| Year |
Citation |
Score |
| 2023 |
Hohmann T, Dubatouka P, Pfeifer K, Koksch B. Establishing Fluorine-Containing Amino Acids as an Orthogonal Tool in Coiled Coil Assembly. Biomacromolecules. 24: 3357-3369. PMID 37379337 DOI: 10.1021/acs.biomac.3c00427 |
0.352 |
|
| 2023 |
Hohmann T, Chowdhary S, Ataka K, Er J, Dreyhsig GH, Heberle J, Koksch B. Introducing Aliphatic Fluoropeptides: Perspectives on Folding Properties, Membrane Partition and Proteolytic Stability. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 36722398 DOI: 10.1002/chem.202203860 |
0.356 |
|
| 2022 |
Chowdhary S, Schmidt RF, Sahoo AK, Tom Dieck T, Hohmann T, Schade B, Brademann-Jock K, Thünemann AF, Netz RR, Gradzielski M, Koksch B. Rational design of amphiphilic fluorinated peptides: evaluation of self-assembly properties and hydrogel formation. Nanoscale. PMID 35796261 DOI: 10.1039/d2nr01648f |
0.326 |
|
| 2022 |
Leppkes J, Dimos N, Loll B, Hohmann T, Dyrks M, Wieseke A, Keller BG, Koksch B. Fluorine-induced polarity increases inhibitory activity of BPTI towards chymotrypsin. Rsc Chemical Biology. 3: 773-782. PMID 35755190 DOI: 10.1039/d2cb00018k |
0.336 |
|
| 2020 |
Chowdhary S, Moschner J, Mikolajczak DJ, Becker M, Thünemann AF, Kästner C, Klemczak D, Stegemann AK, Böttcher C, Metrangolo P, Netz RR, Koksch B. The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation. Chembiochem : a European Journal of Chemical Biology. 21: 3544-3554. PMID 33405360 DOI: 10.1002/Cbic.202000373 |
0.368 |
|
| 2020 |
Mikolajczak DJ, Berger AA, Koksch B. Catalytically Active Peptide-Gold Nanoparticle Conjugates: Prospecting for Artificial Enzymes. Angewandte Chemie (International Ed. in English). PMID 31905254 DOI: 10.1002/Anie.201908625 |
0.358 |
|
| 2020 |
Leppkes J, Hohmann T, Koksch B. Improved enantioselective gram scale synthesis route to N-Fmoc-protected monofluoroethylglycine Journal of Fluorine Chemistry. 232: 109453. DOI: 10.1016/J.Jfluchem.2020.109453 |
0.437 |
|
| 2020 |
Koksch B, Seeberger PH. Peptide Engineering Meeting 8 Peptide Science. 112. DOI: 10.1002/Pep2.24146 |
0.346 |
|
| 2019 |
Zivkovic I, Moschner J, Koksch B, Gruic-Sovulj I. Mechanism of discrimination of isoleucyl-tRNA synthetase against nonproteinogenic α-aminobutyrate and its fluorinated analogues. The Febs Journal. PMID 31486189 DOI: 10.1111/Febs.15053 |
0.336 |
|
| 2019 |
Moschner J, Stulberg V, Fernandes R, Huhmann S, Leppkes J, Koksch B. Approaches to Obtaining Fluorinated α-Amino Acids. Chemical Reviews. PMID 31436087 DOI: 10.1021/Acs.Chemrev.9B00024 |
0.356 |
|
| 2019 |
López-García P, Goktas M, Bergues-Pupo AE, Koksch B, Varón Silva D, Blank KG. Structural determinants of coiled coil mechanics. Physical Chemistry Chemical Physics : Pccp. 21: 9145-9149. PMID 31016294 DOI: 10.1039/C9Cp00665F |
0.33 |
|
| 2019 |
Hellmund KS, Koksch B. Self-Assembling Peptides as Extracellular Matrix Mimics to Influence Stem Cell's Fate. Frontiers in Chemistry. 7: 172. PMID 31001512 DOI: 10.3389/Fchem.2019.00172 |
0.339 |
|
| 2019 |
Hoffmann W, Langenhan J, Huhmann S, Moschner J, Chang R, Accorsi M, Seo J, Jörg R, Meijer G, Koksch B, Bowers MT, von Helden G, Pagel K. An Intrinsic Hydrophobicity Scale for Amino Acids and Its Application to Fluorinated Compounds. Angewandte Chemie (International Ed. in English). PMID 30958917 DOI: 10.1002/Anie.201813954 |
0.357 |
|
| 2019 |
Mikolajczak DJ, Koksch B. Peptide–Gold Nanoparticle Conjugates as Artificial Carbonic Anhydrase Mimics Catalysts. 9: 903. DOI: 10.3390/Catal9110903 |
0.333 |
|
| 2019 |
Thota CK, Berger AA, Harms B, Seidel M, Böttcher C, von Berlepsch H, Xie C, Süssmuth R, Roth C, Koksch B. Short self‐assembling cationic antimicrobial peptide mimetics based on a 3,5‐diaminobenzoic acid scaffold Peptide Science. 112. DOI: 10.1002/Pep2.24130 |
0.419 |
|
| 2018 |
de Freitas MS, Rezaei Araghi R, Brandenburg E, Leiterer J, Emmerling F, Folmert K, Gerling-Driessen UIM, Bardiaux B, Böttcher C, Pagel K, Diehl A, Berlepsch HV, Oschkinat H, Koksch B. The protofilament architecture of a de novo designed coiled coil-based amyloidogenic peptide. Journal of Structural Biology. PMID 29857134 DOI: 10.1016/J.Jsb.2018.05.009 |
0.385 |
|
| 2018 |
Huhmann S, Koksch B. Fine-Tuning the Proteolytic Stability of Peptides with Fluorinated Amino Acids European Journal of Organic Chemistry. 2018: 3667-3679. DOI: 10.1002/Ejoc.201800803 |
0.427 |
|
| 2018 |
Mikolajczak DJ, Scholz J, Koksch B. Tuning the Catalytic Activity and Substrate Specificity of Peptide-Nanoparticle Conjugates Chemcatchem. 10: 5665-5668. DOI: 10.1002/Cctc.201801521 |
0.349 |
|
| 2017 |
Huhmann S, Stegemann AK, Folmert K, Klemczak D, Moschner J, Kube M, Koksch B. Position-dependent impact of hexafluoroleucine and trifluoroisoleucine on protease digestion. Beilstein Journal of Organic Chemistry. 13: 2869-2882. PMID 29564015 DOI: 10.3762/Bjoc.13.279 |
0.458 |
|
| 2017 |
Hoffmann W, Folmert K, Moschner J, Huang X, von Berlepsch H, Koksch B, Bowers MT, von Helden G, Pagel K. NFGAIL Amyloid Oligomers: The Onset of Beta-Sheet Formation and the Mechanism for Fibril Formation. Journal of the American Chemical Society. PMID 29235867 DOI: 10.1021/Jacs.7B09510 |
0.336 |
|
| 2017 |
Mikolajczak DJ, Heier JL, Schade B, Koksch B. Catalytic activity of peptide-nanoparticle conjugates regulated by a conformational change. Biomacromolecules. PMID 28925256 DOI: 10.1021/Acs.Biomac.7B00887 |
0.414 |
|
| 2017 |
Völler JS, Thi To TM, Biava H, Koksch B, Budisa N. Global substitution of hemeproteins with noncanonical amino acids in Escherichia coli with intact cofactor maturation machinery. Enzyme and Microbial Technology. 106: 55-59. PMID 28859810 DOI: 10.1016/J.Enzmictec.2017.06.014 |
0.382 |
|
| 2017 |
Berger AA, Völler JS, Budisa N, Koksch B. Deciphering the Fluorine Code-The Many Hats Fluorine Wears in a Protein Environment. Accounts of Chemical Research. PMID 28803466 DOI: 10.1021/Acs.Accounts.7B00226 |
0.466 |
|
| 2017 |
