Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Frank van Voorst"'
Autor:
Candida Lucas, L. Neves, Rui Pedro Soares de Oliveira, Célia Ferreira, Frank van Voorst, António Martins, Anders Brandt, Morten C. Kielland-Brandt
Publikováno v:
Molecular Biology of the Cell. 16:2068-2076
Glycerol and other polyols are used as osmoprotectants by many organisms. Several yeasts and other fungi can take up glycerol by proton symport. To identify genes involved in active glycerol uptake in Saccharomyces cerevisiae we screened a deletion m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69ad1faa6d10ef6e06321dd856748b12
https://doi.org/10.1091/mbc.e04-10-0884
https://doi.org/10.1091/mbc.e04-10-0884
Autor:
Ben de Kruijff, Frank van Voorst
Publikováno v:
Biochemical Journal. 347:601-612
The architecture of cells, with various membrane-bound compartments and with the protein synthesizing machinery confined to one location, dictates that many proteins have to be transported through one or more membranes during their biogenesis. A lot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce9b8797f5ecacdfa8c91de006c715e4
https://doi.org/10.1042/bj3470601
https://doi.org/10.1042/bj3470601
Publikováno v:
Biochemistry, 37(35), 12261-12268. AMER CHEMICAL SOC
Protein translocation in Escherichia coli is mediated by the SecA ATPase bound to the SecYEG membrane protein complex. SecA translocation ATPase activity as well as protein translocation is dependent on the presence of negatively charged lipids. By u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73a1d1e13aef634088521c1a5a9f77b7
https://doi.org/10.1021/bi9809021
https://doi.org/10.1021/bi9809021
Publikováno v:
Journal of Biological Chemistry. 271:841-846
The core of the vacuolar targeting signal of yeast carboxypeptidase Y (CPY) is recognized by the receptor Vps10p and consists of four contiguous amino acid residues, Gln24-Arg-Pro-Leu27, near the amino terminus of the propeptide (Valls, L.A., Winther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8699d7e46e77a49fbe80712b42a74d1e
https://doi.org/10.1074/jbc.271.2.841
https://doi.org/10.1074/jbc.271.2.841
Autor:
Célia Ferreira, Frank van Voorst, Sónia Carina Silva, Morten C. Kielland-Brandt, Anders Brandt, Cristina Almeida Aguiar, Cândida Lucas
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Saccharomyces cerevisiae Gup1p and its homologue Gup2p, members of the superfamily of membrane-bound O-acyl transferases, were previously associated with glycerol-mediated salt-stress recovery and glycerol symporter activity. Several other phenotypes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16dd00ab36fbd928347f703eb77769fb
https://pubmed.ncbi.nlm.nih.gov/17042752
https://pubmed.ncbi.nlm.nih.gov/17042752
Autor:
Frank van Voorst, Lars Jønson, Anders Brandt, Jens Houghton-Larsen, Morten C. Kielland-Brandt
Publikováno v:
Yeast (Chichester, England). 23(5)
The Saccharomyces cerevisiae deletion collection was screened for impaired growth on glucose-based complex medium containing 6% ethanol. Forty-six mutants were found. Genes encoding proteins involved in vacuolar function, the cell integrity pathway,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67c52b5bc9f1f4ce6667e4f64071bcb6
https://pubmed.ncbi.nlm.nih.gov/16598687
https://pubmed.ncbi.nlm.nih.gov/16598687
Autor:
Ben de Kruijff, Frank van Voorst, Peter Mose Larsen, Anton I.P.M. de Kroon, Marjolein J. F. W. Janssen, Ginette E. J. Ploeger, Martin R. Larsen
Publikováno v:
Biochemistry. 41(18)
In search of mitochondrial proteins interacting with phosphatidylcholine (PC), a photolabeling approach was applied, in which photoactivatable probes were incorporated into isolated yeast mitochondria. Only a limited number of proteins were labeled u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75d3e549f2d91bd18240bd46af7f4f6b
https://pubmed.ncbi.nlm.nih.gov/11980474
https://pubmed.ncbi.nlm.nih.gov/11980474
Publikováno v:
FEBS letters. 486(1)
SecA is the central component of the protein-translocation machinery of Escherichia coli. It is able to interact with the precursor protein, the chaperone SecB, the integral membrane protein complex SecYEG, acidic phospholipids and its own mRNA. We s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11075043e54934841b328744cf484c38
https://pubmed.ncbi.nlm.nih.gov/11108843
https://pubmed.ncbi.nlm.nih.gov/11108843
Publikováno v:
Biochemical Society Transactions. 28:A397-A397
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::459a85ff8dbdcc9818e722a381e0e25d
https://doi.org/10.1042/bst028a397
https://doi.org/10.1042/bst028a397
Autor:
Clia, Ferreira, Frank, van Voorst, Antnio, Martins, Luisa, Neves, Rui, Oliveira, C, Kielland-Brandt Morten, Cndida, Lucas, Anders, Brandt
Publikováno v:
Molecular Biology of the Cell; April 2005, Vol. 16 Issue: 4 p2068-76, 9p