Year |
Citation |
Score |
2023 |
Gavrilov Y, Prestel A, Lindorff-Larsen K, Teilum K. Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2. Protein Science : a Publication of the Protein Society. 32: e4604. PMID 36807681 DOI: 10.1002/pro.4604 |
0.314 |
|
2022 |
Gavrilov Y, Kümmerer F, Orioli S, Prestel A, Lindorff-Larsen K, Teilum K. Double Mutant of Chymotrypsin Inhibitor 2 Stabilized through Increased Conformational Entropy. Biochemistry. PMID 35019273 DOI: 10.1021/acs.biochem.1c00749 |
0.316 |
|
2021 |
Zutz A, Hamborg L, Pedersen LE, Kassem MM, Papaleo E, Koza A, Herrgård MJ, Jensen SI, Teilum K, Lindorff-Larsen K, Nielsen AT. A dual-reporter system for investigating and optimizing protein translation and folding in E. coli. Nature Communications. 12: 6093. PMID 34667164 DOI: 10.1038/s41467-021-26337-1 |
0.313 |
|
2021 |
Lambrughi M, Maiani E, Aykac Fas B, Shaw GS, Kragelund BB, Lindorff-Larsen K, Teilum K, Invernizzi G, Papaleo E. Ubiquitin Interacting Motifs: Duality Between Structured and Disordered Motifs. Frontiers in Molecular Biosciences. 8: 676235. PMID 34262938 DOI: 10.3389/fmolb.2021.676235 |
0.356 |
|
2021 |
Teilum K, Olsen JG, Kragelund BB. On the specificity of protein-protein interactions in the context of disorder. The Biochemical Journal. 478: 2035-2050. PMID 34101805 DOI: 10.1042/BCJ20200828 |
0.304 |
|
2020 |
Hamborg L, Horsted EW, Johansson KE, Willemoës M, Lindorff-Larsen K, Teilum K. Global analysis of protein stability by temperature and chemical denaturation. Analytical Biochemistry. 113863. PMID 32738214 DOI: 10.1016/J.Ab.2020.113863 |
0.433 |
|
2020 |
Wu S, Nguyen TTTN, Moroz OV, Turkenburg JP, Nielsen JE, Wilson KS, Rand KD, Teilum K. Conformational heterogeneity of Savinase from NMR, HDX-MS and X-ray diffraction analysis. Peerj. 8: e9408. PMID 32617193 DOI: 10.7717/Peerj.9408 |
0.382 |
|
2020 |
Christensen NR, De Luca M, Lever MB, Richner M, Hansen AB, Noes-Holt G, Jensen KL, Rathje M, Jensen DB, Erlendsson S, Bartling CR, Ammendrup-Johnsen I, Pedersen SE, Schönauer M, Nissen KB, ... ... Teilum K, et al. A high-affinity, bivalent PDZ domain inhibitor complexes PICK1 to alleviate neuropathic pain. Embo Molecular Medicine. e11248. PMID 32352640 DOI: 10.15252/Emmm.201911248 |
0.339 |
|
2020 |
Pedersen CP, Dalby Nielsen L, Erlendsson S, Teilum K. The Determinants for Ligand Binding of the Domesticated Retroviral Protein Arc Biophysical Journal. 118: 195a. DOI: 10.1016/J.Bpj.2019.11.1177 |
0.417 |
|
2019 |
Nielsen LD, Pedersen CP, Erlendsson S, Teilum K. The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor. Structure (London, England : 1993). PMID 31080121 DOI: 10.1016/J.Str.2019.04.001 |
0.388 |
|
2019 |
Nielsen LD, Foged MM, Albert A, Bertelsen AB, Søltoft CL, Robinson SD, Petersen SV, Purcell AW, Olivera BM, Norton RS, Vasskog T, Safavi-Hemami H, Teilum K, Ellgaard L. The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework. The Journal of Biological Chemistry. PMID 30975904 DOI: 10.1074/Jbc.Ra119.007491 |
0.435 |
|
2019 |
Erlendsson S, Thorsen TS, Vauquelin G, Ammendrup-Johnsen I, Wirth V, Martinez KL, Teilum K, Gether U, Madsen KL. Mechanisms of PDZ domain scaffold assembly illuminated by use of supported cell membrane sheets. Elife. 8. PMID 30605082 DOI: 10.7554/Elife.39180 |
0.431 |
|
2019 |
Dalby Nielsen L, Erlendsson S, Teilum K. Transient Structural Distortion and Oligomerization of the Capsid Forming Protein Arc is Attenuated by Ligand Binding Biophysical Journal. 116: 48a. DOI: 10.1016/J.Bpj.2018.11.304 |
0.464 |
|
2018 |