Völler JS, Dulic M, Gerling-Driessen UI, Biava H, Baumann T, Budisa N, Gruic-Sovulj I, Koksch B. Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein Translation. Acs Central Science. 3: 73-80. PMID 28149956 DOI: 10.1021/Acscentsci.6B00339 |
0.416 |
|
| 2017 |
Budisa N, Völler JS, Koksch B, Acevedo-Rocha CG, Kubyshkin V, Agostini F. Xenobiology meets enzymology: Exploring the potential of unnatural building blocks in biocatalysis. Angewandte Chemie (International Ed. in English). PMID 28085996 DOI: 10.1002/Anie.201610129 |
0.318 |
|
| 2017 |
Robalo JR, Huhmann S, Koksch B, Vila Verde A. The Multiple Origins of the Hydrophobicity of Fluorinated Apolar Amino Acids Chem. 3: 881-897. DOI: 10.1016/J.Chempr.2017.09.012 |
0.365 |
|
| 2016 |
Folmert K, Broncel M, V Berlepsch H, Ullrich CH, Siegert MA, Koksch B. Inhibition of peptide aggregation by means of enzymatic phosphorylation. Beilstein Journal of Organic Chemistry. 12: 2462-2470. PMID 28144314 DOI: 10.3762/Bjoc.12.240 |
0.41 |
|
| 2016 |
Heier JL, Mikolajczak DJ, Böttcher C, Koksch B. Substrate specificity of an actively assembling amyloid catalyst. Biopolymers. PMID 27858968 DOI: 10.1002/Bip.23003 |
0.337 |
|
| 2016 |
Hoernke M, Tassler S, Koksch B, Brezesinski G. Membrane Binding of Peptide Models for early Stages of Amyloid Formation: Lipid Packing Counts more than Charge. Chemistry and Physics of Lipids. PMID 27134131 DOI: 10.1016/J.Chemphyslip.2016.02.010 |
0.381 |
|
| 2015 |
Ye S, Loll B, Berger AA, Mülow U, Alings C, Wahl MC, Koksch B. Fluorine teams up with water to restore inhibitor activity to mutant BPTI. Chemical Science. 6: 5246-5254. PMID 29449928 DOI: 10.1039/C4Sc03227F |
0.335 |
|
| 2015 |
Schöne D, Schade B, Böttcher C, Koksch B. Impact of multivalent charge presentation on peptide-nanoparticle aggregation. Beilstein Journal of Organic Chemistry. 11: 792-803. PMID 26124881 DOI: 10.3762/Bjoc.11.89 |
0.39 |
|
| 2015 |
Gerling-Driessen UI, Mujkic-Ninnemann N, Ponader D, Schöne D, Hartmann L, Koksch B. Exploiting oligo(amido amine) backbones for the multivalent presentation of coiled coil peptides. Biomacromolecules. PMID 26114337 DOI: 10.1021/Acs.Biomac.5B00634 |
0.408 |
|
| 2015 |
Zacco E, Hütter J, Heier JL, Mortier J, Seeberger PH, Lepenies B, Koksch B. Tailored Presentation of Carbohydrates on a Coiled Coil-Based Scaffold for Asialoglycoprotein Receptor Targeting. Acs Chemical Biology. PMID 26057877 DOI: 10.1021/Acschembio.5B00435 |
0.409 |
|
| 2015 |
Zacco E, Anish C, Martin CE, V Berlepsch H, Brandenburg E, Seeberger PH, Koksch B. A Self-Assembling Peptide Scaffold for the Multivalent Presentation of Antigens. Biomacromolecules. 16: 2188-97. PMID 26017366 DOI: 10.1021/Acs.Biomac.5B00572 |
0.394 |
|
| 2015 |
Schubert F, Rossi M, Baldauf C, Pagel K, Warnke S, von Helden G, Filsinger F, Kupser P, Meijer G, Salwiczek M, Koksch B, Scheffler M, Blum V. Exploring the conformational preferences of 20-residue peptides in isolation: Ac-Ala19-Lys + H(+)vs. Ac-Lys-Ala19 + H(+) and the current reach of DFT. Physical Chemistry Chemical Physics : Pccp. 17: 7373-85. PMID 25700010 DOI: 10.1039/C4Cp05541A |
0.377 |
|
| 2015 |
Mortier J, Nyakatura EK, Reimann O, Huhmann S, Daldrop JO, Baldauf C, Wolber G, Miettinen MS, Koksch B. Coiled-coils in phage display screening: insight into exceptional selectivity provided by molecular dynamics. Journal of Chemical Information and Modeling. 55: 495-500. PMID 25648076 DOI: 10.1021/Ci500689C |
0.371 |
|
| 2015 |
Schubert F, Pagel K, Rossi M, Warnke S, Salwiczek M, Koksch B, von Helden G, Blum V, Baldauf C, Scheffler M. Native like helices in a specially designed β peptide in the gas phase. Physical Chemistry Chemical Physics : Pccp. 17: 5376-85. PMID 25611682 DOI: 10.1039/C4Cp05216A |
0.416 |
|
| 2015 |
Gerling UI, Miettinen MS, Koksch B. Concluding the amyloid formation pathway of a coiled-coil-based peptide from the size of the critical nucleus. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 16: 108-14. PMID 25257178 DOI: 10.1002/Cphc.201402400 |
0.354 |
|
| 2015 |
Huhmann S, Nyakatura EK, Erdbrink H, Gerling UIM, Czekelius C, Koksch B. Effects of single substitutions with hexafluoroleucine and trifluorovaline on the hydrophobic core formation of a heterodimeric coiled coil Journal of Fluorine Chemistry. 175: 32-35. DOI: 10.1016/J.Jfluchem.2015.03.003 |
0.487 |
|
| 2015 |
Vukelic S, Ushakov DB, Gilmore K, Koksch B, Seeberger PH. Flow synthesis of fluorinated α-amino acids European Journal of Organic Chemistry. 2015: 3036-3039. DOI: 10.1002/Ejoc.201500300 |
0.36 |
|
| 2014 |
Nyakatura EK, Mortier J, Radtke VS, Wieczorek S, Rezaei Araghi R, Baldauf C, Wolber G, Koksch B. β- and γ-Amino Acids at α-Helical Interfaces: Toward the Formation of Highly Stable Foldameric Coiled Coils. Acs Medicinal Chemistry Letters. 5: 1300-3. PMID 25516788 DOI: 10.1021/Ml500361C |
0.478 |
|
| 2014 |
Asante V, Mortier J, Wolber G, Koksch B. Impact of fluorination on proteolytic stability of peptides: a case study with α-chymotrypsin and pepsin. Amino Acids. 46: 2733-44. PMID 25193166 DOI: 10.1007/S00726-014-1819-7 |
0.456 |
|
| 2014 |
Mortier J, Nyakatura EK, Miettinen M, Baldauf C, Wolber G, Koksch B. Balancing selectivity vs stability using molecular dynamics and umbrella sampling. Journal of Cheminformatics. 6: O22. PMID 24765121 DOI: 10.1186/1758-2946-6-S1-O22 |
0.415 |
|
| 2014 |
Nyakatura EK, Rezaei Araghi R, Mortier J, Wieczorek S, Baldauf C, Wolber G, Koksch B. An unusual interstrand H-bond stabilizes the heteroassembly of helical αβγ-chimeras with natural peptides. Acs Chemical Biology. 9: 613-6. PMID 24341921 DOI: 10.1021/Cb4007979 |
0.453 |
|
| 2014 |
Maity J, Gerling UI, Vukeli? S, Schäfer A, Koksch B. Proline-glutamate chimera's side chain conformation directs the type of β-hairpin structure. Amino Acids. 46: 177-86. PMID 24221353 DOI: 10.1007/S00726-013-1610-1 |
0.384 |
|
| 2014 |
Gerling UIM, Salwiczek M, Cadicamo CD, Erdbrink H, Czekelius C, Grage SL, Wadhwani P, Ulrich AS, Behrends M, Haufe G, Koksch B. Fluorinated amino acids in amyloid formation: A symphony of size, hydrophobicity and α-helix propensity Chemical Science. 5: 819-830. DOI: 10.1039/C3Sc52932K |
