Jochen Balbach - Publications

Affiliations: 
 
Area:
NMR, protein folding

99 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
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  0.68
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  0.72
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  0.72
2016 Garvey M, Baumann M, Wulff M, Kumar ST, Markx D, Morgado I, Knüpfer U, Horn U, Mawrin C, Fändrich M, Balbach J. Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 1-10. PMID 26972581 DOI: 10.3109/13506129.2016.1146989  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2015 Hoffmann A, Kovermann M, Oberwinkler T, Siedler F, Cortina NS, Balbach J, Oesterhelt D. Novel sulfated phosphoglycolipids from Natronomonas moolapensis. Chemistry and Physics of Lipids. 191: 8-15. PMID 26134137 DOI: 10.1016/j.chemphyslip.2015.06.004  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2015 Dinesh DC, Kovermann M, Gopalswamy M, Hellmuth A, Villalobos LIAC, 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: 6230-6235. DOI: 10.1073/pnas.1424077112  0.72
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. DOI: 10.1016/j.febslet.2015.07.008  0.72
2014 Reich S, Kovermann M, Lilie H, Knick P, Geissler R, Golbik RP, Balbach J, Behrens SE. Initiation of RNA synthesis by the hepatitis C virus RNA-dependent RNA polymerase is affected by the structure of the RNA template Biochemistry. 53: 7002-7012. PMID 25310724 DOI: 10.1021/bi5006656  0.72
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  0.72
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  0.72
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  0.72
2014 Kumar A, Balbach J. Real-time protein NMR spectroscopy and investigation of assisted protein folding Biochimica Et Biophysica Acta - General Subjects. DOI: 10.1016/j.bbagen.2014.12.003  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2010 Bernhardt P, Imhof A, Schwaab J, Balbach J, Walcher D, Spieß J, Schmid M. Neoplastic pericardial effusion induces functional nonvalvular mitral valve stenosis Journal of the American College of Cardiology. 56: e29. PMID 20883923 DOI: 10.1016/j.jacc.2009.12.077  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2010 Herbst F, Schröter K, Gunkel I, Gröger S, Thurn-Albrecht T, Balbach J, Binder WH. Aggregation and chain dynamics in supramolecular polymers by dynamic rheology: Cluster formation and self-Aggregation Macromolecules. 43: 10006-10016. DOI: 10.1021/ma101962y  0.72
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  0.72
2009 Pornsuriyasak P, Vetter C, Kaeothip S, Kovermann M, Balbach J, Steinborn D, Demchenko AV. Coordination chemistry approach to the long-standing challenge of stereocontrolled chemical glycosylation Chemical Communications. 6379-6381. PMID 19841783 DOI: 10.1039/b903942b  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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+  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2002 Schäfler AE, Kirmanoglou K, Balbach J, Pecher P, Hannekum A, Schumacher B. The expression of heat shock protein 60 in myocardium of patients with chronic atrial fibrillation Basic Research in Cardiology. 97: 258-261. PMID 12061396 DOI: 10.1007/s003950200019  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
1998 Van Nuland NAJ, Forge V, Balbach J, Dobson CM. Real-Time NMR Studies of Protein Folding Accounts of Chemical Research. 31: 773-780.  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
1992 Mronga S, Balbach J. Multiplet structure in real cosine fourier-transformed zero-quantum spectra without axial peaks Journal of Magnetic Resonance (1969). 98: 421-427. DOI: 10.1016/0022-2364(92)90143-U  0.72
1992 Seip S, Balbach J, Kessler H. Determination of the HN-Hα coupling constant in large isotopically enriched proteins Angewandte Chemie (International Edition in English). 31: 1609-1611.  0.72
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