ArticleNature structural & molecular biology2014
Internal motions prime cIAP1 for rapid activation.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Cytoplasmic and Nuclear Functions of cIAP1.Biomolecules · 2022Review
- Probing allosteric regulations with coevolution-driven molecular simulations.Science advances · 2021Article
- Review
- Protein Dynamics revealed by NMR Relaxation Methods.Emerging topics in life sciences · 2020Article
- Resonant Soft X-Ray Scattering Provides Protein Structure with Chemical Specificity.Structure (London, England : 1993) · 2018Article
- Structural insights into the catalysis and regulation of E3 ubiquitin ligases.Nature reviews. Molecular cell biology · 2016Review
- Geometric Approximation: A New Computational Approach To Characterize Protein Dynamics from NMR Adiabatic Relaxation Dispersion Experiments.Journal of the American Chemical Society · 2016Article
- A dynamic look backward and forward.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Review
- NF-κB functions as a molecular link between tumor cells and Th1/Tc1 T cells in the tumor microenvironment to exert radiation-mediated tumor suppression.Oncotarget · 2016Article
- Genomic insights into head and neck cancer.Cancers of the head & neck · 2016Article
- Inhibitor of apoptosis proteins as intracellular signaling intermediates.The FEBS journal · 2016Review
- Using protein motion to read, write, and erase ubiquitin signals.The Journal of biological chemistry · 2015Review
- Dynamic activation of apoptosis: conformational ensembles of cIAP1 are linked to a spring-loaded mechanism.Nature structural & molecular biology · 2014Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Cellular inhibitor of apoptosis 1 (cIAP1) is a ubiquitin ligase with critical roles in the control of programmed cell death and NF-κB signaling. Under normal conditions, the protein exists as an autoinhibited monomer, but proapoptotic signals lead to its dimerization, activation and proteasomal degradation. This view of cIAP1 as a binary switch has been informed by static structural studies that cannot access the protein's dynamics. Here, we use NMR spectroscopy to study micro- and millisecond motions of specific domain interfaces in human cIAP1 and use time-resolved small-angle X-ray scattering to observe the global conformational changes necessary for activation. Although motions within each interface of the 'closed' monomer are insufficient to activate cIAP1, they enable associations with catalytic partners and activation factors. We propose that these internal motions facilitate rapid peptide-induced opening and dimerization of cIAP1, which undergoes a dramatic spring-loaded structural transition.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.