0.467 |
|
| 2014 |
Baldauf C, Schubert F, Pagel K, Warnke S, Rossi M, Salwiczek M, Koksch B, von Helden G, Blum V. Is there a Beta-Peptide Equivalent of the Alpha-Helix? Biophysical Journal. 106: 654a. DOI: 10.1016/J.Bpj.2013.11.3621 |
0.418 |
|
| 2014 |
Do N, Weindl G, Fleige E, Salwiczek M, Koksch B, Haag R, Schäfer-Korting M. Core-multishell nanotransporters enhance skin penetration of the cell-penetrating peptide low molecular weight protamine Polymers For Advanced Technologies. 25: 1337-1341. DOI: 10.1002/Pat.3362 |
0.342 |
|
| 2013 |
Erdbrink H, Nyakatura EK, Huhmann S, Gerling UI, Lentz D, Koksch B, Czekelius C. Synthesis of enantiomerically pure (2S,3S)-5,5,5-trifluoroisoleucine and (2R,3S)-5,5,5-trifluoro-allo-isoleucine. Beilstein Journal of Organic Chemistry. 9: 2009-14. PMID 24204411 DOI: 10.3762/Bjoc.9.236 |
0.318 |
|
| 2013 |
Baldauf C, Pagel K, Warnke S, von Helden G, Koksch B, Blum V, Scheffler M. How cations change peptide structure. Chemistry (Weinheim An Der Bergstrasse, Germany). 19: 11224-34. PMID 23853047 DOI: 10.1002/Chem.201204554 |
0.414 |
|
| 2013 |
Rakowska PD, Jiang H, Ray S, Pyne A, Lamarre B, Carr M, Judge PJ, Ravi J, Gerling UI, Koksch B, Martyna GJ, Hoogenboom BW, Watts A, Crain J, Grovenor CR, et al. Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers. Proceedings of the National Academy of Sciences of the United States of America. 110: 8918-23. PMID 23671080 DOI: 10.1073/Pnas.1222824110 |
0.351 |
|
| 2013 |
Asante V, Mortier J, Schlüter H, Koksch B. Impact of fluorination on proteolytic stability of peptides in human blood plasma. Bioorganic & Medicinal Chemistry. 21: 3542-6. PMID 23623671 DOI: 10.1016/J.Bmc.2013.03.051 |
0.42 |
|
| 2013 |
Cadicamo CD, Mortier J, Wolber G, Hell M, Heinrich IE, Michel D, Semlin L, Berger U, Korting HC, Höltje HD, Koksch B, Borelli C. Design, synthesis, inhibition studies, and molecular modeling of pepstatin analogues addressing different secreted aspartic proteinases of Candida albicans. Biochemical Pharmacology. 85: 881-7. PMID 23262278 DOI: 10.1016/J.Bcp.2012.12.008 |
0.316 |
|
| 2013 |
Nyakatura EK, Reimann O, Vagt T, Salwiczek M, Koksch B. Accommodating fluorinated amino acids in a helical peptide environment Rsc Advances. 3: 6319-6322. DOI: 10.1039/C3Ra41110A |
0.457 |
|
| 2012 |
Erdbrink H, Peuser I, Gerling UI, Lentz D, Koksch B, Czekelius C. Conjugate hydrotrifluoromethylation of α,β-unsaturated acyl-oxazolidinones: synthesis of chiral fluorinated amino acids. Organic & Biomolecular Chemistry. 10: 8583-6. PMID 23042408 DOI: 10.1039/C2Ob26810H |
0.357 |
|
| 2012 |
Brandenburg E, Berlepsch HV, Leiterer J, Emmerling F, Koksch B. Formation of α-helical nanofibers by mixing β-structured and α-helical coiled coil peptides. Biomacromolecules. 13: 3542-51. PMID 22946440 DOI: 10.1021/Bm300882D |
0.433 |
|
| 2012 |
Rezaei Araghi R, Mahrenholz CC, Volkmer R, Koksch B. Investigation of the network of preferred interactions in an artificial coiled-coil association using the peptide array technique. Beilstein Journal of Organic Chemistry. 8: 640-9. PMID 22563362 DOI: 10.3762/Bjoc.8.71 |
0.437 |
|
| 2012 |
Salwiczek M, Nyakatura EK, Gerling UI, Ye S, Koksch B. Fluorinated amino acids: compatibility with native protein structures and effects on protein-protein interactions. Chemical Society Reviews. 41: 2135-71. PMID 22130572 DOI: 10.1039/C1Cs15241F |
0.462 |
|
| 2012 |
Brandenburg E, von Berlepsch H, Koksch B. Specific in situ discrimination of amyloid fibrils versus α-helical fibres by the fluorophore NIAD-4. Molecular Biosystems. 8: 557-64. PMID 22116468 DOI: 10.1039/C1Mb05370A |
0.371 |
|
| 2012 |
Maity J, Saha P, Gerling U, Lentz D, Koksch B. An Approach for Simultaneous Synthesis of cis- and trans-3-Substituted Proline-Glutamic Acid Chimeras Synthesis. 44. DOI: 10.1055/S-0032-1316986 |
0.356 |
|
| 2012 |
Baldauf C, Pagel K, Warnke S, von Helden G, Meijer G, Koksch B, Blum V, Scheffler M. Local Conformational Preferences of Peptides Near Attached Cations: Structure Determination by First-Principles Theory and IR-Spectroscopy Biophysical Journal. 102: 46a. DOI: 10.1016/J.Bpj.2011.11.280 |
0.368 |
|
| 2012 |
Hoernke M, Koksch B, Brezesinski G. The Conformation of Amyloidogenic Peptides is Governed by (Transient) Interfaces and Influenced by Metal Ion Complexation Biophysical Journal. 102: 489a. DOI: 10.1016/J.Bpj.2011.11.2679 |
0.378 |
|
| 2011 |
Hoernke M, Falenski JA, Schwieger C, Koksch B, Brezesinski G. Triggers for β-sheet formation at the hydrophobic-hydrophilic interface: high concentration, in-plane orientational order, and metal ion complexation. Langmuir : the Acs Journal of Surfaces and Colloids. 27: 14218-31. PMID 22011020 DOI: 10.1021/La203016Z |
0.386 |
|
| 2011 |
Brandenburg E, von Berlepsch H, Gerling UI, Böttcher C, Koksch B. Inhibition of amyloid aggregation by formation of helical assemblies. Chemistry (Weinheim An Der Bergstrasse, Germany). 17: 10651-61. PMID 22003512 DOI: 10.1002/Chem.201100670 |
0.402 |
|
| 2011 |
Hoernke M, Koksch B, Brezesinski G. Amyloidogenic peptides at hydrophobic-hydrophilic interfaces: coordination affinities and the chelate effect dictate the competitive binding of Cu2+ and Zn2+. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 12: 2225-9. PMID 21751332 DOI: 10.1002/Cphc.201100215 |
0.339 |
|
| 2011 |
Gerling UI, Brandenburg E, von Berlepsch H, Pagel K, Koksch B. Structure analysis of an amyloid-forming model peptide by a systematic glycine and proline scan. Biomacromolecules. 12: 2988-96. PMID 21726080 DOI: 10.1021/Bm200587M |
0.455 |
|
| 2011 |
Rezaei Araghi R, Baldauf C, Gerling UI, Cadicamo CD, Koksch B. A systematic study of fundamentals in α-helical coiled coil mimicry by alternating sequences of β- and γ-amino acids. Amino Acids. 41: 733-42. PMID 21638022 DOI: 10.1007/S00726-011-0941-Z |
0.456 |
|
| 2011 |
Araghi RR, Koksch B. A helix-forming αβγ-chimeric peptide with catalytic activity: a hybrid peptide ligase. Chemical Communications (Cambridge, England). 47: 3544-6. PMID 21327202 DOI: 10.1039/C0Cc03760E |
