Výsledky vyhledávání - "Carita Oinonen"

Effects of metal extraction liquors from electric vehicle battery materials production on iron and sulfur oxidation by heap bioleaching microorganisms

Autor: Linda Määttä, Réka Hajdu-Rahkama, Carita Oinonen, Jaakko A. Puhakka

This study reports the effects of metal extraction liquors that are used for production of electric vehicle batteries on biological iron and sulfur oxidation. These liquors include ammonium sulfate and organic solvent constituents, and thus are poten

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e1493ee3a11ff8fb858b2b80840f773
https://trepo.tuni.fi/handle/10024/138460

Zobrazit plný text záznamu

Autoproteolytic activation of human aspartylglucosaminidase

Autor: Anu Jalanko, Leena Peltonen, Carita Oinonen, Jani Saarela, Juha Rouvinen

Publikováno v: University of Helsinki

Aspartylglucosaminidase (AGA) belongs to the N-terminal nucleophile (Ntn) hydrolase superfamily characterized by an N-terminal nucleophile as the catalytic residue. Three-dimensional structures of the Ntn hydrolases reveal a common folding pattern an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeb883704c54204ba748a5b12c312fc2
https://doi.org/10.1042/bj20031496

Zobrazit plný text záznamu

Characterization of DNA Complexes Formed by the Nuclear Receptor Constitutive Androstane Receptor

Autor: Christian Frank, Manuel Macias Gonzalez, Thomas W. Dunlop, Carsten Carlberg, Carita Oinonen

Publikováno v: Journal of Biological Chemistry. 278:43299-43310

The nuclear receptor constitutive androstane receptor (CAR) acts as a xenobiotic sensor and regulates the expression of enzymes, such as several cytochromes P450s and the UDP-glucuronosyltransferase (UGT) type 1A1. CAR binds as a heterodimer with the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c6dddddce86178a13a8655d838351a7
https://doi.org/10.1074/jbc.m305186200

Zobrazit plný text záznamu

Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations

Autor: Jani Saarela, Juha Rouvinen, Carina von Schantz, Minna Laine, Leena Peltonen, Carita Oinonen, Anu Jalanko

Publikováno v: University of Helsinki

A deficiency of functional aspartylglucosaminidase (AGA) causes a lysosomal storage disease, aspartylglucosaminuria (AGU). The recessively inherited disease is enriched in the Finnish population, where 98% of AGU alleles contain one founder mutation,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe93eb519c73933983056008ce634787
https://doi.org/10.1093/hmg/10.9.983

Zobrazit plný text záznamu

Structural comparison of Ntn-hydrolases

Autor: Carita Oinonen, Juha Rouvinen

Publikováno v: Protein Science. 9:2329-2337

The Ntn-hydrolases (N-terminal nucleophile) are a superfamily of diverse enzymes that has recently been characterized. All of the proteins in this family are activated autocatalytically; they contain an N-terminally located catalytic nucleophile, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::094cad010d18dc1a5526728410c8c744
https://doi.org/10.1110/ps.9.12.2329

Zobrazit plný text záznamu

Activation and oligomerization of aspartylglucosaminidase

Autor: Leena Peltonen, Minna Laine, Carita Oinonen, Jani Saarela, Juha Rouvinen, Anu Jalanko, Ritva Tikkanen

Publikováno v: University of Helsinki

Secretory, membrane, and lysosomal proteins undergo covalent modifications and acquire their secondary and tertiary structure in the lumen of the endoplasmic reticulum (ER). In order to pass the ER quality control system and become transported to the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7225fcb5ea1974f19ec2c4f005b6f065
https://pubmed.ncbi.nlm.nih.gov/9737998

Zobrazit plný text záznamu

Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase

Autor: Carita Oinonen, Ritva Tikkanen, Minna Peltola, Leena Peltonen, Juha Rouvinen

Lysosomal targeting of soluble lysosomal hydrolases is mediated by mannose 6-phosphate receptors, which recognize and bind mannose 6-phosphate residues in the oligosaccharide chains of proteins destined for delivery to lysosomes. This recognition mar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16bfe686ed25b0dcf643b84be51001fd
https://europepmc.org/articles/PMC1170273/

Zobrazit plný text záznamu

Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation

Autor: Leena Peltonen, Carita Oinonen, R. Rouvinen, Ritva Tikkanen, Aija Riikonen

Publikováno v: Europe PubMed Central

Aspartylglucosaminidase (AGA) is a lysosomal asparaginase that participates in the breakdown of glycoproteins by cleaving the amide bond between the asparagine and the oligosaccharide chain. Active AGA is an (alphabeta)2 heterotetramer of two non-ide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bea958125ab0e2c337d2a0bc6ec5d25
https://pubmed.ncbi.nlm.nih.gov/8670796

Zobrazit plný text záznamu

Three-dimensional structure of human lysosomal aspartylglucosaminidase

Autor: Leena Peltonen, Carita Oinonen, Juha Rouvinen, Ritva Tikkanen

Publikováno v: Nature structural biology. 2(12)

The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined. This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09c319fff8aadd8941dcd25daa3e4e83
https://pubmed.ncbi.nlm.nih.gov/8846222

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání