• Fiebig T, Cramer JT, Bethe A, Baruch P, Curth U, Fuhring JI, Buettner FFR, Vogel U, Schubert M, Fedorov R & Muhlenhoff M. (2020). Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A. Nat Commun 11, 4723. Doi: 10.1038/s41467-020-18464-y

• Giese S, Reindl T, Reinke PYA, Zattelman L, Fedorov R, Henn A, Taft MH & Manstein DJ. (2020). Mechanochemical properties of human myosin 1C are modulated by isoform-specific differences in the N-terminal extension. J Biol Chem. Doi: 10.1074/jbc.RA120.015187

• Prakash O, Führing J, Post J, Shepherd SM, Eadsforth TC, Gray D, Fedorov R and Routier FH. Identification of Leishmania major UDP-Sugar Pyrophosphorylase Inhibitors Using Biosensor-Based Small Molecule Fragment Library Screening. (2019) Molecules, 24(5): 996. DOI:10.3390/molecules24050996

• Cramer JT, Führing JI, Baruch P, Brütting C, Knölker H-J, Gerardy-Schahn R, and Fedorov R. Decoding Allosteric Networks in Biocatalysts: Rational Approach to Therapies and Biotechnologies. (2018) ACS Catalysis. 8:2683-2692. DOI: 10.1021/acscatal.7b03714

• Hirschmann F, Krause F, Baruch P, Chizhov I, Mueller JW, Manstein DJ, Papenbrock J,  Fedorov R. Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism. (2017) Sci. Rep. 7(1):4160.
   
• Lohöfener J, Steinke N, Kay-Fedorov P, Baruch P, Nikulin A, Tishchenko S, Manstein DJ, and Fedorov R. The activation mechanism of 2’-5’-oligoadenylate synthetase gives new insights into OAS/cGAS triggers of innate immunity. (2015) Structure. 23(5):851-862. DOI: 10.1016/j.str.2015.03.012.
   
• Führing JI, Cramer JT, Schneider J, Baruch P, Gerardy-Schahn R, and Fedorov R. A Quaternary Mechanism Enables the Complex Biological Functions of Octameric Human UDP-glucose Pyrophosphorylase, a Key Enzyme in Cell Metabolism. (2015) Sci. Rep. 5, 9618; DOI:10.1038/srep09618.
   
• Rai A, Fedorov R, & Manstein DJ. Expression, purification and crystallization of a dye-decolourizing peroxidase from Dictyostelium discoideum. (2014). Acta Cryst. F70:252-255.
   
• Mikhaylina AO, Kostareva OS, Sarskikh AV, Fedorov RV, Piendl W, Garber MB, Tishchenko SV. Investigation of the Regulatory Function of Archaeal Ribosomal Protein L4. (2014) Biochemistry (Moscow). 79(1):69-76.
   
• Führing J, Cramer JT, Routier FH, Lamerz A-C, Baruch P, Gerardy-Schahn R and Fedorov R. Catalytic mechanism and allosteric regulation of UDP-glucose pyrophosphorylase from Leishmania major. (2013) ACS Catalysis. 3:2976-2985.
   
• Hellert J, Weidner-Glunde M, Krausze J, Richter U, Adler H, Fedorov R, Pietrek M, Rückert J,  Ritter C, Schulz TF, Lührs T. A Structural Basis for BRD2/4-Mediated Host Chromatin Interaction and Oligomer Assembly of Kaposi Sarcoma-Associated Herpesvirus and Murine Gammaherpesvirus LANA Proteins. (2013) PLoS Pathog 9(10): e1003640. doi:10.1371/journal.ppat.1003640
   
• Führing J, Damerow S, Fedorov R, Schneider J, Münster-Kühnel AK, Gerardy-Schahn R. Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase. (2013) Glycobiology. 23(4):426-37.
• Heissler SM, Selvadurai J, Bond LM, Fedorov R, Kendrick-Jones J, Buss F, Manstein DJ. Kinetic properties and small-molecular inhibition of human myosin-6. (2012) FEBS Lett. 586(19):3208-14.
   
• Preller M, Bauer S, Adamek N, Fujita-Becker S, Fedorov R, Geeves MA, Manstein DJ. Structural basis for the allosteric interference of myosin function by reactive thiol region mutations G680A and G680V. (2011) J. Biol. Chem. 286(40), 35051-35060.
   
• Chinthalapudi K, Taft MH, Martin R, Heissler SM, Preller M, Hartmann FK, Brandstaetter H, Kendrick-Jones J, Tsiavaliaris G, Gutzeit HO, Fedorov R, Buss F, Knölker HJ, Coluccio LM, Manstein DJ. Mechanism and Specificity of Pentachloropseudilin-mediated Inhibition of Myosin Motor Activity. (2011) J. Biol. Chem. 286(34), 29700-8.
   