0.437 |
|
| 2011 |
Botev A, Munter LM, Wenzel R, Richter L, Althoff V, Ismer J, Gerling U, Weise C, Koksch B, Hildebrand PW, Bittl R, Multhaup G. The amyloid precursor protein C-terminal fragment C100 occurs in monomeric and dimeric stable conformations and binds γ-secretase modulators. Biochemistry. 50: 828-35. PMID 21186781 DOI: 10.1021/Bi1014002 |
0.363 |
|
| 2010 |
Wagner SC, Roskamp M, Pallerla M, Araghi RR, Schlecht S, Koksch B. Nanoparticle-induced folding and fibril formation of coiled-coil-based model peptides. Small (Weinheim An Der Bergstrasse, Germany). 6: 1321-8. PMID 20517875 DOI: 10.1002/Smll.200902067 |
0.426 |
|
| 2010 |
Falenski JA, Gerling UI, Koksch B. Multiple glycosylation of de novo designed alpha-helical coiled coil peptides. Bioorganic & Medicinal Chemistry. 18: 3703-6. PMID 20513637 DOI: 10.1016/J.Bmc.2010.03.061 |
0.404 |
|
| 2010 |
Ye S, Ann Berger A, Petzold D, Reimann O, Matt B, Koksch B. Chemical aminoacylation of tRNAs with fluorinated amino acids for in vitro protein mutagenesis. Beilstein Journal of Organic Chemistry. 6: 40. PMID 20502658 DOI: 10.3762/Bjoc.6.40 |
0.396 |
|
| 2010 |
Broncel M, Falenski JA, Wagner SC, Hackenberger CP, Koksch B. How post-translational modifications influence amyloid formation: a systematic study of phosphorylation and glycosylation in model peptides. Chemistry (Weinheim An Der Bergstrasse, Germany). 16: 7881-8. PMID 20491120 DOI: 10.1002/Chem.200902452 |
0.394 |
|
| 2010 |
Broncel M, Wagner SC, Paul K, Hackenberger CP, Koksch B. Towards understanding secondary structure transitions: phosphorylation and metal coordination in model peptides. Organic & Biomolecular Chemistry. 8: 2575-9. PMID 20485793 DOI: 10.1039/C001458C |
0.407 |
|
| 2010 |
Broncel M, Wagner SC, Hackenberger CP, Koksch B. Enzymatically triggered amyloid formation: an approach for studying peptide aggregation. Chemical Communications (Cambridge, England). 46: 3080-2. PMID 20424744 DOI: 10.1039/C001460E |
0.398 |
|
| 2010 |
Salwiczek M, Mikhailiuk PK, Afonin S, Komarov IV, Ulrich AS, Koksch B. Compatibility of the conformationally rigid CF3-Bpg side chain with the hydrophobic coiled-coil interface. Amino Acids. 39: 1589-93. PMID 20386938 DOI: 10.1007/S00726-010-0581-8 |
0.362 |
|
| 2010 |
von Berlepsch H, Brandenburg E, Koksch B, Böttcher C. Peptide adsorption to cyanine dye aggregates revealed by cryo-transmission electron microscopy. Langmuir : the Acs Journal of Surfaces and Colloids. 26: 11452-60. PMID 20364866 DOI: 10.1021/La100944D |
0.41 |
|
| 2010 |
Hoernke M, Koksch B, Brezesinski G. Influence of the hydrophobic interface and transition metal ions on the conformation of amyloidogenic model peptides. Biophysical Chemistry. 150: 64-72. PMID 20347516 DOI: 10.1016/J.Bpc.2010.02.014 |
0.4 |
|
| 2010 |
Vagt T, Nyakatura E, Salwiczek M, Jäckel C, Koksch B. Towards identifying preferred interaction partners of fluorinated amino acids within the hydrophobic environment of a dimeric coiled coil peptide. Organic & Biomolecular Chemistry. 8: 1382-6. PMID 20204211 DOI: 10.1039/B917205J |
0.455 |
|
| 2009 |
Weimann DP, Winkler HD, Falenski JA, Koksch B, Schalley CA. Highly dynamic motion of crown ethers along oligolysine peptide chains. Nature Chemistry. 1: 573-7. PMID 21378938 DOI: 10.1038/Nchem.352 |
0.385 |
|
| 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 |
0.397 |
|
| 2009 |
Becaud J, Mu L, Karramkam M, Schubiger PA, Ametamey SM, Graham K, Stellfeld T, Lehmann L, Borkowski S, Berndorff D, Dinkelborg L, Srinivasan A, Smits R, Koksch B. Direct one-step 18F-labeling of peptides via nucleophilic aromatic substitution. Bioconjugate Chemistry. 20: 2254-61. PMID 19921791 DOI: 10.1021/Bc900240Z |
0.301 |
|
| 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 |
0.433 |
|
| 2009 |
Vagt T, Jäckel C, Samsonov S, Teresa Pisabarro M, Koksch B. Selection of a buried salt bridge by phage display. Bioorganic & Medicinal Chemistry Letters. 19: 3924-7. PMID 19369078 DOI: 10.1016/J.Bmcl.2009.03.062 |
0.433 |
|
| 2009 |
Wagner SC, Roskamp M, Cölfen H, Böttcher C, Schlecht S, Koksch B. Switchable electrostatic interactions between gold nanoparticles and coiled coil peptides direct colloid assembly. Organic & Biomolecular Chemistry. 7: 46-51. PMID 19081944 DOI: 10.1039/B813429D |
0.365 |
|
| 2009 |
Weimann DP, Winkler HDF, Falenski JA, Koksch B, Schalley CA. Erratum: Highly dynamic motion of crown ethers along oligolysine peptide chains Nature Chemistry. 1: 668-668. DOI: 10.1038/Nchem.431 |
0.322 |
|
| 2009 |
Pagel K, Kupser P, Bierau F, Polfer NC, Steill JD, Oomens J, Meijer G, Koksch B, von Helden G. Gas-phase IR spectra of intact α-helical coiled coil protein complexes International Journal of Mass Spectrometry. 283: 161-168. DOI: 10.1016/J.Ijms.2009.02.026 |
0.403 |
|
| 2008 |
Pagel K, Wagner SC, Rezaei Araghi R, von Berlepsch H, Böttcher C, Koksch B. Intramolecular charge interactions as a tool to control the coiled-coil-to-amyloid transformation. Chemistry (Weinheim An Der Bergstrasse, Germany). 14: 11442-51. PMID 19016556 DOI: 10.1002/Chem.200801206 |
0.421 |
|
| 2008 |
Pagel K, Koksch B. Following polypeptide folding and assembly with conformational switches. Current Opinion in Chemical Biology. 12: 730-9. PMID 18840544 DOI: 10.1016/J.Cbpa.2008.09.005 |
0.388 |
|
| 2008 |
Smits R, Cadicamo CD, Burger K, Koksch B. Synthetic strategies to alpha-trifluoromethyl and alpha-difluoromethyl substituted alpha-amino acids. Chemical Society Reviews. 37: 1727-39. PMID 18648692 DOI: 10.1039/B800310F |
0.346 |
|
| 2008 |
Pagel K, Seri T, von Berlepsch H, Griebel J, Kirmse R, Böttcher C, Koksch B. How metal ions affect amyloid formation: Cu2+- and Zn2+-sensitive peptides. Chembiochem : a European Journal of Chemical Biology. 9: 531-6. PMID 18232039 DOI: 10.1002/Cbic.200700656 |
0.403 |
|
| 2007 |
Spengler J, Koksch B, Albericio F. Simple machine-assisted protocol for solid-phase synthesis of depsipeptides. Biopolymers. 88: 823-8. PMID 17922494 DOI: 10.1002/Bip.20858 |
