M. Teresa Pisabarro - Publications

Affiliations: 
Technische Universität Dresden, Dresden, Sachsen, Germany 

15 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2021 Balamurugan K, Pisabarro MT. Stabilizing Role of Water Solvation on Anion-π Interactions in Proteins. Acs Omega. 6: 25350-25360. PMID 34632193 DOI: 10.1021/acsomega.1c03264  0.309
2016 Babik S, Samsonov SA, Pisabarro MT. Computational drill down on FGF1-heparin interactions through methodological evaluation. Glycoconjugate Journal. 34: 427-440. PMID 27858202 DOI: 10.1007/s10719-016-9745-4  0.308
2016 Samsonov SA, Pisabarro MT. Computational analysis of interactions in structurally available protein-glycosaminoglycan complexes. Glycobiology. 26: 850-861. PMID 27496767 DOI: 10.1093/glycob/cww055  0.353
2015 Wodtke R, Ruiz-Gómez G, Kuchar M, Pisabarro MT, Novotná P, Urbanová M, Steinbach J, Pietzsch J, Löser R. Cyclopeptides containing the DEKS motif as conformationally restricted collagen telopeptide analogues: synthesis and conformational analysis. Organic & Biomolecular Chemistry. 13: 1878-96. PMID 25503999 DOI: 10.1039/c4ob02348j  0.309
2013 Samsonov SA, Pisabarro MT. Importance of IdoA and IdoA(2S) ring conformations in computational studies of glycosaminoglycan-protein interactions. Carbohydrate Research. 381: 133-7. PMID 24096273 DOI: 10.1016/j.carres.2013.09.005  0.301
2011 Teyra J, Samsonov SA, Schreiber S, Pisabarro MT. SCOWLP update: 3D classification of protein-protein, -peptide, -saccharide and -nucleic acid interactions, and structure-based binding inferences across folds. Bmc Bioinformatics. 12: 398. PMID 21992011 DOI: 10.1186/1471-2105-12-398  0.412
2011 Samsonov SA, Teyra J, Pisabarro MT. Docking glycosaminoglycans to proteins: analysis of solvent inclusion. Journal of Computer-Aided Molecular Design. 25: 477-89. PMID 21597992 DOI: 10.1007/s10822-011-9433-1  0.352
2009 Samsonov SA, Salwiczek M, Anders G, Koksch B, Pisabarro MT. Fluorine in protein environments: a QM and MD study. The Journal of Physical Chemistry. B. 113: 16400-8. PMID 19947631 DOI: 10.1021/Jp906402B  0.371
2009 Salwiczek M, Samsonov S, Vagt T, Nyakatura E, Fleige E, Numata J, Cölfen H, Pisabarro MT, Koksch B. Position-dependent effects of fluorinated amino acids on the hydrophobic core formation of a heterodimeric coiled coil. Chemistry (Weinheim An Der Bergstrasse, Germany). 15: 7628-36. PMID 19579235 DOI: 10.1002/Chem.200802136  0.343
2008 Baldauf C, Pisabarro MT. Stable hairpins with beta-peptides: route to tackle protein-protein interactions. The Journal of Physical Chemistry. B. 112: 7581-91. PMID 18512885 DOI: 10.1021/Jp076838R  0.409
2008 Samsonov S, Teyra J, Pisabarro MT. A molecular dynamics approach to study the importance of solvent in protein interactions. Proteins. 73: 515-25. PMID 18452208 DOI: 10.1002/prot.22076  0.379
2008 Teyra J, Paszkowski-Rogacz M, Anders G, Pisabarro MT. SCOWLP classification: structural comparison and analysis of protein binding regions. Bmc Bioinformatics. 9: 9. PMID 18182098 DOI: 10.1186/1471-2105-9-9  0.337
2007 Scheike JA, Baldauf C, Spengler J, Albericio F, Pisabarro MT, Koksch B. Amide-to-ester substitution in coiled coils: the effect of removing hydrogen bonds on protein structure. Angewandte Chemie (International Ed. in English). 46: 7766-9. PMID 17876795 DOI: 10.1002/Anie.200702218  0.397
2006 Teyra J, Doms A, Schroeder M, Pisabarro MT. SCOWLP: a web-based database for detailed characterization and visualization of protein interfaces. Bmc Bioinformatics. 7: 104. PMID 16512892 DOI: 10.1186/1471-2105-7-104  0.336
2004 Cobos ES, Pisabarro MT, Vega MC, Lacroix E, Serrano L, Ruiz-Sanz J, Martinez JC. A miniprotein scaffold used to assemble the polyproline II binding epitope recognized by SH3 domains. Journal of Molecular Biology. 342: 355-65. PMID 15313630 DOI: 10.1016/J.Jmb.2004.06.078  0.368
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