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Christina Kiel
Christina Kiel
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Zweryfikowany adres z unipv.it
Tytuł
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Cytowane przez
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Insights into protein–protein binding by binding free energy calculation and free energy decomposition for the Ras–Raf and Ras–RalGDS complexes
H Gohlke, C Kiel, DA Case
Journal of molecular biology 330 (4), 891-913, 2003
12812003
Network pharmacology: curing causal mechanisms instead of treating symptoms
C Nogales, ZM Mamdouh, M List, C Kiel, AI Casas, HHHW Schmidt
Trends in pharmacological sciences, 2021
3712021
Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network
G Markson, C Kiel, R Hyde, S Brown, P Charalabous, A Bremm, J Semple, ...
Genome research 19 (10), 1905-1911, 2009
2122009
Recognizing and defining true Ras binding domains I: biochemical analysis
S Wohlgemuth, C Kiel, A Krämer, L Serrano, F Wittinghofer, C Herrmann
Journal of molecular biology 348 (3), 741-758, 2005
2102005
Engineering signal transduction pathways
C Kiel, E Yus, L Serrano
Cell 140 (1), 33-47, 2010
1572010
Recognizing and defining true Ras binding domains II: in silico prediction based on homology modelling and energy calculations
C Kiel, S Wohlgemuth, F Rousseau, J Schymkowitz, J Ferkinghoff-Borg, ...
Journal of molecular biology 348 (3), 759-775, 2005
1322005
Electrostatically optimized Ras-binding Ral guanine dissociation stimulator mutants increase the rate of association by stabilizing the encounter complex
C Kiel, T Selzer, Y Shaul, G Schreiber, C Herrmann
Proceedings of the National Academy of Sciences 101 (25), 9223-9228, 2004
1312004
Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain
G Piccoli, F Onofri, MD Cirnaru, CJO Kaiser, P Jagtap, A Kastenmüller, ...
Molecular and cellular biology 34 (12), 2147-2161, 2014
1222014
Analysis of disease-linked rhodopsin mutations based on structure, function, and protein stability calculations
EP Rakoczy, C Kiel, R McKeone, F Stricher, L Serrano
Journal of molecular biology 405 (2), 584-606, 2011
1122011
A detailed thermodynamic analysis of ras/effector complex interfaces
C Kiel, L Serrano, C Herrmann
Journal of molecular biology 340 (5), 1039-1058, 2004
1092004
Analyzing protein interaction networks using structural information
C Kiel, P Beltrao, L Serrano
Annu. Rev. Biochem. 77, 415-441, 2008
1042008
The ubiquitin domain superfold: structure-based sequence alignments and characterization of binding epitopes
C Kiel, L Serrano
Journal of molecular biology 355 (4), 821-844, 2006
1012006
Structural fingerprints of the Ras-GTPase activating proteins neurofibromin and p120GAP
MR Ahmadian, C Kiel, P Stege, K Scheffzek
Journal of molecular biology 329 (4), 699-710, 2003
812003
Cell type–specific importance of Ras–c-Raf complex association rate constants for MAPK signaling
C Kiel, L Serrano
Science signaling 2 (81), ra38-ra38, 2009
782009
Structure‐energy‐based predictions and network modelling of RAS opathy and cancer missense mutations
C Kiel, L Serrano
Molecular systems biology 10 (5), 727, 2014
752014
Structures in systems biology
P Beltrao, C Kiel, L Serrano
Current opinion in structural biology 17 (3), 378-384, 2007
732007
Integration of protein abundance and structure data reveals competition in the ErbB signaling network
C Kiel, E Verschueren, JS Yang, L Serrano
Science signaling 6 (306), ra109-ra109, 2013
572013
Improved binding of Raf to Ras· GDP is correlated with biological activity
C Kiel, D Filchtinski, M Spoerner, G Schreiber, HR Kalbitzer, C Herrmann
Journal of Biological Chemistry 284 (46), 31893-31902, 2009
532009
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRASG13D
SA Kennedy, MA Jarboui, S Srihari, C Raso, K Bryan, L Dernayka, ...
Nature communications 11 (1), 1-14, 2020
522020
The Activation of RalGDS Can Be Achieved Independently of Its Ras Binding Domain: IMPLICATIONS OF AN ACTIVATION MECHANISM IN Ras EFFECTOR SPECIFICITY AND SIGNAL DISTRIBUTION* 210
T Linnemann, C Kiel, P Herter, C Herrmann
Journal of Biological Chemistry 277 (10), 7831-7837, 2002
522002
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