Year |
Citation |
Score |
2022 |
Dreydoppel M, Balbach J, Weininger U. Monitoring protein unfolding transitions by NMR-spectroscopy. Journal of Biomolecular Nmr. PMID 34984658 DOI: 10.1007/s10858-021-00389-3 |
0.329 |
|
2021 |
Gruber T, Lewitzky M, Machner L, Weininger U, Feller SM, Balbach J. Macromolecular crowding induces a binding competent transient structure in intrinsically disordered Gab1. Journal of Molecular Biology. 167407. PMID 34929201 DOI: 10.1016/j.jmb.2021.167407 |
0.314 |
|
2021 |
Kumar A, Balbach J. Folding and Stability of Ankyrin Repeats Control Biological Protein Function. Biomolecules. 11. PMID 34198779 DOI: 10.3390/biom11060840 |
0.32 |
|
2020 |
Auerswald A, Gruber T, Balbach J, Meister A. Lipid-Dependent Interaction of Human N-BAR Domain Proteins with Sarcolemma Mono- and Bilayers. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 32649209 DOI: 10.1021/Acs.Langmuir.0C00649 |
0.365 |
|
2020 |
Vasco AV, Moya CG, Gröger S, Brandt W, Balbach J, Pérez CS, Wessjohann LA, Rivera DG. Insights into the secondary structures of lactam N-substituted stapled peptides. Organic & Biomolecular Chemistry. PMID 32400808 DOI: 10.1039/D0Ob00767F |
0.355 |
|
2019 |
Evgrafova Z, Rothemund S, Voigt B, Hause G, Balbach J, Binder WH. Synthesis and Aggregation of Polymer-Amyloid β Conjugates. Macromolecular Rapid Communications. e1900378. PMID 31631446 DOI: 10.1002/Marc.201900378 |
0.312 |
|
2019 |
Kumar A, Kuhn LT, Balbach J. In-Cell NMR: Analysis of Protein⁻Small Molecule Interactions, Metabolic Processes, and Protein Phosphorylation. International Journal of Molecular Sciences. 20. PMID 30658393 DOI: 10.3390/Ijms20020378 |
0.301 |
|
2019 |
Wägele J, De Sio S, Voigt B, Balbach J, Ott M. How Fluorescent Tags Modify Oligomer Size Distributions of the Alzheimer Peptide. Biophysical Journal. 116: 227-238. PMID 30638607 DOI: 10.1016/J.Bpj.2018.12.010 |
0.325 |
|
2019 |
Klamt A, Nagarathinam K, Tanabe M, Kumar A, Balbach J. Hyperbolic Pressure-Temperature Phase Diagram of the Zinc-Finger Protein apoKti11 Detected by NMR Spectroscopy. The Journal of Physical Chemistry. B. PMID 30608169 DOI: 10.1021/Acs.Jpcb.8B11019 |
0.365 |
|
2018 |
Vasco AV, Mendez Y, Porzel A, Balbach J, Wessjohann LA, Rivera DG. A Multicomponent Stapling Approach to Exocyclic Functionalized Helical Pep-tides: Adding Lipids, Sugar, PEGs, Labels and Handles to the Lactam Bridge. Bioconjugate Chemistry. PMID 30575393 DOI: 10.1021/Acs.Bioconjchem.8B00906 |
0.354 |
|
2018 |
Dreydoppel M, Becker P, Raum HN, Gröger S, Balbach J, Weininger U. Equilibrium and Kinetic Unfolding of GB1: Stabilization of the Native State by Pressure. The Journal of Physical Chemistry. B. PMID 30185038 DOI: 10.1021/Acs.Jpcb.8B06888 |
0.349 |
|
2018 |
Camilles M, Link S, Balbach J, Saalwächter K, Krushelnitsky A. Quantitative NMR study of heat-induced aggregation of eye-lens crystallin proteins under crowding conditions. Biochimica Et Biophysica Acta. PMID 30071343 DOI: 10.1016/J.Bbapap.2018.07.007 |
0.357 |
|
2017 |
Geitner AJ, Weininger U, Paulsen H, Balbach J, Kovermann M. Structure based insights into dynamics and function of two domain SlpA from Escherichia coli. Biochemistry. PMID 29155566 DOI: 10.1021/Acs.Biochem.7B00786 |
0.453 |
|
2016 |
Roos M, Ott M, Hofmann M, Link S, Roessler EA, Balbach J, Krushelnitsky AG, Saalwaechter K. Coupling and decoupling of rotational and translational diffusion of proteins under crowding conditions. Journal of the American Chemical Society. PMID 27434647 DOI: 10.1021/Jacs.6B06615 |
0.344 |
|
