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- Publications
- Influence
Phosphorylation in protein-protein binding: effect on stability and function.
- Hafumi Nishi, Kosuke Hashimoto, A. Panchenko
- Biology, Medicine
- Structure
- 7 December 2011
Posttranslational modifications offer a dynamic way to regulate protein activity, subcellular localization, and stability. Here we estimate the effect of phosphorylation on protein binding and… Expand
Cancer Missense Mutations Alter Binding Properties of Proteins and Their Interaction Networks
- Hafumi Nishi, Manoj Tyagi, +5 authors A. Panchenko
- Medicine, Biology
- PloS one
- 14 June 2013
Many studies have shown that missense mutations might play an important role in carcinogenesis. However, the extent to which cancer mutations might affect biomolecular interactions remains unclear.… Expand
Molecular mechanisms of disease-causing missense mutations.
- Shannon K. Stefl, Hafumi Nishi, Marharyta Petukh, A. Panchenko, E. Alexov
- Biology, Medicine
- Journal of molecular biology
- 1 November 2013
Genetic variations resulting in a change of amino acid sequence can have a dramatic effect on stability, hydrogen bond network, conformational dynamics, activity and many other physiologically… Expand
Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization.
- Kosuke Hashimoto, Hafumi Nishi, S. Bryant, A. Panchenko
- Biology, Medicine
- Physical biology
- 13 May 2011
Many soluble and membrane proteins form homooligomeric complexes in a cell which are responsible for the diversity and specificity of many pathways, may mediate and regulate gene expression, activity… Expand
Physicochemical mechanisms of protein regulation by phosphorylation
- Hafumi Nishi, A. Shaytan, A. Panchenko
- Biology, Medicine
- Front. Genet.
- 7 August 2014
Phosphorylation offers a dynamic way to regulate protein activity and subcellular localization, which is achieved through its reversibility and fast kinetics. Adding or removing a dianionic phosphate… Expand
Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes.
- Hafumi Nishi, J. Fong, Christiana Chang, S. Teichmann, A. Panchenko
- Biology, Medicine
- Molecular bioSystems
- 4 June 2013
Phosphorylation offers a dynamic way to regulate protein activity, subcellular localization, and stability. The majority of signaling pathways involve an extensive set of protein-protein… Expand
Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.
- Hafumi Nishi, Kosuke Hashimoto, T. Madej, A. Panchenko
- Biology, Medicine
- Progress in molecular biology and translational…
- 2013
Protein homooligomers afford several important benefits for the cell; they mediate and regulate gene expression, activity of many enzymes, ion channels, receptors, and cell-cell adhesion processes.… Expand
Crosstalk between signaling pathways provided by single and multiple protein phosphorylation sites.
- Hafumi Nishi, E. Demir, A. Panchenko
- Biology, Medicine
- Journal of molecular biology
- 30 January 2015
Cellular fate depends on the spatiotemporal separation and integration of signaling processes that can be provided by phosphorylation events. In this study, we identify the crucial points in… Expand
Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach
- K. Yamada, Satoshi Omori, Hafumi Nishi, M. Miyagi
- Biology, Computer Science
- BMC Bioinformatics
- 2 June 2017
TLDR
Dynamic recognition and linkage specificity in K63 di-ubiquitin and TAB2 NZF domain complex
- Kei Moritsugu, Hafumi Nishi, Keiichi Inariyama, M. Kobayashi, A. Kidera
- Chemistry, Medicine
- Scientific Reports
- 7 November 2018
Poly-ubiquitin (poly-Ub) is involved in various cellular processes through the linkage-specific recognition of Ub-binding domains (UBD). In this study, using molecular dynamics (MD) simulation… Expand