ArticleBiochemical and biophysical research communications2008
Identification of the interaction sites of Inhibitor-3 for protein phosphatase-1.
Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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
9 citing papers in PubMed.
- Alternating binding and p97-mediated dissociation of SDS22 and I3 recycles active PP1 between holophosphatases.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- SDS22 coordinates the assembly of holoenzymes from nascent protein phosphatase-1.Nature communications · 2024Article
- Structural basis of ubiquitin-independent PP1 complex disassembly by p97.The EMBO journal · 2023Article
- Inhibitor-3 inhibits Protein Phosphatase 1 via a metal binding dynamic protein-protein interaction.Nature communications · 2023Article
- Targeted substrate loop insertion by VCP/p97 during PP1 complex disassembly.Nature structural & molecular biology · 2021Article
- Phosphatase inhibitor PPP1R11 modulates resistance of human T cells toward Treg-mediated suppression of cytokine expression.Journal of leukocyte biology · 2019Article
- Protein Phosphatase 1-Targeting Small-Molecule C31 Inhibits Ebola Virus Replication.The Journal of infectious diseases · 2018Article
- Endogenous inhibitor proteins that connect Ser/Thr kinases and phosphatases in cell signaling.IUBMB life · 2012Review
- Plasmodium falciparum inhibitor-3 homolog increases protein phosphatase type 1 activity and is essential for parasitic survival.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Inhibitor-3 is a potent inhibitor of protein phosphatase-1, with an IC(50) in the nanomolar range for the inhibition of the dephosphorylation of phosphorylase a. Human Inhibitor-3 possesses a putative protein phosphatase-1 binding motif, (39)KKVEW(43). We provide direct evidence that this sequence is involved in PP1 interaction by examining the effects of site-directed mutations of Inhibitor-3 on its ability to inhibit protein phosphatase-1. A second interaction site whose deletion led to loss of inhibitory potency was identified between residues 65 and 77. The existence of two interaction sites is consistent with the high inhibitory potency of Inhibitor-3, and with current models for other inhibitor and targeting proteins that interact with protein phosphatase-1 with high affinity.
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