2016 |
Rothe M, Gruber T, Gröger S, Balbach J, Saalwächter K, Roos M. Transient binding accounts for apparent violation of the generalized Stokes-Einstein relation in crowded protein solutions. Physical Chemistry Chemical Physics : Pccp. 18: 18006-14. PMID 27326536 DOI: 10.1039/C6Cp01056C |
0.365 |
|
2016 |
Adler J, Baumann M, Voigt B, Scheidt H, Bhowmik D, Häupl T, Abel B, Madhu PK, Balbach J, Maiti S, Huster D. A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid beta (1-40). Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 27224205 DOI: 10.1002/Cphc.201600413 |
0.354 |
|
2016 |
Daum B, Auerswald A, Gruber T, Hause G, Balbach J, Kühlbrandt W, Meister A. Supramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane. Journal of Structural Biology. PMID 27016283 DOI: 10.1016/J.Jsb.2016.03.017 |
0.326 |
|
2016 |
Villmow M, Baumann M, Malesevic M, Sachs R, Hause G, Fändrich M, Balbach J, Schiene-Fischer C. Inhibition of Aβ(1-40) Fibril Formation by Cyclophilins. The Biochemical Journal. PMID 26994210 DOI: 10.1042/Bcj20160098 |
0.34 |
|
2016 |
Wulff M, Baumann M, Thümmler A, Yadav JK, Heinrich L, Knüpfer U, Schlenzig D, Schierhorn A, Rahfeld JU, Horn U, Balbach J, Demuth HU, Fändrich M. Enhanced Fibril Fragmentation of N-Terminally Truncated and Pyroglutamyl-Modified Aβ Peptides. Angewandte Chemie (International Ed. in English). PMID 26970534 DOI: 10.1002/Anie.201511099 |
0.34 |
|
2016 |
Kumar A, Baumann M, Balbach J. Small Molecule Inhibited Parathyroid Hormone Mediated cAMP Response by N-Terminal Peptide Binding. Scientific Reports. 6: 22533. PMID 26932583 DOI: 10.1038/Srep22533 |
0.35 |
|
2016 |
Wulff M, Baumann M, Thümmler A, Yadav JK, Heinrich L, Knüpfer U, Schlenzig D, Schierhorn A, Rahfeld J, Horn U, Balbach J, Demuth H, Fändrich M. Verstärkte Fibrillen-Fragmentierung N-terminal verkürzter, Pyroglutamat-modifizierter Aβ-Peptide Angewandte Chemie. 128: 5165-5168. DOI: 10.1002/Ange.201511099 |
0.309 |
|
2015 |
Roos M, Hofmann M, Link S, Ott M, Balbach J, Rössler E, Saalwächter K, Krushelnitsky A. The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range. Journal of Biomolecular Nmr. 63: 403-15. PMID 26582718 DOI: 10.1007/S10858-015-0001-1 |
0.322 |
|
2015 |
Gruber T, Balbach J. Protein Folding Mechanism of the Dimeric AmphiphysinII/Bin1 N-BAR Domain. Plos One. 10: e0136922. PMID 26368922 DOI: 10.1371/Journal.Pone.0136922 |
0.451 |
|
2015 |
Zimmermann S, Pfennig S, Neumann P, Yonus H, Weininger U, Kovermann M, Balbach J, Stubbs MT. High-resolution structures of the D-alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo- and holo-forms. Febs Letters. 589: 2283-9. PMID 26193422 DOI: 10.1016/J.Febslet.2015.07.008 |
0.431 |
|
2015 |
Dinesh DC, Kovermann M, Gopalswamy M, Hellmuth A, Calderón Villalobos LI, Lilie H, Balbach J, Abel S. Solution structure of the PsIAA4 oligomerization domain reveals interaction modes for transcription factors in early auxin response. Proceedings of the National Academy of Sciences of the United States of America. 112: 6230-5. PMID 25918389 DOI: 10.1073/Pnas.1424077112 |
0.439 |
|
2015 |
Roos M, Link S, Balbach J, Krushelnitsky A, Saalwächter K. NMR-detected brownian dynamics of αB-crystallin over a wide range of concentrations. Biophysical Journal. 108: 98-106. PMID 25564856 DOI: 10.1016/J.Bpj.2014.11.1858 |
0.341 |
|
2015 |
Gopalswamy M, Kumar A, Adler J, Baumann M, Henze M, Kumar ST, Fändrich M, Scheidt HA, Huster D, Balbach J. Structural characterization of amyloid fibrils from the human parathyroid hormone. Biochimica Et Biophysica Acta. 1854: 249-57. PMID 25554227 DOI: 10.1016/J.Bbapap.2014.12.020 |
