Výsledky vyhledávání - "Gina Bottger"

Recognition of peroxisomal targeting signal type 1 by the import receptor Pex5p

Autor: Gina Bottger, Phil Barnett, André Klein, Daphne Konings, Henk F. Tabak, Ben Distel

Publikováno v: Journal of biological chemistry, 276(18), 15034-15041. American Society for Biochemistry and Molecular Biology Inc.

We have studied how Pex5p recognizes peroxisomal targeting signal type 1 (PTS1)-containing proteins. A randomly mutagenized pex5 library was screened in a two-hybrid setup for mutations that disrupted the interaction with the PTS1 protein Mdh3p or fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9e3fe21f5801cde22c1bcbb701a8ca8
https://doi.org/10.1074/jbc.m010776200

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The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction

Autor: Gina Bottger, Henk F. Tabak, André Klein, Phil Barnett, Ben Distel

Publikováno v: EMBO journal, 19(23), 6382-6391. Wiley-Blackwell

Src homology 3 (SH3) domains are small non-catalytic protein modules capable of mediating protein-protein interactions by binding to proline-X-X-proline (P-X-X-P) motifs. Here we demonstrate that the SH3 domain of the integral peroxisomal membrane pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d59d125f682b8bd824e2cf525ead9cb7
https://doi.org/10.1093/emboj/19.23.6382

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Development of an enzyme-linked immunosorbent assay method to detect mustard protein in mustard seed oil

Autor: Gina Bottger, R.A.A. Vlooswijk, Stef J. Koppelman, Gert van Duijn, Jacco Dekker, Hans van Bergen, Peter van der Schaft

Publikováno v: Journal of Food Protection, 1, 70, 179-183

An enzyme-linked immunosorbent assay for the detection of mustard protein was developed. The assay is based on a polyclonal antiserum directed against a mixture of mustard proteins raised in rabbits. The assay has a detection limit of 1.5 ppm (millig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16ce81b4078cc8b261c58a8dbdda990a
https://pubmed.ncbi.nlm.nih.gov/17265878

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Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxisomes that is dependent on Pex5p

Autor: Gina Bottger, Marlene van den Berg, Henk F. Tabak, André Klein, Ben Distel

Publikováno v: Journal of biological chemistry, 277(28), 25011-25019. American Society for Biochemistry and Molecular Biology Inc.

The peroxisomal protein acyl-CoA oxidase (Pox1p) of Saccharomyces cerevisiae lacks either of the two well characterized peroxisomal targeting sequences known as PTS1 and PTS2. Here we demonstrate that peroxisomal import of Pox1p is nevertheless depen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3098d49644640d91e56598120ad50a77
https://pubmed.ncbi.nlm.nih.gov/11967269

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Saccharomyces cerevisiae PTS1 Receptor Pex5p Interacts with the SH3 Domain of the Peroxisomal Membrane Protein Pex13p in an Unconventional, Non-PXXP–related Manner

Autor: Phil Barnett, Gina Bottger, Henk F. Tabak, Ben Distel, Astrid Kragt, André Klein

Publikováno v: Molecular biology of the cell, 11(11), 3963-3976. American Society for Cell Biology

A number of peroxisome-associated proteins have been described that are involved in the import of proteins into peroxisomes, among which is the receptor for peroxisomal targeting signal 1 (PTS1) proteins Pex5p, the integral membrane protein Pex13p, w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cace3f35b4b00f6bbf36629b05f6975
https://europepmc.org/articles/PMC15050/

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Rab4 and Rab7 define distinct nonoverlapping endosomal compartments

Autor: Bas Nagelkerken, Gina Bottger, Peter van der Sluijs

Publikováno v: The Journal of biological chemistry. 271(46)

Several Rab GTPases have been localized to distinct compartments of the endocytic pathway. Rab4 is associated with early endosomes and recycling vesicles and regulates membrane recycling from early endosomes. Rab7 is localized to late endosomes and i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::434ee3573668b0ecdebbc02c4025069e
https://pubmed.ncbi.nlm.nih.gov/8910576

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