Dagmar Ringe

发表

Proteins in organic solvents.

D. Ringe, C. Mattos, Carla Mattos, 2001, Current opinion in structural biology.

Werner-washburne " Sleeping Beauty " : Quiescence in Saccharomyces Cerevisiae †

G. C. Johnston, G. Petsko, D. Ringe, 2022 .

Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.

G A Petsko, G. Petsko, D. Ringe, 1999, Journal of molecular biology.

Preservation of forelimb function by UPF1 gene therapy in a rat model of TDP-43-induced motor paralysis

G. Petsko, L. Maquat, D. Ringe, 2014, Gene Therapy.

POVScript+: a program for model and data visualization using persistence of vision ray-tracing

Dagmar Ringe, Gregory A. Petsko, Timothy D. Fenn, 2003 .

Q&A: What are pharmacological chaperones and why are they interesting?

G. Petsko, Dagmar Ringe, 2009, Journal of biology.

Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability.

G A Petsko, G. Petsko, A. Szilágyi, 1997, Protein engineering.

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus.

G. Petsko, D. Ringe, S. Lovett, 1997, Journal of molecular biology.

Identification of the primary metal ion-activation sites of the diphtheria tox represser by X-ray crystallography and site-directed mutational analysis

D. Ringe, J. Murphy, Xiaochun Ding, 1996, Nature Structural Biology.

Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme.

G. Petsko, D. Ringe, D. Harrison, 1994, Biochemistry.

Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS

Jared R. Auclair, Joseph P. Salisbury, G. Petsko, 2024, PLoS biology.