0.369 |
|
2015 |
Glatt S, Zabel R, Vonkova I, Kumar A, Netz DJ, Pierik AJ, Rybin V, Lill R, Gavin AC, Balbach J, Breunig KD, Müller CW. heterodimer and its double role in modificationsStructure of the Kti11/Kti13 of tRNA and eukaryotic elongation factor 2. Structure (London, England : 1993). 23: 149-60. PMID 25543256 DOI: 10.1016/J.Str.2014.11.008 |
0.385 |
|
2015 |
Kumar A, Balbach J. Real-time protein NMR spectroscopy and investigation of assisted protein folding. Biochimica Et Biophysica Acta. 1850: 1965-72. PMID 25497212 DOI: 10.1016/J.Bbagen.2014.12.003 |
0.448 |
|
2014 |
Thieme T, Patzschke R, Job F, Liebold J, Seemann P, Lilie H, Balbach J, Schwarz E. Biophysical and structural characterization of a folded core domain within the proregion of growth and differentiation factor-5. The Febs Journal. 281: 4866-77. PMID 25174448 DOI: 10.1111/Febs.13025 |
0.354 |
|
2014 |
Kumar A, Gopalswamy M, Wishart C, Henze M, Eschen-Lippold L, Donnelly D, Balbach J. N-terminal phosphorylation of parathyroid hormone (PTH) abolishes its receptor activity. Acs Chemical Biology. 9: 2465-70. PMID 25158085 DOI: 10.1021/Cb5004515 |
0.306 |
|
2014 |
Löw C, Quistgaard EM, Kovermann M, Anandapadamanaban M, Balbach J, Nordlund P. Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A Biological Chemistry. 395: 881-889. PMID 25003389 DOI: 10.1515/Hsz-2014-0106 |
0.335 |
|
2013 |
Hacke M, Gruber T, Schulenburg C, Balbach J, Arnold U. Consequences of proline-to-alanine substitutions for the stability and refolding of onconase. The Febs Journal. 280: 4454-62. PMID 23796075 DOI: 10.1111/Febs.12406 |
0.414 |
|
2013 |
Kovermann M, Schmid FX, Balbach J. Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD Biological Chemistry. 394: 965-975. PMID 23585180 DOI: 10.1515/Hsz-2013-0137 |
0.595 |
|
2013 |
Hoffmann-Thoms S, Weininger U, Eckert B, Jakob RP, Koch JR, Balbach J, Schmid FX. Initiation of phage infection by partial unfolding and prolyl isomerization Journal of Biological Chemistry. 288: 12979-12991. PMID 23486474 DOI: 10.1074/Jbc.M112.442525 |
0.622 |
|
2013 |
Krug U, Patzschke R, Zebisch M, Balbach J, Sträter N. Contribution of the two domains of E. coli 5′-nucleotidase to substrate specificity and catalysis Febs Letters. 587: 460-466. PMID 23333297 DOI: 10.1016/J.Febslet.2013.01.010 |
0.398 |
|
2013 |
Kovermann M, Balbach J. Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein Biophysical Chemistry. 171: 16-23. PMID 23268194 DOI: 10.1016/J.Bpc.2012.11.003 |
0.416 |
|
2013 |
Kovermann M, Weininger U, Balbach J. NMR solution structure of the two domain PPIase SlpA from Escherichia coli Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2M2A/Pdb |
0.364 |
|
2013 |
Kovermann M, Chandrasekaran DD, Gopalswamy M, Abel S, Balbach J. Solution structure of the dimerization domain of Aux/IAA transcription factor Ps-IAA4 from pea (Pisum sativum) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr18870 |
0.322 |
|
2012 |
Morgado I, Wieligmann K, Bereza M, Rönicke R, Meinhardt K, Annamalai K, Baumann M, Wacker J, Hortschansky P, Malešević M, Parthier C, Mawrin C, Schiene-Fischer C, Reymann KG, Stubbs MT, ... Balbach J, et al. Molecular basis of β-amyloid oligomer recognition with a conformational antibody fragment Proceedings of the National Academy of Sciences of the United States of America. 109: 12503-12508. PMID 22814377 DOI: 10.1073/Pnas.1206433109 |
0.332 |
|
2012 |