0.311 |
|
| 2007 |
Jaeckel C, Koksch B. The Potential of Fluorine for Peptide and Protein Modification Cheminform. 38. DOI: 10.1002/chin.200720241 |
0.316 |
|
| 2007 |
Hakelberg M, Koksch B. Fluorine in Peptides: Coiled coil model systems as tools to evaluate the influence of fluorinated amino acids on structure and stability of peptides Chimica Oggi. 25: 48-53. |
0.323 |
|
| 2006 |
Smits R, Koksch B. How C(alpha)-Fluoroalkyl amino acids and peptides interact with enzymes: studies concerning the influence on proteolytic stability, enzymatic resolution and peptide coupling. Current Topics in Medicinal Chemistry. 6: 1483-98. PMID 16918464 DOI: 10.2174/156802606777951055 |
0.463 |
|
| 2006 |
Burger K, Hennig L, Tsouker P, Spengler J, Albericio F, Koksch B. Synthesis of alpha-trifluoromethyl alpha-amino acids with aromatic, heteroaromatic and ferrocenyl subunits in the side chain. Amino Acids. 31: 55-62. PMID 16715413 DOI: 10.1007/S00726-006-0322-1 |
0.321 |
|
| 2006 |
Vagt T, Zschörnig O, Huster D, Koksch B. Membrane binding and structure of de novo designed alpha-helical cationic coiled-coil-forming peptides. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 7: 1361-71. PMID 16680794 DOI: 10.1002/Cphc.200600010 |
0.421 |
|
| 2006 |
Pagel K, Wagner SC, Samedov K, von Berlepsch H, Böttcher C, Koksch B. Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Journal of the American Chemical Society. 128: 2196-7. PMID 16478157 DOI: 10.1021/Ja057450H |
0.411 |
|
| 2005 |
Pagel K, Vagt T, Koksch B. Directing the secondary structure of polypeptides at will: from helices to amyloids and back again? Organic & Biomolecular Chemistry. 3: 3843-50. PMID 16239998 DOI: 10.1039/B510098D |
0.406 |
|
| 2005 |
Piñeiro A, Villa A, Vagt T, Koksch B, Mark AE. A molecular dynamics study of the formation, stability, and oligomerization state of two designed coiled coils: possibilities and limitations. Biophysical Journal. 89: 3701-13. PMID 16150975 DOI: 10.1529/Biophysj.104.055590 |
0.369 |
|
| 2005 |
Dreier B, Fuller RP, Segal DJ, Lund CV, Blancafort P, Huber A, Koksch B, Barbas CF. Development of zinc finger domains for recognition of the 5'-CNN-3' family DNA sequences and their use in the construction of artificial transcription factors. The Journal of Biological Chemistry. 280: 35588-97. PMID 16107335 DOI: 10.1074/jbc.M506654200 |
0.695 |
|
| 2005 |
Pagel K, Vagt T, Kohajda T, Koksch B. From alpha-helix to beta-sheet--a reversible metal ion induced peptide secondary structure switch. Organic & Biomolecular Chemistry. 3: 2500-2. PMID 15999178 DOI: 10.1039/B505979H |
0.385 |
|
| 2005 |
Pagel K, Seeger K, Seiwert B, Villa A, Mark AE, Berger S, Koksch B. Advanced approaches for the characterization of a de novo designed antiparallel coiled coil peptide. Organic & Biomolecular Chemistry. 3: 1189-94. PMID 15785806 DOI: 10.1039/B418167K |
0.411 |
|
| 2005 |
Jäckel C, Koksch B. Cover Picture: Fluorine in Peptide Design and Protein Engineering (Eur. J. Org. Chem. 21/2005) European Journal of Organic Chemistry. 2005: 4471-4471. DOI: 10.1002/Ejoc.200590042 |
0.487 |
|
| 2005 |
Jäckel C, Koksch B. Fluorine in peptide design and protein engineering European Journal of Organic Chemistry. 4483-4503. DOI: 10.1002/Ejoc.200500205 |
0.443 |
|
| 2004 |
Jäckel C, Seufert W, Thust S, Koksch B. Evaluation of the molecular interactions of fluorinated amino acids with native polypeptides. Chembiochem : a European Journal of Chemical Biology. 5: 717-20. PMID 15122644 DOI: 10.1002/Cbic.200300840 |
0.34 |
|
| 2004 |
Koksch B, Dahl C, Radics G, Vocks A, Arnold K, Arnhold J, Sieler J, Burger K. Fluoro-modified chemotactic peptides: fMLF analogues. Journal of Peptide Science : An Official Publication of the European Peptide Society. 10: 67-81. PMID 14994985 DOI: 10.1002/Psc.515 |
0.41 |
|
| 2004 |
Osipov SN, Lange T, Tsouker P, Spengler J, Hennig L, Koksch B, Berger S, El-Kousy SM, Burger K. Hexafluoroacetone as a protecting and activating reagent: Synthesis of new types of fluoro-substituted α-amino, α-hydroxy and α-mercapto acids Synthesis. 1821-1829. DOI: 10.1055/S-2004-829131 |
0.38 |
|
| 2004 |
Thust S, Koksch B. Discovery of carboxypeptidase Y as a catalyst for the incorporation of sterically demanding α-fluoroalkyl amino acids into peptides Tetrahedron Letters. 45: 1163-1165. DOI: 10.1016/J.Tetlet.2003.12.007 |
0.377 |
|
| 2004 |
Koksch B, Quaedflieg PJLM, Michel T, Burger K, Broxterman QB, Schoemaker HE. Enzymatic resolution of Cα-fluoroalkyl substituted amino acids Tetrahedron Asymmetry. 15: 1401-1407. DOI: 10.1016/J.Tetasy.2004.02.027 |
0.325 |
|
| 2003 |
Thust S, Koksch B. Protease-catalyzed peptide synthesis for the site-specific incorporation of alpha-fluoroalkyl amino acids into peptides. The Journal of Organic Chemistry. 68: 2290-6. PMID 12636393 DOI: 10.1021/Jo020613P |
0.411 |
|
| 2003 |
Segal DJ, Beerli RR, Blancafort P, Dreier B, Effertz K, Huber A, Koksch B, Lund CV, Magnenat L, Valente D, Barbas CF. Evaluation of a modular strategy for the construction of novel polydactyl zinc finger DNA-binding proteins. Biochemistry. 42: 2137-48. PMID 12590603 DOI: 10.1021/Bi026806O |
0.7 |
|
| 2003 |
Radics G, Koksch B, El-Kousy SM, Spengler J, Burger K. L-α-Methylhomoisoserine: A New Versatile Building Block for Peptide and Depsipeptide Modification Synlett. 1826-1829. DOI: 10.1055/S-2003-41477 |
0.362 |
|
| 2002 |
Michel T, Koksch B, Osipov SN, Golubev AS, Sieler J, Burger K. Peptide synthesis with α-(difluoromethyl)-substituted α-amino acids Collection of Czechoslovak Chemical Communications. 67: 1533-1559. DOI: 10.1002/CHIN.200312177 |
0.379 |
|
| 2000 |
Koksch B, Mütze K, Osipov SN, Golubev AS, Burger K. Synthesis of highly fluorinated dipeptide building blocks Tetrahedron Letters. 41: 3825-3828. DOI: 10.1016/S0040-4039(00)00540-2 |
0.339 |
|
| 1999 |
Burger K, Kluge M, Fehn S, Koksch B, Hennig L, Müller G. A New Approach to Glycopeptides. Angewandte Chemie (International Ed. in English). 38: 1414-1416. PMID 29711583 DOI: 10.1002/(Sici)1521-3773(19990517)38:10<1414::Aid-Anie1414>3.0.Co;2-L |