Papaleo E, Camilloni C, Teilum K, Vendruscolo M, Lindorff-Larsen K. Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs. Peerj. 6: e5125. PMID 30013831 DOI: 10.7717/Peerj.5125 |
0.47 |
|
2018 |
Rasmussen KK, Falkesgaard MH, Winther M, Roed NK, Quistgaard CL, Teisen MN, Edslev SM, Petersen DL, Aljubouri A, Christensen C, Thulstrup PW, Lo Leggio L, Teilum K, Walmod PS. NCAM2 Fibronectin type-III domains form a rigid structure that binds and activates the Fibroblast Growth Factor Receptor. Scientific Reports. 8: 8957. PMID 29895898 DOI: 10.1038/S41598-018-27089-7 |
0.389 |
|
2017 |
Stiefler-Jensen D, Schwarz-Linnet T, de Lichtenberg C, Nguyen TTTN, Rand KD, Huang L, She Q, Teilum K. The extraordinary thermal stability of EstA from S. islandicus is independent of post translational modifications. Protein Science : a Publication of the Protein Society. PMID 28681456 DOI: 10.1002/Pro.3220 |
0.328 |
|
2017 |
Muschiol S, Erlendsson S, Aschtgen MS, Oliveira V, Schmieder P, de Lichtenberg C, Teilum K, Boesen T, Akbey U, Henriques-Normark B. Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae. The Journal of Biological Chemistry. PMID 28659339 DOI: 10.1074/Jbc.M117.787671 |
0.394 |
|
2017 |
Olsen JG, Teilum K, Kragelund BB. Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness. Cellular and Molecular Life Sciences : Cmls. PMID 28597296 DOI: 10.1007/S00018-017-2560-7 |
0.454 |
|
2017 |
Erlendsson S, Gotfryd K, Larsen FH, Mortensen JS, Geiger MA, van Rossum BJ, Oschkinat H, Gether U, Teilum K, Loland CJ. Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR. Elife. 6. PMID 28117663 DOI: 10.7554/Elife.19314 |
0.43 |
|
2016 |
Teilum K, Kunze MB, Erlendsson S, Kragelund BB. (S)Pinning down protein interactions by NMR. Protein Science : a Publication of the Protein Society. PMID 28019676 DOI: 10.1002/Pro.3105 |
0.43 |
|
2016 |
Højgaard C, Kofoed C, Espersen R, Johansson KE, Villa M, Willemoës M, Lindorff-Larsen K, Teilum K, Winther JR. A Soluble, Folded Protein Without Charged Amino Acid Residues. Biochemistry. PMID 27307139 DOI: 10.1021/Acs.Biochem.6B00269 |
0.447 |
|
2016 |
Erlendsson S, Gotfryd K, Larsen FH, Mortensen JS, Geiger M, Rossum Bv, Oschkinat H, Gether U, Teilum K, Loland CJ. Author response: Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR Elife. DOI: 10.7554/Elife.19314.016 |
0.352 |
|
2015 |
Teilum K, Olsen JG, Kragelund BB. Globular and disordered-the non-identical twins in protein-protein interactions. Frontiers in Molecular Biosciences. 2: 40. PMID 26217672 DOI: 10.3389/Fmolb.2015.00040 |
0.422 |
|
2015 |
Karlsen ML, Thorsen TS, Johner N, Ammendrup-Johnsen I, Erlendsson S, Tian X, Simonsen JB, Høiberg-Nielsen R, Christensen NM, Khelashvili G, Streicher W, Teilum K, Vestergaard B, Weinstein H, Gether U, et al. Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering. Structure (London, England : 1993). PMID 26073603 DOI: 10.1016/J.Str.2015.04.020 |
0.381 |
|
2014 |
Erlendsson S, Rathje M, Heidarsson PO, Poulsen FM, Madsen KL, Teilum K, Gether U. Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligands. The Journal of Biological Chemistry. 289: 25327-40. PMID 25023278 DOI: 10.1074/Jbc.M114.548743 |
0.615 |
|
2014 |
Weininger U, Brath U, Modig K, Teilum K, Akke M. Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection. Journal of Biomolecular Nmr. 59: 23-9. PMID 24706175 DOI: 10.1007/S10858-014-9826-2 |
0.415 |
|
2014 |
Jensen KS, Pedersen JT, Winther JR, Teilum K. The pKa value and accessibility of cysteine residues are key determinants for protein substrate discrimination by glutaredoxin. Biochemistry. 53: 2533-40. PMID 24673564 DOI: 10.1021/Bi4016633 |