• Naue N, Fedorov R, Pich A, Manstein DJ, Curth U. Site-directed mutagenesis of the χ subunit of DNA polymerase III and single-stranded DNA-binding protein of E. coli reveals key residues for their interaction. (2011) Nucleic Acids Res. 39(4), 1398-407.
• Forke R, Gruner KK, Knott KE, Auschill S, Agarwal S, Martin R, Böhl M, Richter S, Tsiavaliaris G, Fedorov R, Manstein DJ, Gutzeit HO, and Knölker H-J. Total synthesis of biologically active alkaloids using transition metals. (2010) Pure Appl. Chem., 82(11), 1975-1991.
   
• Amrute-Nayak M, Diensthuber RP, Steffen W, Kathmann D, Hartmann FK, Fedorov R, Urbanke C, Manstein DJ, Brenner B, and Tsiavaliaris G. Targeted optimization of a protein nanomachine for operation in biohybrid devices. (2010) Angew. Chem. Int. Ed. 49, 312-316.
   
• Martin R, Agarwal S, Jäger A, Böhl M, Richter S, Tsiavaliaris G, Fedorov R, Manstein DJ, Gutzeit HO, Knölker H-J. Specific Inhibitors of Myosin ATPase via Silver-Catalyzed Synthesis of Pyrroles. The Chemistry and Biological Activity of Synthetic and Natural Compounds – Modern Aspects of Chemistry of Heterocycles. (2010) V.G. Kartsev, Ed.; ICSPF Press, Moscow; 1, 110-117. 
• Martin R, Jäger A, Böhl M, Richter S, Fedorov R, Manstein DJ, Gutzeit HO, and Knölker H-J. Total Synthesis of Pentabromo- and Pentachloropseudilin, and Synthetic Analogues—Allosteric Inhibitors of Myosin ATPase. (2009) Angew. Chem. Int. Ed. 48, 8042 –8046.
   
• Martin R, Jäger A, Böhl M, Richter S, Fedorov R, Manstein DJ, Gutzeit HO, and Knölker H-J. Total Synthesis of Pentabromo- and Pentachloropseudilin, and Synthetic Analogues—Allosteric Inhibitors of Myosin ATPase. (2009) Angew. Chem. 121, 8186 –8190.
   
• Fedorov R, Böhl M, Tsiavaliaris G, Hartmann FK, Taft MH, Baruch P, Brenner B, Martin R, Knölker H-J, Gutzeit HO & Manstein DJ. The mechanism of pentabromopseudilin inhibition of myosin motor activity. (2009) Nature Structural & Molecular Biology, 16, 80-88.
   
• Stolboushkina E, Nikonov S, Nikulin A, Bläsi U, Manstein DJ, Fedorov R, Garber M, and Nikonov O. Crystal Structure of the Intact Archaeal Translation Initiation Factor 2 Demonstrates Very High Conformational Flexibility in the a- and b- Subunits. (2008) J. Mol. Biol. 382, 680-691.
   
• Witte G, Fedorov R and Ute Curth U. Biophysical analysis of Thermus aquaticus single-stranded DNA binding protein. (2008) Biophys. J., 94(6), 2269-2279.
   
• Nikonov O, Stolboushkina E, Nikulin A, Hasenöhrl D, Bläsi U, Manstein DJ, Fedorov R, Garber M and Nikonov S. New insights into the interactions of the translation initiation factor 2 from archaea with guanine nucleotides and initiator tRNA. (2007) J. Mol. Biol. 373(2), 328-336.
   
• Fedorov R, Witte G, Urbanke C, Manstein DJ, Curth U. 3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins. (2006) Nucleic Acids Res 34, 6708-6717.
   
• Domratcheva T, Fedorov R, Schlichting I. Analysis of the Primary Photocycle Reactions Occurring in the Light, Oxygen, and Voltage Blue-Light Receptor by Multiconfigurational Quantum-Chemical Methods. (2006) J. Chem. Theory Comput.; 2(6), 1565 – 1574.
   
• Matter HH, Arun Kumar HS, Fedorov R, Frey A, Kotsonis P, Hartmann E, Fröhlich LG, Reif A, Pfleiderer W, Scheurer P, Ghosh DK, Schlichting I and Schmidt HHHW. Structural Analysis of Isoform-Specific Inhibitors Targeting the Tetrahydrobiopterin Binding Site of Human Nitric Oxide Synthases. (2005) J. Med. Chem., 48(15), 4783-4792.
   
• Geeves MA, Fedorov R and Manstein DJ. Molecular mechanism of actomyosin-based motility. (2005) CMLS, Cell. Mol. Life Sci. 62(13), 1462-1477.
   
• Fedorov R, Vasan R, Ghosh DK and Ilme Schlichting. Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specificity and inhibitor design. (2004) PNAS  101, 5892-5897.
   
• Kottke T, Dick B, Fedorov R, Schlichting I, Deutzmannm R, Hegemann P. Irreversible Photoreduction of Flavin in a Mutated Phot-LOV1 Domain. (2003) Biochemistry  42, 9854-9862.
   
