Výsledky vyhledávání - "D M, van Aalten"

Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution

Autor: A M, Haapalainen, D M, van Aalten, G, Meriläinen, J E, Jalonen, P, Pirilä, R K, Wierenga, J K, Hiltunen, T, Glumoff

Publikováno v: Journal of molecular biology. 313(5)

beta-Oxidation of amino acyl coenzyme A (acyl-CoA) species in mammalian peroxisomes can occur via either multifunctional enzyme type 1 (MFE-1) or type 2 (MFE-2), both of which catalyze the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::45ee2838072de259d23407112f3d5d24
https://pubmed.ncbi.nlm.nih.gov/11700068

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Crystal structure of the phosphatidylinositol 3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): molecular basis of lipid specificity

Autor: C C, Thomas, S, Dowler, M, Deak, D R, Alessi, D M, van Aalten

Publikováno v: The Biochemical journal. 358(Pt 2)

Phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] and its immediate breakdown product PtdIns(3,4)P(2) function as second messengers in growth factor- and insulin-induced signalling pathways. One of the ways that these 3-phosphoinositides a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5ce0de076793c97ccf40f8d9df213506
https://pubmed.ncbi.nlm.nih.gov/11513726

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The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase

Autor: A M, Mursula, D M, van Aalten, J K, Hiltunen, R K, Wierenga

Publikováno v: Journal of molecular biology. 309(4)

The active-site geometry of the first crystal structure of a Delta(3)-Delta(2)-enoyl-coenzyme A (CoA) isomerase (the peroxisomal enzyme from the yeast Saccharomyces cerevisiae) shows that only one catalytic base, Glu158, is involved in shuttling the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0e6a458bad6b3b6ebb230c4eaa021068
https://pubmed.ncbi.nlm.nih.gov/11399063

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Functional concerted motions in the bovine serum retinol-binding protein

Autor: P L, Chau, D M, van Aalten, R P, Bywater, J B, Findlay

Publikováno v: Journal of computer-aided molecular design. 13(1)

The large concerted motions in the apo/holo bovine serum retinol-binding protein were studied using molecular dynamics simulation and 'essential dynamics' analysis. Initially, concerted motions were calculated from conformational differences between

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::46ed10f79896530183da69c0485e43b6
https://pubmed.ncbi.nlm.nih.gov/10087496

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Domain motions in bacteriophage T4 lysozyme: a comparison between molecular dynamics and crystallographic data

Autor: B L, de Groot, S, Hayward, D M, van Aalten, A, Amadei, H J, Berendsen

Publikováno v: Proteins. 31(2)

A comparison of a series of extended molecular dynamics (MD) simulations of bacteriophage T4 lysozyme in solvent with X-ray data is presented. Essential dynamics analyses were used to derive collective fluctuations from both the simulated trajectorie

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::33b4898c4f10a1a69496059272936d9e
https://pubmed.ncbi.nlm.nih.gov/9593186

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Prediction of protein conformational freedom from distance constraints

Autor: B L, de Groot, D M, van Aalten, R M, Scheek, A, Amadei, G, Vriend, H J, Berendsen

Publikováno v: Proteins. 29(2)

A method is presented that generates random protein structures that fulfil a set of upper and lower interatomic distance limits. These limits depend on distances measured in experimental structures and the strength of the interatomic interaction. Str

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8a715301e026c35cc8aa6dd3259d6d32
https://pubmed.ncbi.nlm.nih.gov/9329088

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