S. Dames

发表

Structural basis for Hif-1α/CBP recognition in the cellular hypoxic response

H. Dyson, P. Wright, M. Martinez-Yamout, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Subtype-specific modulation of estrogen receptor-coactivator interaction by phosphorylation.

M. Scheepstra, L. Brunsveld, S. Dames, 2015, ACS chemical biology.

A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFB subunit cyclin T1.

S. Grzesiek, M. Geyer, C. Urbanke, 2010, Biochemistry.

Positional screening and NMR structure determination of side-chain-to-side-chain cyclized β3-peptides.

M. Geyer, L. Brunsveld, E. Vaz, 2012, Organic & biomolecular chemistry.

Structure and dynamics of a stabilized coiled-coil domain in the P-TEFb regulator Hexim1.

S. Grzesiek, M. Geyer, W. Blankenfeldt, 2011, Journal of molecular biology.

Insights into the Low Adhesive Capacity of Human T-cadherin from the NMR Structure of Its N-terminal Extracellular Domain*

S. Grzesiek, T. Ahrens, J. Engel, 2008, Journal of Biological Chemistry.

Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb

S. Grzesiek, B. Peterlin, M. Barborič, 2007, Proceedings of the National Academy of Sciences.

The FKBP-rapamycin binding domain of human TOR undergoes strong conformational changes in the presence of membrane mimetics with and without the regulator phosphatidic acid.

S. Dames, Nina M. Link, Diana C Rodriguez Camargo, 2012, Biochemistry.

A fast and simple method to prepare the FKBP-rapamycin binding domain of human target of rapamycin for NMR binding assays.

S. Dames, 2008, Protein expression and purification.

Structural analysis of the human Fibroblast Growth Factor Receptor 4 kinase Expression and purification of the human calcium channel ORAI 1

S. Dames, E. Lesca, 2014 .

Regulation of the Target of Rapamycin and Other Phosphatidylinositol 3-Kinase-Related Kinases by Membrane Targeting

S. Dames, Maristella De Cicco, M. S. Abd Rahim, 2015, Membranes.

NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding.

Viktor A. Jaravine, A. Alexandrescu, S. Dames, 1999, Journal of molecular biology.

Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease.

K. Beyreuther, H. Sticht, D. Willbold, 1995, European journal of biochemistry.

Structural Basis for the Association of the Redox-sensitive Target of Rapamycin FATC Domain with Membrane-mimetic Micelles*

S. Dames, 2009, The Journal of Biological Chemistry.

NMR– and MD simulation–based structural characterization of the membrane-associating FATC domain of ataxia telangiectasia mutated

D. Tieleman, S. Dames, Yevhen K. Cherniavskyi, 2019, The Journal of Biological Chemistry.

1H, 15N, and 13C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)

Anja Wacker, S. Dames, M. S. A. Rahim, 2018, Biomolecular NMR Assignments.

NMR analysis of the backbone dynamics of the small GTPase Rheb and its interaction with the regulatory protein FKBP38

S. Dames, L. Kiss, Maristella De Cicco, 2018, FEBS letters.

The Solution Structure of the FATC Domain of the Protein Kinase Target of Rapamycin Suggests a Role for Redox-dependent Structural and Cellular Stability*

S. Grzesiek, S. Dames, J. Mulet, 2005, Journal of Biological Chemistry.

A fragment of staphylococcal nuclease with an OB‐fold structure shows hydrogen‐exchange protection factors in the range reported for “molten globules”

A. Alexandrescu, S. Dames, R. Wiltscheck, 1996, Protein science : a publication of the Protein Society.

NMR- and Circular Dichroism-monitored Lipid Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidylinositol 3-Kinase-related Kinases (PIKK)*

S. Dames, Lisa A. M. Sommer, Martin P. C. Schaad, 2013, The Journal of Biological Chemistry.

Structural characterization of the antimicrobial peptides myxinidin and WMR in bacterial membrane mimetic micelles and bicelles

D. Tieleman, A. Falanga, S. Galdiero, 2021, bioRxiv.

Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin‐1

R. Kammerer, J. Engel, A. Alexandrescu, 1999, FEBS letters.

Characterization of the immersion properties of the peripheral membrane anchor of the FATC domain of the kinase "target of rapamycin" by NMR, oriented CD spectroscopy, and MD simulations.

D. Tieleman, A. Ulrich, W. F. D. Bennett, 2014, The journal of physical chemistry. B.

Characterization of residue‐dependent differences in the peripheral membrane association of the FATC domain of the kinase ‘target of rapamycin’ by NMR and CD spectroscopy

S. Dames, Lisa A. M. Sommer, 2014, FEBS letters.

Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids.

Martin Blackledge, Pau Bernado, S. Grzesiek, 2006, Journal of the American Chemical Society.

Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G*

Ville R. I. Kaila, S. Dames, M. Wittwer, 2016, The Journal of Biological Chemistry.

Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms

R. Kammerer, J. Engel, T. Schulthess, 1997, Protein science : a publication of the Protein Society.

NMR structure of a parallel homotrimeric coiled coil

Andrei T. Alexandrescu, R. Kammerer, J. Engel, 1998, Nature Structural &Molecular Biology.

Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C*

S. Grzesiek, H. Sass, M. Geyer, 2011, The Journal of Biological Chemistry.

Target of rapamycin FATC domain as a general membrane anchor: The FKBP‐12 like domain of FKBP38 as a case study

L. Milroy, S. Dames, Maristella De Cicco, 2018, Protein science : a publication of the Protein Society.

One short cysteine‐rich sequence pattern – two different disulfide‐bonded structures – a molecular dynamics simulation study

S. Dames, 2015, Journal of peptide science : an official publication of the European Peptide Society.

A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content.

Simon Bernèche, Olivier Bignucolo, S. Grzesiek, 2016, Journal of chemical theory and computation.

Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C*

S. Grzesiek, H. Sass, M. Geyer, 2011, The Journal of Biological Chemistry.