0.309 |
|
| 1999 |
Bordusa F, Dahl C, Jakubke HD, Burger K, Koksch B. Synthesis of α-fluoroalkyl substituted peptides via enzymatic fragment condensation Tetrahedron Asymmetry. 10: 307-313. DOI: 10.1016/S0957-4166(98)00508-4 |
0.428 |
|
| 1998 |
Burger K, Mütze K, Hollweck W, Koksch B. Incorporation of α-trifluoromethyl substituted α-amino acids into C- and N-terminal position of peptides and peptide mimetics using multicomponent reactions Tetrahedron. 54: 5915-5928. DOI: 10.1016/S0040-4020(98)00291-9 |
0.431 |
|
| 1998 |
Koksch B, Sewald N. Modifizierung von Peptiden Nachrichten Aus Chemie, Technik Und Laboratorium. 46: 27-30. DOI: 10.1002/Nadc.19980460113 |
0.346 |
|
| 1997 |
Koksch B, Sewald N, Hofmann HJ, Burger K, Jakubke HD. Proteolytically stable peptides by incorporation of alpha-Tfm amino acids. Journal of Peptide Science : An Official Publication of the European Peptide Society. 3: 157-67. PMID 9230481 DOI: 10.1002/(SICI)1099-1387(199705)3:3<157::AID-PSC94>3.0.CO;2-W |
0.315 |
|
| 1997 |
Koksch B, Sewald N, Hofmann H, Burger K, Jakubke H. Proteolytically stable peptides by incorporation of α-Tfm amino acids Journal of Peptide Science. 3: 157-167. DOI: 10.1002/(Sici)1099-1387(199705)3:3<157::Aid-Psc94>3.0.Co;2-W |
0.453 |
|
| 1997 |
Koksch B, Jakubke HD, Hofmann HJ, Gussmann M, Burger K. Influence of α-fluoralkyl substituted amino acids on secondary structure and properties of peptides Amino Acids. 13: 73. |
0.329 |
|
| 1996 |
Koksch B, Sewald N, Burger K, Jakubke HD. Peptide modification by incorporation ofα-trifluoromethyl substituted amino acids. Amino Acids. 11: 425-34. PMID 24178726 DOI: 10.1007/Bf00807946 |
0.43 |
|
| 1996 |
Koksch B, Sewald N, Burger K, Jakubke HD. Peptide modification by incorporation of α-trifluoromethyl substituted amino acids Amino Acids. 11: 425-434. |
0.334 |
|
| 1996 |
Koksch B, Sewald N, Jakubke HD, Burger K. Synthesis and Incorporation of α-Trifluoromethyl-Substituted Amino Acids into Peptides Acs Symposium Series. 639: 42-58. |
0.327 |
|
| 1995 |
Sewald N, Hollweck W, Mütze K, Schierlinger C, Seymour LC, Gaa K, Burger K, Koksch B, Jakubke HD. Peptide modification by introduction ofα-trifluoromethyl substituted amino acids. Amino Acids. 8: 187-94. PMID 24186327 DOI: 10.1007/Bf00806491 |
0.436 |
|
| 1994 |
Burger K, Schierlinger C, Mütze K, Hollweck W, Koksch B. 2-Trifluormethyl-substituierte Aminosäuren, 20. N- und C-terminaler Einbau von α-Trifluormethyl-substituierten α-Aminosäuren in Azapeptide Liebigs Annalen Der Chemie. 1994: 407-413. DOI: 10.1002/Jlac.199419940414 |
0.327 |
|
| 1993 |
Burger K, M�tze K, Hollweck W, Koksch B, Kuhl P, Jakubke H, Riede J, Schier A. Untersuchungen zur proteasekatalysierten und chemischen Peptidbindungskn�pfung mit ?-trifluormethylsubstituierten ?-Aminos�uren Journal F�R Praktische Chemie/Chemiker-Zeitung. 335: 321-331. DOI: 10.1002/Prac.19933350404 |
0.379 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 2019 |
Yang V, Pedrosa SS, Fernandes R, Maurício AC, Koksch B, Gärtner F, Amorim I, Vale N. Synthesis of PEGylated methotrexate conjugated with a novel CPP6, in sillico structural insights and activity in MCF-7 cells Journal of Molecular Structure. 1192: 201-207. DOI: 10.1016/J.Molstruc.2019.04.118 |
0.297 |
|
| 2021 |
Huhmann S, Nyakatura EK, Rohrhofer A, Moschner J, Schmidt B, Eichler J, Roth C, Koksch B. Systematic Evaluation of Fluorination as Modification for Peptide-Based Fusion Inhibitors against HIV-1 Infection. Chembiochem : a European Journal of Chemical Biology. 22: 3443-3451. PMID 34605595 DOI: 10.1002/cbic.202100417 |
0.296 |
|
| 1996 |
Koksch B, Ullmann D, Jakubke HD, Burger K. Synthesis, structure and biological activity of α-trifluoromethyl-substituted thyreotropin releasing hormone Journal of Fluorine Chemistry. 80: 53-57. DOI: 10.1016/S0022-1139(96)03461-6 |
0.296 |
|
| 2003 |
Radics G, Pires R, Koksch B, El-Kousy SM, Burger K. New building blocks for peptide and depsipeptide synthesis: Hexafluoroacetone protected L-homoisoserine and D,L-homoisocysteine derivatives Tetrahedron Letters. 44: 1059-1062. DOI: 10.1016/S0040-4039(02)02712-0 |
0.296 |
|
| 2010 |
Kupser P, Pagel K, Oomens J, Polfer N, Koksch B, Meijer G, von Helden G. Amide-I and -II vibrations of the cyclic beta-sheet model peptide gramicidin S in the gas phase. Journal of the American Chemical Society. 132: 2085-93. PMID 20092340 DOI: 10.1021/Ja909842J |
0.293 |
|
| 2010 |
BURGER K, MUETZE K, HOLLWECK W, KOKSCH B, KUHL P, JAKUBKE H, RIEDE J, SCHIER A. ChemInform Abstract: Protease-Catalyzed and Chemical Peptide Bond Formation with α- Trifluoromethyl-Substituted α-Amino Acids. Cheminform. 25: no-no. DOI: 10.1002/chin.199421059 |
0.291 |
|
| 2009 |
Cadicamo CD, Asante V, Abu Ammar M, Borelli C, Korting HC, Koksch B. Investigation of the synthetic route to pepstatin analogues by SPPS using O-protected and O-unprotected statine as building blocks. Journal of Peptide Science : An Official Publication of the European Peptide Society. 15: 272-7. PMID 19189272 DOI: 10.1002/Psc.1111 |
0.291 |
|
| 2014 |
Do N, Weindl G, Grohmann L, Salwiczek M, Koksch B, Korting HC, Schäfer-Korting M. Cationic membrane-active peptides - anticancer and antifungal activity as well as penetration into human skin. Experimental Dermatology. 23: 326-31. PMID 24661024 DOI: 10.1111/Exd.12384 |
0.289 |
|
| 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 |
0.287 |
|
| 2015 |
Völler J, Biava H, Koksch B, Hildebrandt P, Budisa N. Orthogonal translation meets electron transfer: in vivo labeling of cytochrome c for probing local electric fields. Chembiochem : a European Journal of Chemical Biology. 16: 742-5. PMID 25706908 DOI: 10.1002/Cbic.201500022 |
0.287 |
|
| 2012 |
Fasting C, Schalley CA, Weber M, Seitz O, Hecht S, Koksch B, Dernedde J, Graf C, Knapp EW, Haag R. Multivalency as a chemical organization and action principle. Angewandte Chemie (International Ed. in English). 51: 10472-98. PMID 22952048 DOI: 10.1002/Anie.201201114 |
0.287 |
|
| 2009 |