Jakob RP, Geitner AJ, Weininger U, Balbach J, Dobbek H, Schmid FX. Structural and energetic basis of infection by the filamentous bacteriophage IKe Molecular Microbiology. 84: 1124-1138. PMID 22591114 DOI: 10.1111/J.1365-2958.2012.08079.X |
0.591 |
|
2012 |
Hoffmann A, Kovermann M, Lilie H, Fiedler M, Balbach J, Rudolph R, Pfeifer S. New binding mode to TNF-alpha revealed by ubiquitin-based artificial binding protein Plos One. 7. PMID 22363609 DOI: 10.1371/Journal.Pone.0031298 |
0.352 |
|
2012 |
Kaluarachchi H, Altenstein M, Sugumar SR, Balbach J, Zamble DB, Haupt C. Nickel binding and [NiFe]-hydrogenase maturation by the metallochaperone SlyD with a single metal-binding site in Escherichia coli Journal of Molecular Biology. 417: 28-35. PMID 22310044 DOI: 10.1016/J.Jmb.2012.01.037 |
0.392 |
|
2012 |
Sachs R, Max KE, Heinemann U, Balbach J. RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution. Rna (New York, N.Y.). 18: 65-76. PMID 22128343 DOI: 10.1261/Rna.02809212 |
0.346 |
|
2011 |
Klepsch MM, Kovermann M, Löw C, Balbach J, Permentier HP, Fusetti F, de Gier JW, Slotboom DJ, Berntsson RP. Escherichia coli peptide binding protein OppA has a preference for positively charged peptides. Journal of Molecular Biology. 414: 75-85. PMID 21983341 DOI: 10.1016/J.Jmb.2011.09.043 |
0.355 |
|
2011 |
Casares-Atienza S, Weininger U, Cámara-Artigas A, Balbach J, Garcia-Mira MM. Three-state thermal unfolding of onconase Biophysical Chemistry. 159: 267-274. PMID 21840114 DOI: 10.1016/J.Bpc.2011.07.005 |
0.308 |
|
2011 |
Haupt C, Weininger U, Kovermann M, Balbach J. Local and coupled thermodynamic stability of the two-domain and bifunctional enzyme SlyD from Escherichia coli Biochemistry. 50: 7321-7329. PMID 21770389 DOI: 10.1021/Bi2000627 |
0.443 |
|
2011 |
Haupt C, Patzschke R, Weininger U, Gröger S, Kovermann M, Balbach J. Transient enzyme - Substrate recognition monitored by real-time NMR Journal of the American Chemical Society. 133: 11154-11162. PMID 21661729 DOI: 10.1021/Ja2010048 |
0.482 |
|
2011 |
Kahra D, Kovermann M, Löw C, Hirschfeld V, Haupt C, Balbach J, Hübner CG. Conformational plasticity and dynamics in the generic protein folding catalyst SlyD unraveled by single-molecule FRET Journal of Molecular Biology. 411: 781-790. PMID 21596048 DOI: 10.1016/J.Jmb.2011.05.002 |
0.418 |
|
2011 |
Garvey M, Tepper K, Haupt C, Knüpfer U, Klement K, Meinhardt J, Horn U, Balbach J, Fändrich M. Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer's Aβ peptide Biochemical and Biophysical Research Communications. 409: 385-388. PMID 21575606 DOI: 10.1016/J.Bbrc.2011.04.141 |
0.304 |
|
2011 |
Kovermann M, Zierold R, Haupt C, Löw C, Balbach J. NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD Biochimica Et Biophysica Acta - Proteins and Proteomics. 1814: 873-881. PMID 21466862 DOI: 10.1016/J.Bbapap.2011.03.016 |
0.402 |
|
2011 |
Drechsler N, Fröbel J, Jahreis G, Gopalswamy M, Balbach J, Bosse-Doenecke E, Rudolph R. Binding specificity of the ectodomain of the parathyroid hormone receptor Biophysical Chemistry. 154: 66-72. PMID 21339037 DOI: 10.1016/J.Bpc.2011.01.002 |
0.31 |
|
2011 |
Theisgen S, Thomas L, Schröder T, Lange C, Kovermann M, Balbach J, Huster D. The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2 European Biophysics Journal. 40: 565-576. PMID 21327964 DOI: 10.1007/S00249-011-0680-9 |
0.36 |
|
2011 |
Lorenz SH, Jakob RP, Weininger U, Balbach J, Dobbek H, Schmid FX. The filamentous phages fd and IF1 use different mechanisms to infect escherichia coli Journal of Molecular Biology. 405: 989-1003. PMID 21110981 DOI: 10.1016/J.Jmb.2010.11.030 |