• Fedorov R, Hartmann E, Ghosh DK and Schlichting I. Structural basis for the specificity of the nitric oxide synthase inhibitors W1400 and Nw-propyl-L-Arg for the inducible and neuronal isoforms. (2003) J. Biol. Chem., 278, 45818-45825.
   
• Fedorov R, Schlichting I, Hartmann E, Domratcheva T, Fuhrmann M and Hegemann P. Crystal structures and molecular mechanism of a light induced signaling switch: the Phot-LOV1 domain from Chlamydomonas reinhardtii. (2003) Biophysical J. 84, 2474-2482.
   
• Fedorov R, Ghosh DK and Schlichting I. Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase – structural models of the short-lived oxygen complexes. (2003) Archives of Biochemistry and Biophysics. 409, 25-31.
   
• Nevskaya N, Tishchenko S, Paveliev M, Smolinskaya Y, Fedorov R, Piendl W, Nakamura Y, Toyoda T, Garber M and Nikonov S. Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface. (2002) Acta Cryst. D58, 1023-1029.
   
• Fedorov R, Meshcheryakov V, Gongadze G, Fomenkova N, Nevskaya N, Selmer M, Laurberg M, Kristensen O, Al-Karadaghi S, Liljas A, Garber M and Nikonov S. Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins. (2001) Acta Cryst. D57, 968-976.
   
• Davydova N, Fedorov R, Streltsov V, Liljas A and Garber M. Crystals of a mutant form of ribosomal protein L22 rendering bacterial ribosomes resistant to erythromycin. (2001) Acta Cryst. D57, 1150-1152.
• Gongadze GM, Perederina AA, Meshcheryakov VA, Fedorov RV, Moskalenko SE, Rak AV, Serganov AA, Shcherbakov DV, Nikonov SV and Garber MB. The Thermus thermophilus 5S rRNA-protein complex: Identification of specific binding sites for proteins L5 and L18 in the 5S rRNA. (2001) Molecular Biology (Moscow) 35, 610-616.
   
• Rak A, Fedorov R, Alexandrov K, Albert S, Goody RS, Gallwitz D & Scheidig AJ Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins. (2000) The EMBO Journal  19(19), 5105-5113.
• Nevskaya N, Tishchenko S, Fedorov R, Al-Karadaghi S, Liljas A, Kraft A, Piendl W, Garber M and Nikonov S. Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family. (2000) Structure with Folding & Design  8(4), 363-371.
   
• Fedorov R, Nevskaya N, Khairullina A, Tishchenko S, Mikhailov A, Garber M and Nikonov S. Structure of ribosomal protein L30 from Thermus thermophilus at 1.9A resolution: conformational flexibility of the molecule. (1999) Acta Cryst. D55, 1827-1833.
   
• Nikonov SV, Nevskaya NA, Fomenkova NP, Nikulin AD, Fedorov RV, Eliseikina IA, Tishchenko SV, Garber MB. Structural Investigations of Bacterial Ribosomal Proteins. (1999) Surface. X-Ray, Synchrotron and Neutron Studies  2, 6-9.
   
• Nikonov SV, Nevskaya NA, Fedorov RV, Khairullina AR, Tishchenko SV, Nikulin AD and Garber MB. Structural Studies of Ribosomal Proteins. (1998) Biol. Chem. 379, 795-805.
• Garber M, Davydova N, Fedorov R, Gongadze G, Kalinin A, Meshcheryakov V, Moskalenko S, Mudrik E, Nevskaya N, Nikonov S, Nikulin A, Peredelina A, Rak A, Serganov A, Shcherbakov D, Tin O, Tishchenko S, Vassilieva J, Kraft A, Piendl W, Ehresmann C, Ehresmann B, Allard P, Helgstrand M, Hard T. Ribosomal proteins: Crystallization, crystallographic and solution studies. (1998) The Proceedings of the workshop on "Structure Research of the Ribosome and its functional complexes", GKSS Research Center Greesthacht GmbH, Greesthacht, Germany, 9-11.09.1998, pp.47-51.
   
• Nikonov SV, Fomenkova NP, Nikulin AD, Fedorov RV, Nevskaya NA. The ribosome structure: RNA-protein and protein-protein interactions. (1998)  Molecular Biology (Moscow) 32 (5), 773-781.
   
• Fedorov RV. Quasi-Degenerate Perturbation Theory for Intermediate Hamiltonians in application to the calculations of low-lying electronic states of Fe, Ni and Ti. (1997) Vestnik MGU, series 2, Chemistry  38 (1), 17-20.

Dietmar J. Manstein, Roman Fedorov, Georgios Tsiavaliaris, Hans-Joachim Knölker, René Martin, Juliane Kirst, Herwig O. Gutzeit, Markus Böhl, Marcus Furch. „Means for treating myosin-related diseases“ (WO/2009/065600), International Application No.: PCT/EP2008/009891; Publication Date: 28.05.2008; International Filing Date: 21.11. 2008.