0.43 |
|
2014 |
Iešmantavi?ius V, Dogan J, Jemth P, Teilum K, Kjaergaard M. Helical propensity in an intrinsically disordered protein accelerates ligand binding. Angewandte Chemie (International Ed. in English). 53: 1548-51. PMID 24449148 DOI: 10.1002/Anie.201307712 |
0.505 |
|
2013 |
Kukic P, Farrell D, McIntosh LP, GarcÃa-Moreno E B, Jensen KS, Toleikis Z, Teilum K, Nielsen JE. Protein dielectric constants determined from NMR chemical shift perturbations. Journal of the American Chemical Society. 135: 16968-76. PMID 24124752 DOI: 10.1021/Ja406995J |
0.384 |
|
2013 |
Kjaergaard M, Andersen L, Nielsen LD, Teilum K. A folded excited state of ligand-free nuclear coactivator binding domain (NCBD) underlies plasticity in ligand recognition. Biochemistry. 52: 1686-93. PMID 23373423 DOI: 10.1021/Bi4001062 |
0.475 |
|
2012 |
Christensen LC, Jensen NW, Vala A, Kamarauskaite J, Johansson L, Winther JR, Hofmann K, Teilum K, Ellgaard L. The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region. The Journal of Biological Chemistry. 287: 26388-99. PMID 22700979 DOI: 10.1074/Jbc.M112.346775 |
0.443 |
|
2012 |
Kjaergaard M, Poulsen FM, Teilum K. Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered. Biophysical Journal. 102: 1627-35. PMID 22500763 DOI: 10.1016/J.Bpj.2012.02.014 |
0.673 |
|
2012 |
Dagil R, Knudsen MJ, Olsen JG, O'Shea C, Franzmann M, Goffin V, Teilum K, Breinholt J, Kragelund BB. The WSXWS motif in cytokine receptors is a molecular switch involved in receptor activation: insight from structures of the prolactin receptor. Structure (London, England : 1993). 20: 270-82. PMID 22325776 DOI: 10.1016/J.Str.2011.12.010 |
0.338 |
|
2011 |
Jensen KS, Winther JR, Teilum K. Millisecond dynamics in glutaredoxin during catalytic turnover is dependent on substrate binding and absent in the resting states. Journal of the American Chemical Society. 133: 3034-42. PMID 21323311 DOI: 10.1021/Ja1096539 |
0.396 |
|
2011 |
Webb H, Tynan-Connolly BM, Lee GM, Farrell D, O'Meara F, Søndergaard CR, Teilum K, Hewage C, McIntosh LP, Nielsen JE. Remeasuring HEWL pK(a) values by NMR spectroscopy: methods, analysis, accuracy, and implications for theoretical pK(a) calculations. Proteins. 79: 685-702. PMID 21287606 DOI: 10.1002/Prot.22886 |
0.396 |
|
2011 |
Teilum K, Olsen JG, Kragelund BB. Protein stability, flexibility and function. Biochimica Et Biophysica Acta. 1814: 969-76. PMID 21094283 DOI: 10.1016/J.Bbapap.2010.11.005 |
0.457 |
|
2010 |
Kjaergaard M, Teilum K, Poulsen FM. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proceedings of the National Academy of Sciences of the United States of America. 107: 12535-40. PMID 20616042 DOI: 10.1073/Pnas.1001693107 |
0.656 |
|
2009 |
Teilum K, Smith MH, Schulz E, Christensen LC, Solomentsev G, Oliveberg M, Akke M. Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization. Proceedings of the National Academy of Sciences of the United States of America. 106: 18273-8. PMID 19828437 DOI: 10.1073/Pnas.0907387106 |
0.394 |
|
2009 |
Teilum K, Olsen JG, Kragelund BB. Functional aspects of protein flexibility. Cellular and Molecular Life Sciences : Cmls. 66: 2231-47. PMID 19308324 DOI: 10.1007/S00018-009-0014-6 |
0.45 |
|
2008 |
Teilum K, Kragelund BB, Poulsen FM. Application of Hydrogen Exchange Kinetics to Studies of Protein Folding Protein Folding Handbook. 2: 634-672. DOI: 10.1002/9783527619498.ch18 |
0.539 |
|
2007 |