0.573 |
|
2011 |
Lilie H, Bär D, Kettner K, Weininger U, Balbach J, Naumann M, Müller EC, Otto A, Gast K, Golbik R, Kriegel T. Yeast hexokinase isoenzyme ScHxk2: stability of a two-domain protein with discontinuous domains. Protein Engineering, Design & Selection : Peds. 24: 79-87. PMID 21075772 DOI: 10.1093/Protein/Gzq098 |
0.469 |
|
2010 |
Dahse K, Garvey M, Kovermann M, Vogel A, Balbach J, Fändrich M, Fahr A. DHPC Strongly Affects the Structure and Oligomerization Propensity of Alzheimer's Aβ(1-40) Peptide Journal of Molecular Biology. 403: 643-659. PMID 20851128 DOI: 10.1016/J.Jmb.2010.09.021 |
0.331 |
|
2010 |
Jakob RP, Zierer BK, Weininger U, Hofmann SD, Lorenz SH, Balbach J, Dobbek H, Schmid FX. Elimination of a Cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding Journal of Molecular Biology. 399: 331-346. PMID 20394751 DOI: 10.1016/J.Jmb.2010.04.007 |
0.596 |
|
2010 |
Schulenburg C, Weininger U, Neumann P, Meiselbach H, Stubbs MT, Sticht H, Balbach J, Ulbrich-Hofmann R, Arnold U. Impact of the C-terminal disulfide bond on the folding and stability of onconase Chembiochem. 11: 978-986. PMID 20349493 DOI: 10.1002/Cbic.200900773 |
0.431 |
|
2010 |
Löw C, Neumann P, Tidow H, Weininger U, Haupt C, Friedrich-Epler B, Scholz C, Stubbs MT, Balbach J. Crystal structure determination and functional characterization of the metallochaperone SlyD from thermus thermophilus Journal of Molecular Biology. 398: 375-390. PMID 20230833 DOI: 10.1016/J.Jmb.2010.03.014 |
0.461 |
|
2010 |
Weininger U, Jakob RP, Kovermann M, Balbach J, Schmid FX. The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity Protein Science. 19: 6-18. PMID 19866485 DOI: 10.1002/Pro.277 |
0.639 |
|
2010 |
Bosse-Doenecke E, Weininger U, Gopalswamy M, Balbach J, Knudsen SM, Rudolph R. Corrigendum to "High yield production of recombinant native and modified peptides exemplified by ligands for G-protein coupled receptors" [Protein Expr. Purif. 58 (2008) 114-121] (DOI:10.1016/j.pep.2007.10.012) Protein Expression and Purification. 70: 298. DOI: 10.1016/J.Pep.2010.01.013 |
0.332 |
|
2009 |
Weininger U, Zeeb M, Neumann P, L̈ow C, Stubbs MT, Lipps G, Balbach J. Structure-based stability analysis of an extremely stable dimeric DNA binding protein from Sulfolobus islandicus Biochemistry. 48: 10030-10037. PMID 19788170 DOI: 10.1021/Bi900760N |
0.404 |
|
2009 |
Schulenburg C, Löw C, Weininger U, Mrestani-Klaus C, Hofmann H, Balbach J, Ulbrich-Hofmann R, Arnold U. The folding pathway of onconase is directed by a conserved intermediate Biochemistry. 48: 8449-8457. PMID 19655705 DOI: 10.1021/Bi900596J |
0.438 |
|
2009 |
Weininger U, Jakob RP, Eckert B, Schweimer K, Schmid FX, Balbach J. A remote prolyl isomerization controls domain assembly via a hydrogen bonding network Proceedings of the National Academy of Sciences of the United States of America. 106: 12335-12340. PMID 19617535 DOI: 10.1073/Pnas.0902102106 |
0.591 |
|
2009 |
Weininger U, Haupt C, Schweimer K, Graubner W, Kovermann M, Brüser T, Scholz C, Schaarschmidt P, Zoldak G, Schmid FX, Balbach J. NMR Solution Structure of SlyD from Escherichia coli: Spatial Separation of Prolyl Isomerase and Chaperone Function Journal of Molecular Biology. 387: 295-305. PMID 19356587 DOI: 10.1016/J.Jmb.2009.01.034 |
0.63 |
|
2009 |
Löw C, Homeyer N, Weininger U, Sticht H, Balbach J. Conformational switch upon phosphorylation: Human CDK inhibitor p19 INK4d between the native and partially folded state Acs Chemical Biology. 4: 53-63. PMID 19063602 DOI: 10.1021/Cb800219M |
