- Prion Interaction with the 37-kDa/67-kDa Laminin Receptor on Enterocytes as a Cellular Model for Intestinal Uptake of Prions
[作者:Kolodziejczak, D; Dias, BD; Zuber, C; Jovanovic, K; Omar, A; Beck, J; Vana, K; Mbazima, V; Richt, J; Brenig, B; Weiss, SFT,期刊:Journal of Molecular Biology, 页码:293-300 , 文章类型: Article,,卷期:2010年402-2]
- Enterocytes, a major cell population of the intestinal epithelium, represent one possible barrier to the entry of prions after oral exposure. We established a cell culture system employing enterocytes from different spec...
- Structural Similarity between the Prion Domain of HET-s and a Homologue Can Explain Amyloid Cross-Seeding in Spite of Limited Sequence Identity
[作者:Wasmer, C; Zimmer, A; Sabate, R; Soragni, A; Saupe, SJ; Ritter, C; Meier, BH,期刊:Journal of Molecular Biology, 页码:311-325 , 文章类型: Article,,卷期:2010年402-2]
- We describe a distant homologue of the fungal HET-s prion, which is found in the fungus Fusarium graminearum. The domain FgHET-s(218-289), which corresponds to the prion domain in HET-s from Podospora anserina, forms amy...
- The Escherichia coli PriA Helicase-Double-Stranded DNA Complex: Location of the Strong DNA-Binding Subsite on the Helicase Domain of the Protein and the Affinity Control by the Two Nucleotide-Binding Sites of the Enzyme
[作者:Szymanski, MR; Jezewska, MJ; Bujalowski, W,期刊:Journal of Molecular Biology, 页码:344-362 , 文章类型: Article,,卷期:2010年402-2]
- The Escherichia coli PriA helicase complex with the double-stranded DNA (dsDNA), the location of the strong DNA-binding subsite, and the effect of the nucleotide cofactors, bound to the strong and weak nucleotide-binding...
- The Unique Binding Mode of Cellulosomal CBM4 from Clostridium thermocellum Cellobiohydrolase A
[作者:Alahuhta, M; Xu, Q; Bomble, YJ; Brunecky, R; Adney, WS; Ding, SY; Himmel, ME; Lunin, VV,期刊:Journal of Molecular Biology, 页码:374-387 , 文章类型: Article,,卷期:2010年402-2]
- The crystal structure of the carbohydrate-binding module (CBM) 4 Ig fused domain from the cellulosomal cellulase cellobiohydrolase A (CbhA) of Clostridium thermocellum was solved in complex with cellobiose at 2.11 angstr...
- Cysteine-to-Serine Mutants Dramatically Reorder the Active Site of Human ABO(H) Blood Group B Glycosyltransferase without Affecting Activity: Structural Insights into Cooperative Substrate Binding
[作者:Schuman, B; Persson, M; Landry, RC; Polakowski, R; Weadge, JT; Seto, NOL; Borisova, SN; Palcic, MM; Evans, SV,期刊:Journal of Molecular Biology, 页码:399-411 , 文章类型: Article,,卷期:2010年402-2]
- A common feature in the structures of GT-A-fold-type glycosyltransferases is a mobile polypeptide loop that has been observed to participate in substrate recognition and enclose the active site upon substrate binding. Th...
- Redox Regulation of Plasmodium falciparum Ornithine delta-Aminotransferase
[作者:Jortzik, E; Fritz-Wolf, K; Sturm, N; Hipp, M; Rahlfs, S; Becker, K,期刊:Journal of Molecular Biology, 页码:445-459 , 文章类型: Article,,卷期:2010年402-2]
- Ornithine delta-aminotransferase (OAT) of the malaria parasite Plasmodium falciparum catalyzes the reversible conversion of ornithine into glutamate-5-semialdehyde and glutamate and is-in contrast to its human counterpar...
- Structure-Based Prediction of the Peptide Sequence Space Recognized by Natural and Synthetic PDZ Domains
[作者:Smith, CA; Kortemme, T,期刊:Journal of Molecular Biology, 页码:460-474 , 文章类型: Article,,卷期:2010年402-2]
- Protein-protein recognition, frequently mediated by members of large families of interaction domains, is one of the cornerstones of biological function. Here, we present a computational, structure-based method to predict...
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