Lundström P, Teilum K, Carstensen T, Bezsonova I, Wiesner S, Hansen DF, Religa TL, Akke M, Kay LE. Fractional 13C enrichment of isolated carbons using [1-13C]- or [2- 13C]-glucose facilitates the accurate measurement of dynamics at backbone Calpha and side-chain methyl positions in proteins. Journal of Biomolecular Nmr. 38: 199-212. PMID 17554498 DOI: 10.1007/S10858-007-9158-6 |
0.305 |
|
2006 |
Ghasriani H, Teilum K, Johnsson Y, Fernlund P, Drakenberg T. Solution structures of human and porcine beta-microseminoprotein. Journal of Molecular Biology. 362: 502-15. PMID 16930619 DOI: 10.1016/J.Jmb.2006.07.029 |
0.412 |
|
2006 |
Teilum K, Poulsen FM, Akke M. The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein. Proceedings of the National Academy of Sciences of the United States of America. 103: 6877-82. PMID 16641108 DOI: 10.1073/Pnas.0509100103 |
0.585 |
|
2006 |
Teilum K, Brath U, Lundström P, Akke M. Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements. Journal of the American Chemical Society. 128: 2506-7. PMID 16492013 DOI: 10.1021/Ja055660O |
0.353 |
|
2005 |
Teilum K, Hoch JC, Goffin V, Kinet S, Martial JA, Kragelund BB. Solution structure of human prolactin. Journal of Molecular Biology. 351: 810-23. PMID 16045928 DOI: 10.1016/J.Jmb.2005.06.042 |
0.369 |
|
2005 |
Teilum K, Thormann T, Caterer NR, Poulsen HI, Jensen PH, Knudsen J, Kragelund BB, Poulsen FM. Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins. 59: 80-90. PMID 15690348 DOI: 10.1002/Prot.20340 |
0.566 |
|
2005 |
Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/Ps.041205405 |
0.607 |
|
2004 |
Lindorff-Larsen K, Kristjansdottir S, Teilum K, Fieber W, Dobson CM, Poulsen FM, Vendruscolo M. Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein. Journal of the American Chemical Society. 126: 3291-9. PMID 15012160 DOI: 10.1021/Ja039250G |
0.648 |
|
2002 |
Groes M, Teilum K, Olesen K, Poulsen FM, Henriksen A. Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule from Saccharomyces carlsbergensis. Acta Crystallographica. Section D, Biological Crystallography. 58: 2135-7. PMID 12454478 DOI: 10.1107/S0907444902015494 |
0.551 |
|
2002 |
Teilum K, Kragelund BB, Poulsen FM. Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling. Journal of Molecular Biology. 324: 349-57. PMID 12441112 DOI: 10.1016/S0022-2836(02)01039-2 |
0.639 |
|
2002 |
Teilum K, Maki K, Kragelund BB, Poulsen FM, Roder H. Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proceedings of the National Academy of Sciences of the United States of America. 99: 9807-12. PMID 12096190 DOI: 10.1073/Pnas.152321499 |
0.604 |
|
2002 |
Thomsen JK, Kragelund BB, Teilum K, Knudsen J, Poulsen FM. Transient intermediary states with high and low folding probabilities in the apparent two-state folding equilibrium of ACBP at low pH. Journal of Molecular Biology. 318: 805-14. PMID 12054824 DOI: 10.1016/S0022-2836(02)00159-6 |
0.622 |
|
2001 |
Henriksen A, Mirza O, Indiani C, Teilum K, Smulevich G, Welinder KG, Gajhede M. Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions. Protein Science : a Publication of the Protein Society. 10: 108-15. PMID 11266599 DOI: 10.1110/Ps.37301 |
0.354 |
|
2000 |
Teilum K, Kragelund BB, Knudsen J, Poulsen FM. Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. Journal of Molecular Biology. 301: 1307-14. PMID 10966822 DOI: 10.1006/Jmbi.2000.4003 |
0.622 |
|
1999 |
Teilum K, Ostergaard L, Welinder KG. Disulfide bond formation and folding of plant peroxidases expressed as inclusion body protein in Escherichia coli thioredoxin reductase negative strains. Protein Expression and Purification. 15: 77-82. PMID 10024473 DOI: 10.1006/Prep.1998.0985 |
0.365 |
|
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