0.352 |
|
2009 |
Hofmann H, Weininger U, Löw C, Golbik RP, Balbach J, Ulbrich-Hofmann R. Fast amide proton exchange reveals close relation between native-state dynamics and unfolding kinetics Journal of the American Chemical Society. 131: 140-146. PMID 19061322 DOI: 10.1021/Ja8048942 |
0.404 |
|
2008 |
Hoffmann A, Funkner A, Neumann P, Juhnke S, Walther M, Schierhorn A, Weininger U, Balbach J, Reuter G, Stubbs MT. Biophysical characterization of refolded Drosophila spätzle, a cystine knot protein, reveals distinct properties of three isoforms Journal of Biological Chemistry. 283: 32598-32609. PMID 18790733 DOI: 10.1074/Jbc.M801815200 |
0.407 |
|
2008 |
Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers Biophysical Journal. 95: 4315-4323. PMID 18658220 DOI: 10.1529/Biophysj.108.134155 |
0.414 |
|
2008 |
Rohrberg J, Sachs R, Lodderstedt G, Sackewitz M, Balbach J, Schwarz E. Monitoring fibril formation of the N-terminal domain of PABPN1 carrying an alanine repeat by tryptophan fluorescence and real-time NMR Febs Letters. 582: 1587-1592. PMID 18406354 DOI: 10.1016/J.Febslet.2008.04.002 |
0.423 |
|
2008 |
Löw C, Weininger U, Neumann P, Klepsch M, Lilie H, Stubbs MT, Balbach J. Structural insights into an equilibrium folding intermediate of an archaeal ankyrin repeat protein Proceedings of the National Academy of Sciences of the United States of America. 105: 3779-3784. PMID 18305166 DOI: 10.1073/Pnas.0710657105 |
0.462 |
|
2008 |
Bosse-Doenecke E, Weininger U, Gopalswamy M, Balbach J, Knudsen SM, Rudolph R. High yield production of recombinant native and modified peptides exemplified by ligands for G-protein coupled receptors Protein Expression and Purification. 58: 114-121. PMID 18248821 DOI: 10.1016/J.Pep.2007.10.012 |
0.36 |
|
2008 |
Lodderstedt G, Sachs R, Faust J, Bordusa F, Kühn U, Golbik R, Kerth A, Wahle E, Balbach J, Schwarz E. Hofmeister salts and potential therapeutic compounds accelerate in vitro fibril formation of the N-terminal domain of PABPN1 containing a disease-causing alanine extension Biochemistry. 47: 2181-2189. PMID 18205394 DOI: 10.1021/Bi701322G |
0.369 |
|
2008 |
Zeeb M, Balbach J. Kinetic Protein Folding Studies using NMR Spectroscopy Protein Folding Handbook. 1: 536-572. DOI: 10.1002/9783527619498.ch16 |
0.325 |
|
2007 |
Löw C, Weininger U, Zeeb M, Zhang W, Laue ED, Schmid FX, Balbach J. Folding Mechanism of an Ankyrin Repeat Protein: Scaffold and Active Site Formation of Human CDK Inhibitor p19INK4d Journal of Molecular Biology. 373: 219-231. PMID 17804013 DOI: 10.1016/J.Jmb.2007.07.063 |
0.597 |
|
2007 |
Max KE, Zeeb M, Bienert R, Balbach J, Heinemann U. Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus. The Febs Journal. 274: 1265-79. PMID 17266726 DOI: 10.1111/J.1742-4658.2007.05672.X |
0.452 |
|
2006 |
Zeeb M, Max KEA, Weininger U, Löw C, Sticht H, Balbach J. Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution Nucleic Acids Research. 34: 4561-4571. PMID 16956971 DOI: 10.1093/Nar/Gkl376 |
0.393 |
|
2006 |
Max KE, Zeeb M, Bienert R, Balbach J, Heinemann U. T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB. Journal of Molecular Biology. 360: 702-14. PMID 16780871 DOI: 10.1016/J.Jmb.2006.05.044 |
0.388 |
|
2006 |
Kliemannel M, Weininger U, Balbach J, Schwarz E, Rudolph R. Examination of the slow unfolding of pro-nerve growth factor argues against a loop threading mechanism for nerve growth factor Biochemistry. 45: 3517-3524. PMID 16533032 DOI: 10.1021/Bi051896T |
0.411 |
|
2006 |
