubmed.ncbi.nlm.nih.gov/28842490

The Missing Electrostatic Interactions Between DNA Substrate and Sulfolobus solfataricus DNA Photolyase: What is the Role of Charged Amino Acids in Thermophilic DNA Binding Proteins?

Autor: Robert J. Stanley, Antonia Olejnikova, Ban H. Edani, Yvonne M. Gindt, Ariana N. Roberts, Sudipto Munshi

Publikováno v: J Phys Chem B

DNA photolyase can be used to study how a protein with its required cofactor has adapted over a large temperature range. The enzymatic activity and thermodynamics of substrate binding for protein from Sulfolobus solfataricus were directly compared to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb405487de2151ac7d5495dd20ee4dc
https://europepmc.org/articles/PMC7301758/