A novel experimental approach for the selective isolation and characterization of human RNase MRP

Autor: Merel Derksen, Vicky Mertens, Eline A. Visser, Janine Arts, Wilma Vree Egberts, Ger J. M. Pruijn

Publikováno v: RNA Biology, Vol 19, Iss 1, Pp 305-312 (2022)

RNase MRP is a ribonucleoprotein complex involved in the endoribonucleolytic cleavage of different RNAs. Mutations in the RNA component of the RNP are the cause of cartilage hair hypoplasia. Patients with cartilage hair hypoplasia are characterized b

Externí odkaz: https://doaj.org/article/1ef8102a5f35469ebbed264ceedfbd6a

Anti-Cytosolic 5'-Nucleotidase 1A Autoantibodies Are Absent in Juvenile Dermatomyositis

Autor: Wilma Vree Egberts, Eline A. Visser, Ger J. M. Pruijn, Wolfgang Schlumberger, Annet van Royen-Kerkhof, Baziel G.M. van Engelen, Lucy R. Wedderburn, Christiaan G J Saris, Judith Wienke, Anke Rietveld, Sarah L Tansley, Hui Lu

Publikováno v: Arthritis & Rheumatology, 73, 1329-1333
Arthritis & Rheumatology, 73, 7, pp. 1329-1333

Contains fulltext : 238504.pdf (Publisher’s version ) (Open Access) OBJECTIVE: To assess anti-cytosolic 5'-nucleotidase 1A (anti-cN-1A) autoantibodies in children with juvenile dermatomyositis (DM) and healthy controls, using 3 different methods of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23f84a1804e0398f69bdc523c8416902
http://hdl.handle.net/2066/238504

The small heat shock proteins, HSPB1 and HSPB5, interact differently with lipid membranes

Autor: Nelson Arispe, Ivan Bello, Ricardo Capone, Wilbert C. Boelens, Wilma Vree Egberts, Antonio De Maio, David M. Cauvi

Publikováno v: Cell stress & chaperones, vol 24, iss 5

Increasing evidence shows that heat shock proteins (hsp) escape the cytosol gaining access to the extracellular environment, acting as signaling agents. Since the majority of these proteins lack the information necessary for their export via the clas

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::968ab03279508bf97daa4518e6772ed2
https://europepmc.org/articles/PMC6717221/

The small heat-shock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio

Autor: Wilbert C. Boelens, John den Engelsman, Wilma Vree Egberts, Bram Kamps, Patricia Y. W. Dankers, Carol V. Robinson, Csaba Böde, Sandor Boros, J. Andrew Aquilina, Laura A. Lane, Justin L. P. Benesch, Wilfried W. de Jong

Publikováno v: Journal of Biological Chemistry, 393, 5
Journal of Biological Chemistry, 393
Journal of Molecular Biology, 393, 1022-32
Journal of Molecular Biology, 393, 5, pp. 1022-32
Journal of Molecular Biology, 393(5), 1022-1032. Academic Press Inc.

Contains fulltext : 81177.pdf (Publisher’s version ) (Closed access) Various mammalian small heat-shock proteins (sHSPs) can interact with one another to form large polydisperse assemblies. In muscle cells, HSPB2/MKBP (myotonic dystrophy protein ki

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbd10932e15721de0f61f76455dd1231
https://hdl.handle.net/2066/75686

Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro

Autor: Ger J. M. Pruijn, Claudia Soede-Huijbregts, Jan W. Drijfhout, Wilma Vree Egberts, Floris P. J. T. Rutjes, Reinout Raijmakers, Peter A. van Veelen, Albert J.W. Zendman, Erik R. Vossenaar, Jos M.H. Raats

Publikováno v: Journal of Molecular Biology, 367, 1118-1129
Journal of Molecular Biology, 367, 4, pp. 1118-1129

Peptidylarginine deiminase (PAD) enzymes catalyze the conversion of arginine residues in proteins to citrulline residues. Citrulline is a non-standard amino acid that is not incorporated in proteins during translation, but can be generated post-trans

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d742744a9ac397555dca81219c0d60b9
http://hdl.handle.net/2066/34477