2019 - German National Academy of Sciences Leopoldina - Deutsche Akademie der Naturforscher Leopoldina – Nationale Akademie der Wissenschaften Biochemistry and Biophysics
2014 - Member of the National Academy of Sciences
2012 - Fellow of the American Academy of Arts and Sciences
Member of the European Molecular Biology Organization (EMBO)
The scientist’s investigation covers issues in Biochemistry, Cell biology, Ubiquitin, Ubiquitin ligase and NEDD8. Many of her studies involve connections with topics such as Biophysics and Biochemistry. Her work carried out in the field of Cell biology brings together such families of science as Postsynaptic potential, Transcription factor, Cellular differentiation and Cyclin.
Her Ubiquitin research includes elements of Proteasome, DNA ligase, Enzyme and Phosphorylation. Her NEDD8 study combines topics in areas such as Protein neddylation and Pevonedistat. Her CUL1 research includes themes of SCF complex, SCF ubiquitin ligase complex and S-Phase Kinase-Associated Proteins.
Her scientific interests lie mostly in Cell biology, Ubiquitin, Ubiquitin ligase, Biochemistry and NEDD8. Her Cell biology research is multidisciplinary, incorporating elements of Autophagy, F-box protein, DNA ligase, Enzyme and Anaphase-promoting complex. Brenda A. Schulman focuses mostly in the field of Ubiquitin, narrowing it down to topics relating to Protein subunit and, in certain cases, Protein engineering.
Her study looks at the relationship between Ubiquitin ligase and topics such as Computational biology, which overlap with Proteomics. Her Biochemistry study frequently involves adjacent topics like Biophysics. Her NEDD8 study integrates concerns from other disciplines, such as Protein neddylation, Stereochemistry, Cullin, Neddylation and Pevonedistat.
Cell biology, Ubiquitin, Ubiquitin ligase, Enzyme and DNA ligase are her primary areas of study. Her research integrates issues of Autophagy, ATG8, Receptor and NEDD8 in her study of Cell biology. The various areas that Brenda A. Schulman examines in her Ubiquitin study include Biophysics and Active site.
Her Ubiquitin ligase study combines topics in areas such as Protein subunit, Computational biology, Substrate and Binding site. Her biological study deals with issues like Protein structure, which deal with fields such as Mutation. The concepts of her Cullin study are interwoven with issues in Neddylation and CUL1.
Her primary areas of investigation include Cell biology, Ubiquitin, DNA ligase, Cullin and Ubiquitin ligase. Her Cell biology study integrates concerns from other disciplines, such as ATG8, Autophagy, ISG15 and CUL5. Her research in Ubiquitin intersects with topics in Regulator, Enzyme, Active site and Quantitative proteomics.
Her DNA ligase research includes elements of Protein structure and Saccharomyces cerevisiae. Her Cullin study frequently draws connections between adjacent fields such as NEDD8. Her work deals with themes such as Suppressor and Proteostasis, which intersect with Ubiquitin ligase.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.
Ning Zheng;Brenda A. Schulman;Brenda A. Schulman;Langzhou Song;Julie J. Miller.
Nature (2002)
Deletion of IKZF1 and prognosis in acute lymphoblastic leukemia.
Charles G Mullighan;Xiaoping Su;Jinghui Zhang;Ina Radtke.
The New England Journal of Medicine (2009)
Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
Brenda A. Schulman;J. Wade Harper.
Nature Reviews Molecular Cell Biology (2009)
Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation
David M. Duda;Laura A. Borg;Daniel C. Scott;Harold W. Hunt.
Cell (2008)
JAK mutations in high-risk childhood acute lymphoblastic leukemia.
Charles G. Mullighan;Jinghui Zhang;Richard C. Harvey;J. Racquel Collins-Underwood.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex.
Brenda A. Schulman;Andrea C. Carrano;Philip D. Jeffrey;Zachary Bowen.
Nature (2000)
Structure of a β-TrCP1-Skp1-β-Catenin Complex: Destruction Motif Binding and Lysine Specificity of the SCFβ-TrCP1 Ubiquitin Ligase
Geng Wu;Guozhou Xu;Brenda A. Schulman;Philip D. Jeffrey.
Molecular Cell (2003)
Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis
Alban Ordureau;Shireen A. Sarraf;David M. Duda;Jin-Mi Heo.
Molecular Cell (2014)
Parkin Is a Component of an SCF-like Ubiquitin Ligase Complex and Protects Postmitotic Neurons from Kainate Excitotoxicity
John F. Staropoli;Caroline McDermott;Cécile Martinat;Brenda Schulman.
Neuron (2003)
A Calcium-Regulated MEF2 Sumoylation Switch Controls Postsynaptic Differentiation
Aryaman Shalizi;Brice Gaudillière;Zengqiang Yuan;Judith Stegmüller.
Science (2006)
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