Salwiczek M, Koksch B. Effects of fluorination on the folding kinetics of a heterodimeric coiled coil. Chembiochem : a European Journal of Chemical Biology. 10: 2867-70. PMID 19859931 DOI: 10.1002/Cbic.200900518 |
0.286 |
|
| 2017 |
Koksch B, Seeberger PH. Editorial overview: Synthetic biomolecules: Biopolymers. Current Opinion in Chemical Biology. 40: A4-A5. PMID 29156193 DOI: 10.1016/J.Cbpa.2017.10.028 |
0.284 |
|
| 2006 |
Jäckel C, Salwiczek M, Koksch B. Fluorine in a native protein environment--How the spatial demand and polarity of fluoroalkyl groups affect protein folding. Angewandte Chemie (International Ed. in English). 45: 4198-203. PMID 16688784 DOI: 10.1002/Anie.200504387 |
0.281 |
|
| 2006 |
Burger K, Hennig L, Tsouker P, Spengler J, Albericio F, Koksch B. Domino reactions with fluorinated five-membered heterocycles. alpha-Trifluoromethyl alpha-amino acids with unsaturated side-chains. Amino Acids. 31: 427-33. PMID 16715414 DOI: 10.1007/S00726-006-0321-2 |
0.278 |
|
| 2010 |
Rezaei Araghi R, Jäckel C, Cölfen H, Salwiczek M, Völkel A, Wagner SC, Wieczorek S, Baldauf C, Koksch B. A beta/gamma motif to mimic alpha-helical turns in proteins. Chembiochem : a European Journal of Chemical Biology. 11: 335-9. PMID 20039254 DOI: 10.1002/Cbic.200900700 |
0.277 |
|
| 2007 |
Scheike J, Baldauf C, Spengler J, Albericio F, Pisabarro M, Koksch B. Estersubstitutionen in α-helicalen Coiled-Coil-Peptiden: Effekt der Eliminierung von Wasserstoffbrücken auf die Struktur von Proteinen Angewandte Chemie. 119: 7912-7916. DOI: 10.1002/Ange.200702218 |
0.275 |
|
| 2011 |
Kashiwada A, Tsuboi M, Takamura N, Brandenburg E, Matsuda K, Koksch B. Design and characterization of endosomal-pH-responsive coiled coils for constructing an artificial membrane fusion system. Chemistry (Weinheim An Der Bergstrasse, Germany). 17: 6179-86. PMID 21503987 DOI: 10.1002/Chem.201003392 |
0.274 |
|
| 2004 |
Burger K, Kluge M, Koksch B, Fehn S, Böttcher C, Hennig L, Müller G. Hexafluoroacetone as protecting and activating reagent: A new approach to O-glycosides Heterocycles. 64: 143-152. DOI: 10.3987/Com-04-S(P)6 |
0.268 |
|
| 2021 |
Thota CK, Mikolajczak DJ, Roth C, Koksch B. Enhancing Antimicrobial Peptide Potency through Multivalent Presentation on Coiled-Coil Nanofibrils. Acs Medicinal Chemistry Letters. 12: 67-73. PMID 33488966 DOI: 10.1021/acsmedchemlett.0c00425 |
0.26 |
|
| 2009 |
Maisch D, Wadhwani P, Afonin S, Böttcher C, Koksch B, Ulrich AS. Chemical labeling strategy with (R)- and (S)-trifluoromethylalanine for solid state 19F NMR analysis of peptaibols in membranes. Journal of the American Chemical Society. 131: 15596-7. PMID 19827760 DOI: 10.1021/Ja9067595 |
0.26 |
|
| 2022 |
Hohmann T, Dyrks M, Chowdhary S, Weber M, Nguyen D, Moschner J, Koksch B. Gram-Scale Asymmetric Synthesis of Fluorinated Amino Acids Using a Chiral Nickel(II) Complex. The Journal of Organic Chemistry. PMID 35926217 DOI: 10.1021/acs.joc.2c00522 |
0.259 |
|
| 2016 |
Vukelic S, Koksch B, Seeberger PH, Gilmore K. A Sustainable, Semi-Continuous Flow Synthesis of Hydantoins. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 27338000 DOI: 10.1002/Chem.201602609 |
0.253 |
|
| 2021 |
Agostini F, Sinn L, Petras D, Schipp CJ, Kubyshkin V, Berger AA, Dorrestein PC, Rappsilber J, Budisa N, Koksch B. Multiomics Analysis Provides Insight into the Laboratory Evolution of toward the Metabolic Usage of Fluorinated Indoles. Acs Central Science. 7: 81-92. PMID 33532571 DOI: 10.1021/acscentsci.0c00679 |
0.248 |
|
| 2001 |
Moroni M, Koksch B, Osipov SN, Crucianelli M, Frigerio M, Bravo P, Burger K. First synthesis of totally orthogonal protected alpha-(trifluoromethyl)- and alpha-(difluoromethyl)arginines. The Journal of Organic Chemistry. 66: 130-3. PMID 11429889 DOI: 10.1021/Jo0009043 |
0.243 |
|
| 2022 |
Fernandes R, Chowdhary S, Mikula N, Saleh N, Kanevche K, von Berlepsch H, Hosogi N, Heberle J, Weber M, Böttcher C, Koksch B. Cyanine Dye Coupling Mediates Self-assembly of a pH Sensitive Peptide into Novel 3D Architectures. Angewandte Chemie (International Ed. in English). PMID 36161448 DOI: 10.1002/anie.202208647 |
0.243 |
|
| 2009 |
Salwiczek M, Vagt T, Koksch B. Application of Artificial Model Systems to Study the Interactions of Fluorinated Amino Acids within the Native Environment of Coiled Coil Proteins Fluorine in Medicinal Chemistry and Chemical Biology. 389-409. DOI: 10.1002/9781444312096.ch15 |
0.242 |
|
| 2014 |
Gilmore K, Vukeli? S, McQuade DT, Koksch B, Seeberger PH. Continuous reductions and reductive aminations using solid NaBH4 Organic Process Research and Development. 18: 1771-1776. DOI: 10.1021/Op500310S |
0.241 |
|
| 2017 |
Agostini F, Völler J, Koksch B, Acevedo‐Rocha CG, Kubyshkin V, Budisa N. Biokatalyse mit nicht‐natürlichen Aminosäuren: Enzymologie trifft Xenobiologie Angewandte Chemie. 129: 9810-9835. DOI: 10.1002/Ange.201610129 |
0.24 |
|
| 2017 |
Gomez JDC, Hagenbach A, Gerling-Driessen UIM, Koksch B, Beindorff N, Brenner W, Abram U. Thiourea derivatives as chelating agents for bioconjugation of rhenium and technetium. Dalton Transactions (Cambridge, England : 2003). PMID 28702615 DOI: 10.1039/C7Dt01834G |
0.238 |
|
| 2001 |
Osipov SN, Kobel'Kova NM, Kolomiets AF, Pumpor K, Koksch B, Burger K. α-fluoromethyl tryptophans via imino ene reaction Synlett. 1287-1289. DOI: 10.1055/S-2001-16054 |
0.237 |
|
| 2008 |
Piehl S, Heberer T, Balizs G, Scanlan TS, Smits R, Koksch B, Köhrle J. Thyronamines are isozyme-specific substrates of deiodinases. Endocrinology. 149: 3037-45. PMID 18339710 DOI: 10.1210/En.2007-1678 |
0.233 |
|
| 2023 |
Vale N, Ribeiro E, Cruz I, Stulberg V, Koksch B, Costa B. New Perspective for Using Antimicrobial and Cell-Penetrating Peptides to Increase Efficacy of Antineoplastic 5-FU in Cancer Cells. Journal of Functional Biomaterials. 14. PMID 38132819 DOI: 10.3390/jfb14120565 |
0.232 |
|
| 2024 |
Heinz F, Proksch J, Schmidt RF, Gradzielski M, Koksch B, Keller BG. How Chromophore Labels Shape the Structure and Dynamics of a Peptide Hydrogel. Biomacromolecules. PMID 38288602 DOI: 10.1021/acs.biomac.3c01225 |
