Mechanism of auxin perception by the TIR1 ubiquitin ligase
- Xu Tan, L. I. Calderon-Villalobos, N. Zheng
- Environmental ScienceNature
- 5 April 2007
These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket, establishing the first structural model of a plant hormone receptor.
Structural role of Sfi1p–centrin filaments in budding yeast spindle pole body duplication
- Sam Li, A. Sandercock, Paul T. Conduit, C. Robinson, Roger L. Williams, J. Kilmartin
- BiologyJournal of Cell Biology
- 19 June 2006
A model for SPB duplication where the half-bridge doubles in length by association of the Sfi1p C termini, thereby providing a new Sfi2p N terminus to initiate SPB assembly is suggested.
In vitro reconstitution of the human RISC-loading complex
- I. MacRae, E. Ma, Min Zhou, C. Robinson, J. Doudna
- BiologyProceedings of the National Academy of Sciences
- 15 January 2008
It is shown that the human RLC assembles spontaneously in vitro from purified components, and the reconstituted RLC, containing one copy of each protein, has the dicing, slicing, guide-strand selection, and Ago2-loading activities observed for the endogenous RLC.
The structure of the dynactin complex and its interaction with dynein
- L. Urnavicius, Kai Zhang, A. Carter
- Biology, ChemistryScience
- 27 March 2015
The reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of β-actin, which is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the α-helical shoulder domain.
The protofilament structure of insulin amyloid fibrils
- J. L. Jimenez, E. J. Nettleton, M. Bouchard, C. Robinson, C. Dobson, H. Saibil
- BiologyProceedings of the National Academy of Sciences…
- 1 July 2002
Cryo-electron microscopy is used, combining single particle analysis and helical reconstruction, to characterize these fibrils and to study the three-dimensional (3D) arrangement of their component protofilaments, suggesting that very small, local changes in β-sheet twist are important in establishing the long-range coiling of the prot ofilaments into fibrILS of diverse morphology.
Ion mobility–mass spectrometry analysis of large protein complexes
- B. Ruotolo, J. Benesch, A. Sandercock, Suk-Joon Hyung, C. Robinson
- BiologyNature Protocols
- 1 June 2008
Within this protocol, general approaches to data interpretation, methods of predicting whether specific model structures for a given protein assembly can be separated by ion mobility, and generalized strategies for data normalization and modeling are covered.
Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles.
- M. Marty, A. Baldwin, E. Marklund, Georg K. A. Hochberg, J. Benesch, C. Robinson
- PhysicsAnalytical Chemistry
- 1 April 2015
UniDec (Universal Deconvolution), software that provides a rapid, robust, and flexible deconvolution of mass spectra and ion mobility-mass spectra with minimal user intervention is developed, using systems of increasing complexity.
Collision cross sections of proteins and their complexes: a calibration framework and database for gas-phase structural biology.
- M. F. Bush, Z. Hall, K. Giles, J. Hoyes, C. Robinson, B. Ruotolo
- BiologyAnalytical Chemistry
- 27 October 2010
This database indicates that collision cross sections in both helium and nitrogen gases can be well-correlated for larger biomolecular ions, but non-cor related differences for smaller ions can be more significant.
Targeting C-reactive protein for the treatment of cardiovascular disease
- M. Pepys, G. Hirschfield, S. Wood
- Biology, MedicineNature
- 27 April 2006
Therapeutic inhibition of CRP is a promising new approach to cardioprotection in acute myocardial infarction and may also provide neuroprotection in stroke and potential wider applications include other inflammatory, infective and tissue-damaging conditions characterized by increased CRP production.
Structural basis for protein–protein interactions in the 14-3-3 protein family
- Xiaowen Yang, W. H. Lee, J. Elkins
- Biology, ChemistryProceedings of the National Academy of Sciences
- 14 November 2006
Structural detail for five 14-3-3 isoforms bound to ligands is provided, providing structural coverage for all isoforms of a human protein family, and shows that the 14- 3-3 proteins are adaptable structures in which internal flexibility is likely to facilitate recognition and binding of their interaction partners.
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