Výsledky vyhledávání - "Eiwitvouwing en cellulaire factoren"

Characterization of a Torovirus Main Proteinase

Autor: Smits, S.L., Snijder, E.J., de Groot, R.J., Eiwitvouwing en cellulaire factoren, Strategic Infection Biology, Dep Scheikunde, Dep Infectieziekten Immunologie

Publikováno v: Journal of Virology, 80(8), 4157. American Society for Microbiology
Journal of Virology

Viruses of the order Nidovirales encode huge replicase polyproteins. These are processed primarily by the chymotrypsin-like main proteinases (M pro s). So far, M pro s have been studied only for corona-, arteri-, and roniviruses. Here, we report the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5f8b42a386d97df0e93fc6f275dbb0e
https://doi.org/10.1128/jvi.80.8.4157-4167.2006

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Molecular basis for regulation of the heat shock transcription factor s32 by the DnaK and DnaJ chaperones

Autor: Rodriguez, Fernanda, Arsène-Ploetze, F., Rist, W., Rüdiger, S.G.D., Schneider-Mergener, J., Mayer, M.P., Bukau, B., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Molecular Cell, 32, 347. Cell Press

Central to the transcriptional control of the Escherichia coli heat shock regulon is the stress-dependent inhibition of the s32 subunit of RNA polymerase by reversible association with the DnaK chaperone, mediated by the DnaJ cochaperone. Here we ide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::027dc5b10c834565bc640e3677f075ad
https://dspace.library.uu.nl/handle/1874/33029

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Protein folding includes oligomerization – examples from the endoplasmic reticulum and cytosol

Autor: Christis, C., Lubsen, N.H., Braakman, I., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: The FEBS journal, 275, 4700. Blackwell Publishing Ltd

A correct three-dimensional structure is a prerequisite for protein functionality, and therefore for life. Thus, it is not surprising that our cells are packed with proteins that assist protein folding, the process in which the native three-dimension

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::97d6554fb41e311d6297de8e651071ed
https://dspace.library.uu.nl/handle/1874/33033

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The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion

Autor: Sanders, R.W., van Anken, E., Nabatov, A.A., Liscaljet, I.M., Bontjer, I., Eggink, D., Melchers, M., Busser, E., Dankers, M.M., de Groot, F.., Braakman, L.J., Berkhout, B., Paxton, W.A., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Retrovirology, 5. BioMed Central

Background: The HIV-1 envelope glycoprotein gp120, which mediates viral attachment to target cells, consists for ~50% of sugar, but the role of the individual sugar chains in various aspects of gp120 folding and function is poorly understood. Here we

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::2117e36afb2c70683453bd8005c2a01e
https://dspace.library.uu.nl/handle/1874/32181

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The structure and Interactions of the proline-rich domain of ASPP2

Autor: Rotem, S., Katz, C., Benyamini, H., Lebendiker, M., Veprintsev, D., Rüdiger, S.G.D., Danieli, T., Friedler, A., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Journal of Biological Chemistry, 283(27), 18990. American Society for Biochemistry and Molecular Biology Inc.

ASPP2 is a pro-apoptotic protein that stimulates the p53-mediated apoptotic response. The C terminus of ASPP2 contains ankyrin (Ank) repeats and a SH3 domain, which mediate its interactions with numerous partner proteins such as p53,NF B, and Bcl-2.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::1140eb26d44a723698ce6bbfaf7e9a85
https://dspace.library.uu.nl/handle/1874/33026

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Peroxisomes: minted by the ER

Autor: Tabak, H.F., van der Zand, A., Braakman, L.J., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Current Opinion in Cell Biology, 20, 393. Elsevier

Peroxisomesare one ofnumerous organelles in a eukaryotic cell; they are small, single-membrane-bound vesicles involved in cellular metabolism, particularly fatty acid degradation. Transport of metabolites and co-factors in and across the membrane is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::60fda5ec3a542731d0e796f2ed4ed6ae
https://dspace.library.uu.nl/handle/1874/33030

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Molecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2

Autor: Katz, C., Benyamini, H., Rotem, S., Lebendiker, M., Danieli, T., Iosub, A., Refaely, H., Dines, M., Bronner, V., Bravman, T., Shalev, D.E., Rüdiger, S.G.D., Friedler, A., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 105(34), 12277. National Academy of Sciences

We have characterized the molecular basis of the interaction between ASPP2 and Bcl-2, which are key proteins in the apoptotic pathway. The C-terminal ankyrin repeats and SH3 domain of ASPP2 (ASPP2Ank-SH3) mediate its interactions with the antiapoptot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::e0c5e02972aa19c6f0fb71eada917188
https://dspace.library.uu.nl/handle/1874/33027

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Cargo load reduction

Autor: Braakman, I., Otsu, M., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Science, 321, 499. American Association for the Advancement of Science

In eukaryotic cells, most newly synthesized secretory proteins are first translocated into the endoplasmic reticulum (ER) and transit through organelles that constitute a secretory pathway. However, a fraction of them never reach the desired native s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::38fdf9634e6d3b83360b7985897ec4db
https://dspace.library.uu.nl/handle/1874/33034

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Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the hiv-1 envelope glycoprotein

Autor: van Anken, E., Sanders, R.W., Liscaljet, I.M., Land, A., Bontjer, I., Tillemans, S., Nabatov, A.A., Paxton, W.A., Berkhout, B., Braakman, L.J., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Molecular Biology of the Cell, 19, 4298. American Society for Cell Biology

Protein folding in the endoplasmic reticulum goes hand in hand with disulfide bond formation, and disulfide bonds are considered key structural elements for a protein’s folding and function. We used the HIV-1 Envelope glycoprotein to examine in det

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::fdcce07fa415930756a889cb892c2a21
https://dspace.library.uu.nl/handle/1874/32180

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Correlation of Levels of Folded Recombinant p53 in Escherichia coli with Thermodynamic Stability in Vitro

Autor: Mayer, S., Rüdiger, S.G.D., Ang, H.C., Joerger, A.C., Fersht, A.R., Eiwitvouwing en cellulaire factoren, Dep Scheikunde

Publikováno v: Journal of Molecular Biology, 327, 268. Academic Press Inc.

The amount of folded functional protein in a cell is controlled by a number of factors, including the relative rates of its biosynthetic and specific degradation processes, and its intrinsic thermodynamic stability. Mutationinduced loss of stability

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::375ba155eab5d9aaf046192b276d4292
https://dspace.library.uu.nl/handle/1874/26804

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