0.23 |
|
| 2006 |
Jäckel C, Salwiczek M, Koksch B. Fluor in nativer Peptidumgebung – wie Raumanspruch und Polarität von Fluoralkylgruppen die Proteinfaltung beeinflussen Angewandte Chemie. 118: 4305-4309. DOI: 10.1002/Ange.200504387 |
0.23 |
|
| 2010 |
BURGER K, SCHIERLINGER C, MUETZE K, HOLLWECK W, KOKSCH B. ChemInform Abstract: 2-Trifluoromethyl-Substituted Amino Acids. Part 20. Incorporation of . alpha.-Trifluoromethyl-Substituted α-Amino Acids into the N- and C-Terminal Position of Azapeptides. Cheminform. 25: no-no. DOI: 10.1002/chin.199435246 |
0.228 |
|
| 2021 |
Berger AA, Leppkes J, Koksch B. Investigations from the Belly of the Beast: N-Terminally Labeled Incretin Peptides That Are Both Potent Receptor Agonists and Stable to Protease Digestion. Acs Central Science. 7: 400-402. PMID 33791422 DOI: 10.1021/acscentsci.1c00265 |
0.217 |
|
| 2008 |
Salwiczek M, Jäckel C, Koksch B. Molecular Interactions of Fluorinated Amino Acids in a Native Polypeptide Environment Fluorine and Health. 737-759. DOI: 10.1016/B978-0-444-53086-8.00017-5 |
0.215 |
|
| 2022 |
Ataka K, Drauschke J, Stulberg V, Koksch B, Heberle J. pH-induced insertion of pHLIP into a lipid bilayer: In-situ SEIRAS characterization of a folding intermediate at neutral pH. Biochimica Et Biophysica Acta. Biomembranes. 183873. PMID 35104491 DOI: 10.1016/j.bbamem.2022.183873 |
0.21 |
|
| 2020 |
Thota CK, Berger AA, Elomaa L, Nie C, Böttcher C, Koksch B. Coassembly Generates Peptide Hydrogel with Wound Dressing Material Properties. Acs Omega. 5: 8557-8563. PMID 32337417 DOI: 10.1021/acsomega.9b04371 |
0.208 |
|
| 2022 |
Wehrhan L, Leppkes J, Dimos N, Loll B, Koksch B, Keller BG. Water Network in the Binding Pocket of Fluorinated BPTI-Trypsin Complexes─Insights from Simulation and Experiment. The Journal of Physical Chemistry. B. PMID 36409613 DOI: 10.1021/acs.jpcb.2c05496 |
0.203 |
|
| 2012 |
Fasting C, Schalley CA, Weber M, Seitz O, Hecht S, Koksch B, Dernedde J, Graf C, Knapp E, Haag R. Multivalenz als chemisches Organisations- und Wirkprinzip Angewandte Chemie. 124: 10622-10650. DOI: 10.1002/Ange.201201114 |
0.201 |
|
| 2012 |
Fasting C, Schalley CA, Weber M, Seitz O, Hecht S, Koksch B, Dernedde J, Graf C, Knapp E, Haag R. Cover Picture: Multivalency as a Chemical Organization and Action Principle (Angew. Chem. Int. Ed. 42/2012) Angewandte Chemie International Edition. 51: 10419-10419. DOI: 10.1002/Anie.201207626 |
0.2 |
|
| 2018 |
Mikolajczak DJ, Koksch B. Peptide‐Gold Nanoparticle Conjugates as Sequential Cascade Catalysts Chemcatchem. 10: 4324-4328. DOI: 10.1002/Cctc.201800961 |
0.194 |
|
| 2023 |
Khan MF, Chowdhary S, Koksch B, Murphy CD. Biodegradation of Amphipathic Fluorinated Peptides Reveals a New Bacterial Defluorinating Activity and a New Source of Natural Organofluorine Compounds. Environmental Science & Technology. 57: 9762-9772. PMID 37341426 DOI: 10.1021/acs.est.3c01240 |
0.188 |
|
| 1999 |
Burger K, Kluge M, Fehn S, Koksch B, Hennig L, Müller G. Ein neuer Zugang zu Glycopeptiden Angewandte Chemie. 111: 1513-1515. DOI: 10.1002/(Sici)1521-3757(19990517)111:10<1513::Aid-Ange1513>3.0.Co;2-# |
0.187 |
|
| 2019 |
Hoffmann W, Langenhan J, Huhmann S, Moschner J, Chang R, Accorsi M, Seo J, Rademann J, Meijer G, Koksch B, Bowers MT, von Helden G, Pagel K. Eine intrinsische Hydrophobieskala für Aminosäuren und ihre Anwendung auf fluorierte Verbindungen Angewandte Chemie. 131: 8300-8304. DOI: 10.1002/Ange.201813954 |
0.184 |
|
| 2008 |
Smits R, Cadicamo CD, Burger K, Koksch B. ChemInform Abstract: Synthetic Strategies to α-Trifluoromethyl and α-Difluoromethyl Substituted α-Amino Acids Cheminform. 39. DOI: 10.1002/chin.200846241 |
0.177 |
|
| 2012 |
Fasting C, Schalley CA, Weber M, Seitz O, Hecht S, Koksch B, Dernedde J, Graf C, Knapp E, Haag R. Titelbild: Multivalenz als chemisches Organisations- und Wirkprinzip (Angew. Chem. 42/2012) Angewandte Chemie. 124: 10567-10567. DOI: 10.1002/Ange.201207626 |
0.175 |
|
| 2023 |
Giesecke Y, Asimi V, Stulberg V, Kleinau G, Scheerer P, Koksch B, Grötzinger C. Is the Neuropeptide PEN a Ligand of GPR83? International Journal of Molecular Sciences. 24. PMID 37894796 DOI: 10.3390/ijms242015117 |
0.159 |
|
| 2023 |
Almalla A, Elomaa L, Bechtella L, Daneshgar A, Yavvari P, Mahfouz Z, Tang P, Koksch B, Sauer I, Pagel K, Hillebrandt KH, Weinhart M. Papain-Based Solubilization of Decellularized Extracellular Matrix for the Preparation of Bioactive, Thermosensitive Pregels. Biomacromolecules. 24: 5620-5637. PMID 38009757 DOI: 10.1021/acs.biomac.3c00602 |
0.139 |
|
| 2023 |
Balke J, Díaz Gutiérrez P, Rafaluk-Mohr T, Proksch J, Koksch B, Alexiev U. Osmolytes Modulate Photoactivation of Phytochrome: Probing Protein Hydration. Molecules (Basel, Switzerland). 28. PMID 37630372 DOI: 10.3390/molecules28166121 |
0.137 |
|
| 2010 |
Moroni M, Koksch B, Osipov SN, Crucianelli M, Frigerio M, Bravo P, Burger K. ChemInform Abstract: First Synthesis of Totally Orthogonal Protected α-(Trifluoromethyl)- and α-(Difluoromethyl)arginines. Cheminform. 32: no-no. DOI: 10.1002/chin.200125170 |
0.122 |
|
| 1997 |
Koksch B, Überham U, Jakubke HD. Untersuchungen zur Stabilität von N-Benzyloxy-carbonyl-geschütztem α-Trifluormethylglycin-methylester Pharmazie. 52: 74-75. |
0.083 |
|
| 1999 |
Burger K, Kluge M, Fehn S, Koksch B, Hennig L, Muller G. A new approach to glycopeptide Angewandte Chemie - International Edition. 38: 1414-1416. DOI: 10.1002/(SICI)1521-3773(19990517)38:10<1414::AID-ANIE1414>3.0.CO;2-L |
0.054 |
|
| 2015 |
Ye S, Loll B, Berger AA, Mülow U, Alings C, Wahl MC, Koksch B. Fluorine teams up with water to restore inhibitor activity to mutant BPTI Chemical Science. 6: 5246-5254. DOI: 10.1039/c4sc03227f |
0.045 |
|
| 2020 |
Yang V, Gouveia MJ, Santos J, Koksch B, Amorim I, Gärtner F, Vale N. Breast cancer: insights in disease and influence of drug methotrexate. Rsc Medicinal Chemistry. 11: 646-664. PMID 33479665 DOI: 10.1039/d0md00051e |
0.039 |
|
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