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  Dr. JULIAN FUCHS  
 
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Title : Dr.
First Name : JULIAN
Last Name : FUCHS
University/Institution : University of Cambridge
Email ID : jf544@cam.ac.uk
City : Cambridge
Country : United Kingdom
State : Cambridgeshire
Zipcode : CB21EW
Department : Chemistry
Company Name :
Area of Research
Molecular Modeling, Structural Bioinformatics, Computer-aided Drug Design
Brief Description of Research Interest :
Julian received his MSc (2010) and PhD in Chemistry (2014) at University of Innsbruck, Austria, in the group of Prof. Klaus Liedl. His main research areas are biomolecular recognition processes and the thermodynamics governing their specificity. Thereby, structure-based approaches including extensive molecular dynamics simulations complement data-driven methods. During his studies Julian enjoyed research stays at Roche Basel, Switzerland, working on innovative methodologies in structure-based drug design, as well as a stay at University of Natural Resources and Life Sciences, Vienna, Austria, focussing on long range electrostatics schemes in computer simulations.

Julian joined the group of Prof. Glen at the Unilever Centre for Molecular Science Informatics at University of Cambridge in March 2014 as Research Associate. His current research employs structure-based design approaches aiming at targeting challenging protein-protein interfaces with peptides, peptidomimetics and small molecules.

Representative Publications :
see http://www-ucc.ch.cam.ac.uk/members/jf544 for a complete list:

"Heteroaromatic Pi-stacking Energy Landscapes", J Chem Inf Model 2014, 54(5), 1371-1379. "Matched Molecular Pair Analysis: Significance and the Impact of Experimental Uncertainty", J Med Chem 2014, 57(9), 3786-3802.

"Interface Dynamics Explain Assembly Dependency of Influenza Neuraminidase Catalytic Activity", J Biomol Struct Dyn 2014, accepted.

"Specificity of a Protein-Protein Interface: Local Dynamics Direct Substrate Recognition of Effector Caspases", Proteins 2014, 82(4), 546-555.

"Substrate Sequences Tell Similar Stories as Binding Cavities: Commentary", J Chem Inf Model 2013, 53(12), 3115-3116.

"Substrate-Driven Mapping of the Degradome by Comparison of Sequence Logos", PLoS Comput Biol 2013, 9(11), e1003353. "An Additional Substrate Binding Site in a Bacterial Phenylalanine Hydroxylase", Eur Biophys J 2013, 42(9), 691-708.

"Entropy from State Probabilities: Hydration Entropy of Cations", J Phys Chem B 2013, 117(21), 6466-6472. "Cleavage Entropy as a Quantitative Measure of Protease Specificity", PLoS Comput Biol 2013, 9(4), e1003007.

"First Insights into Structure-Function Relationships of Alkylglycerol Monooxygenase", Pteridines 2013, 24(1), 99-103. "Dynamic Regulation of Phenylalanine Hydroxylase by Simulated Redox Manipulation", PLoS ONE 2012, 7(12), e53005.

"Catalytic Residues and a Predicted Structure of Tetrahydrobiopterin-Dependent Alkylglycerol Monooxygenase", Biochem J 2012, 443(1), 277-284.

"Rationalizing Tight Ligand Binding Through Cooperative Interaction Networks", J Chem Inf Model 2011, 51(12), 3180-3198.

"Minor Groove Binders and Drugs Targeting Proteins Cover Complementary Regions in Chemical Shape Space", J Chem Inf Model 2011, 51(9), 2223-2232.

"Sequence Specific Positions of Water Molecules in the Interface between DNA and Minor Groove Binders", ChemPhysChem 2008, 9(18), 2766-2771.
 
     
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