Scholz C, Eckert B, Hagn F, Schaarschmidt P, Balbach J, Schmid FX. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities Biochemistry. 45: 20-33. PMID 16388577 DOI: 10.1021/Bi051922N |
0.623 |
|
2006 |
Szyperski T, Mills JL, Perl D, Balbach J. Combined NMR-observation of cold denaturation in supercooled water and heat denaturation enables accurate measurement of ΔCp of protein unfolding European Biophysics Journal. 35: 363-366. PMID 16240113 DOI: 10.1007/S00249-005-0028-4 |
0.342 |
|
2005 |
Zeeb M, Balbach J. NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements Journal of the American Chemical Society. 127: 13207-13212. PMID 16173748 DOI: 10.1021/Ja051141+ |
0.429 |
|
2005 |
Hofweber R, Horn G, Langmann T, Balbach J, Kremer W, Schmitz G, Kalbitzer HR. The influence of cold shock proteins on transcription and translation studied in cell-free model systems. The Febs Journal. 272: 4691-702. PMID 16156790 DOI: 10.1111/J.1742-4658.2005.04885.X |
0.371 |
|
2005 |
Eckert B, Martin A, Balbach J, Schmid FX. Prolyl isomerization as a molecular timer in phage infection Nature Structural and Molecular Biology. 12: 619-623. PMID 15937494 DOI: 10.1038/Nsmb946 |
0.56 |
|
2005 |
Zeeb M, Balbach J. Millisecond protein folding studied by NMR spectroscopy Protein and Peptide Letters. 12: 139-146. PMID 15723639 DOI: 10.2174/0929866053005917 |
0.44 |
|
2005 |
Scholz C, Schaarschmidt P, Engel AM, Andres H, Schmitt U, Faatz E, Balbach J, Schmid FX. Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules Journal of Molecular Biology. 345: 1229-1241. PMID 15644217 DOI: 10.1016/J.Jmb.2004.10.091 |
0.508 |
|
2004 |
Zeeb M, Balbach J. Protein folding studied by real-time NMR spectroscopy Methods. 34: 65-74. PMID 15283916 DOI: 10.1016/J.Ymeth.2004.03.014 |
0.407 |
|
2004 |
Kliemannel M, Rattenholl A, Golbik R, Balbach J, Lilie H, Rudolph R, Schwarz E. The mature part of proNGF induces the structure of its pro-peptide Febs Letters. 566: 207-212. PMID 15147896 DOI: 10.1016/J.Febslet.2004.04.034 |
0.366 |
|
2004 |
Bienert R, Zeeb M, Dostál L, Feske A, Magg C, Max K, Welfle H, Balbach J, Heinemann U. Single-stranded DNA bound to bacterial cold-shock proteins: preliminary crystallographic and Raman analysis. Acta Crystallographica. Section D, Biological Crystallography. 60: 755-7. PMID 15039576 DOI: 10.1107/S0907444904002422 |
0.338 |
|
2004 |
Zeeb M, Lipps G, Lilie H, Balbach J. Folding and Association of an Extremely Stable Dimeric Protein from Sulfolobus islandicus Journal of Molecular Biology. 336: 227-240. PMID 14741218 DOI: 10.1016/J.Jmb.2003.12.003 |
0.395 |
|
2003 |
Zeeb M, Jacob MH, Schindler T, Balbach J. 15N relaxation study of the cold shock protein CspB at various solvent viscosities Journal of Biomolecular Nmr. 27: 221-234. PMID 12975582 DOI: 10.1023/A:1025449611201 |
0.389 |
|
2003 |
Zeeb M, Balbach J. Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization Protein Science. 12: 112-123. PMID 12493834 DOI: 10.1110/Ps.0219703 |
0.315 |
|
2002 |
Zeeb M, Rösner H, Zeslawski W, Canet D, Holak TA, Balbach J. Protein folding and stability of human CDK inhibitor p19INK4d Journal of Molecular Biology. 315: 447-457. PMID 11786024 DOI: 10.1006/Jmbi.2001.5242 |
0.418 |
|
2000 |
Steegborn C, Schneider-Hassloff H, Zeeb M, Balbach J. Cooperativity of a protein folding reaction probed at multiple chain positions by real-time 2D NMR spectroscopy Biochemistry. 39: 7910-7919. PMID 10891071 DOI: 10.1021/Bi000270U |
0.415 |
|
2000 |
