His primary scientific interests are in Biochemistry, Protein structure, Computational biology, Molecular biology and Signal transduction. Alex N. Bullock has included themes like Protein hydroxylation, Hypoxia-Inducible Factor 1, Function and Protein folding in his Protein structure study. His Computational biology research is multidisciplinary, relying on both Proteasome, Ubiquitin, Ubiquitin-Protein Ligases and Protein–protein interaction.
The various areas that he examines in his Protein–protein interaction study include Proteins metabolism and In vitro binding. His research in Molecular biology intersects with topics in Cyclin A2, Cyclin E, Cyclin A, CDK-activating kinase and Cyclin D. Alex N. Bullock combines subjects such as Bisindolylmaleimide, Cyclin-dependent kinase 9, Murine leukemia virus, Kinase and Enzyme inhibitor with his study of Signal transduction.
Alex N. Bullock focuses on Crystal structure, Crystallography, Kinase, Cell biology and Domain. His studies deal with areas such as Resolution, Stereochemistry, Protein kinase domain and Peptide as well as Crystal structure. His study looks at the relationship between Peptide and topics such as PIM1, which overlap with Serine/threonine-specific protein kinase.
As a member of one scientific family, he mostly works in the field of Kinase, focusing on Cancer research and, on occasion, Mutant. His research integrates issues of BMPR2, Protein structure and Ubiquitin, Ubiquitin ligase in his study of Cell biology. His work is connected to Plasma protein binding and Binding site, as a part of Biochemistry.
Alex N. Bullock mainly investigates Kinase, Crystal structure, Cell biology, Crystallography and Receptor. His studies in Kinase integrate themes in fields like Bone morphogenetic protein, ACVR1, FKBP, Signal transduction and Stereochemistry. His work deals with themes such as Cancer research, Mutant, Neuroscience and Brain tumor childhood, which intersect with ACVR1.
His research in Cell biology is mostly concerned with Phosphorylation. His Protein kinase domain research incorporates elements of BMPR2, Missense mutation, Loss function, Indene and Protein structure. His Degron study combines topics from a wide range of disciplines, such as Computational biology and Peptide.
The scientist’s investigation covers issues in Kinase, Cancer research, Receptor, Cell biology and Ubiquitin. His Kinase study integrates concerns from other disciplines, such as Alanine, Stereochemistry, Serine and Potassium channel. His Cancer research study also includes fields such as
Alex N. Bullock focuses mostly in the field of Receptor, narrowing it down to topics relating to Signal transduction and, in certain cases, Function, Transforming growth factor and Phosphorylation. His Cell biology research includes themes of Nod, Nucleotide and ADME. In the subject of general Ubiquitin, his work in Ubiquitin ligase is often linked to Architecture domain and Toolbox, thereby combining diverse domains of study.
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Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family
Kirsty S. Hewitson;Luke A. McNeill;Madeline V. Riordan;Ya-Min Tian.
Journal of Biological Chemistry (2002)
Rescuing the function of mutant p53
Alex N. Bullock;Alan R. Fersht.
Nature Reviews Cancer (2001)
Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy
Alex N Bullock;Julia Henckel;Alan R Fersht.
Thermodynamic stability of wild-type and mutant p53 core domain
Alex N. Bullock;Julia Henckel;Brian S. DeDecker;Christopher M. Johnson.
Proceedings of the National Academy of Sciences of the United States of America (1997)
Recurrent activating ACVR1 mutations in diffuse intrinsic pontine glioma
Kathryn R Taylor;Alan Mackay;Nathalène Truffaux;Yaron S Butterfield.
Nature Genetics (2014)
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases
Oleg Fedorov;Brian Marsden;Vanda Pogacic;Peter Rellos.
Proceedings of the National Academy of Sciences of the United States of America (2007)
Computational redesign of protein-protein interaction specificity.
Tanja Kortemme;Lukasz A Joachimiak;Lukasz A Joachimiak;Alex N Bullock;Alex N Bullock;Aaron D Schuler.
Nature Structural & Molecular Biology (2004)
The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
Sonja Baumli;Graziano Lolli;Edward D Lowe;Sonia Troiani.
The EMBO Journal (2008)
Ruthenium half-sandwich complexes bound to protein kinase Pim-1.
Judit É. Debreczeni;Alex N. Bullock;G. Ekin Atilla;Douglas S. Williams.
Angewandte Chemie (2006)
Structural basis of Keap1 interactions with Nrf2.
Peter Canning;Fiona J. Sorrell;Alex N. Bullock.
Free Radical Biology and Medicine (2015)
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