Balbach J. Compaction during protein folding studied by real-time NMR diffusion experiments [6] Journal of the American Chemical Society. 122: 5887-5888. DOI: 10.1021/Ja994514D |
0.355 |
|
1999 |
Forge V, Wijesinha RT, Balbach J, Brew K, Robinson CV, Redfield C, Dobson CM. Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin Journal of Molecular Biology. 288: 673-688. PMID 10329172 DOI: 10.1006/Jmbi.1999.2687 |
0.441 |
|
1999 |
Balbach J, Steegborn C, Schindler T, Schmid FX. A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy. Journal of Molecular Biology. 285: 829-42. PMID 9878447 DOI: 10.1006/Jmbi.1998.2364 |
0.59 |
|
1998 |
Balbach J, Seip S, Kessler H, Scharf M, Kashani-Poor N, Engels JW. Structure and dynamic properties of the single disulfide-deficient alpha-amylase inhibitor [C45A/C73A]tendamistat: an NMR study. Proteins. 33: 285-94. PMID 9779794 DOI: 10.1002/(Sici)1097-0134(19981101)33:2<285::Aid-Prot11>3.0.Co;2-G |
0.355 |
|
1997 |
Balbach J, Forge V, Lau WS, Jones JA, van Nuland NA, Dobson CM. Detection of residue contacts in a protein folding intermediate. Proceedings of the National Academy of Sciences of the United States of America. 94: 7182-5. PMID 9207065 DOI: 10.1073/Pnas.94.14.7182 |
0.433 |
|
1997 |
Jacob M, Schindler T, Balbach J, Schmid FX. Diffusion control in an elementary protein folding reaction. Proceedings of the National Academy of Sciences of the United States of America. 94: 5622-7. PMID 9159122 DOI: 10.1073/Pnas.94.11.5622 |
0.582 |
|
1996 |
Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM. Protein folding monitored at individual residues during a two-dimensional NMR experiment. Science (New York, N.Y.). 274: 1161-3. PMID 8895458 DOI: 10.1126/Science.274.5290.1161 |
0.422 |
|
1995 |
Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM. Following protein folding in real time using NMR spectroscopy. Nature Structural Biology. 2: 865-70. PMID 7552710 DOI: 10.1038/Nsb1095-865 |
0.4 |
|
1994 |
Marković-Housley Z, Balbach J, Stolz B, Génovésio-Taverne JC. Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli. Febs Letters. 340: 202-6. PMID 8131846 DOI: 10.1016/0014-5793(94)80138-X |
0.383 |
|
1994 |
Seip S, Balbach J, Behrens S, Kessler H, Flükiger K, de Meyer R, Erni B. Mannose transporter of Escherichia coli. Backbone assignments and secondary structure of the IIA domain of the IIABMan subunit. Biochemistry. 33: 7174-83. PMID 8003484 DOI: 10.1021/Bi00189A021 |
0.428 |
|
1994 |
Balbach J, Kessler H. 13C-Edited Double-Quantum Spectroscopy of Peptides and Proteins Journal of Magnetic Resonance, Series B. 105: 83-87. DOI: 10.1006/Jmrb.1994.1105 |
0.315 |
|
1994 |
Seip S, Balbach J, Kessler H. Determination of Backbone Conformation of Isotopically Enriched Proteins Based on Coupling Constants Journal of Magnetic Resonance, Series B. 104: 172-179. DOI: 10.1006/Jmrb.1994.1072 |
0.365 |
|
1993 |
Seip S, Balbach J, Kessler H. A simple way for sequential assignment in isotopically enriched proteins using a H(N)CACO correlation Journal of Biomolecular Nmr. 3: 233-237. DOI: 10.1007/Bf00178265 |
0.342 |
|
1992 |
Seip S, Balbach J, Kessler H. An improved technique for correlating backbone amide protons with 15N and Hα protons (HN(CA)H) in isotopically enriched proteins Journal of Magnetic Resonance (1969). 100: 406-410. DOI: 10.1016/0022-2364(92)90274-B |
0.308 |
|
1992 |
Seip S, Balbach J, Kessler H. Determination of the HN–Hα Coupling Constant in Large Isotopically Enriched Proteins Angewandte Chemie. 31: 1609-1611. DOI: 10.1002/Anie.199216091 |
0.319 |
|
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