Other names published for COF1: cofilin, YLL050C
COF1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
COF1 - Protein-protein Interactions (23)
| Reference | Other Genes Addressed |
|---|---|
| McCullough BR, et al. (2011) Cofilin-linked changes in actin filament flexibility promote severing. Biophys J 101(1):151-9 | |
| Suarez C, et al. (2011) Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries. Curr Biol 21(10):862-8 | |
| Bryan KE and Rubenstein PA (2009) Allele-specific Effects of Human Deafness {gamma}-Actin Mutations (DFNA20/26) on the Actin/Cofilin Interaction. J Biol Chem 284(27):18260-9 | |
| Quintero-Monzon O, et al. (2009) Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover. J Biol Chem 284(16):10923-34 | |
| Scoville D, et al. (2009) Effects of binding factors on structural elements in F-actin. Biochemistry 48(2):370-8 | |
| Fan X, et al. (2008) Intrinsic capability of budding yeast cofilin to promote turnover of tropomyosin-bound actin filaments. PLoS ONE 3(11):e3641 | |
| Grintsevich EE, et al. (2008) Mapping the cofilin binding site on yeast G-actin by chemical cross-linking. J Mol Biol 377(2):395-409 | |
| Stokasimov E, et al. (2008) Role of intermonomer ionic bridges in the stabilization of the actin filament. J Biol Chem 283(50):34844-54 | |
| Benchaar SA, et al. (2007) Mapping the interaction of cofilin with subdomain 2 on actin. Biochemistry 46(1):225-33 | |
| Clark MG and Amberg DC (2007) Biochemical and genetic analyses provide insight into the structural and mechanistic properties of actin filament disassembly by the Aip1p cofilin complex in Saccharomyces cerevisiae. Genetics 176(3):1527-39 | |
| Kudryashov DS, et al. (2006) Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface. J Mol Biol 358(3):785-97 | |
| Moseley JB, et al. (2006) Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo. J Cell Sci 119(Pt 8):1547-57 | |
| Muhlrad A, et al. (2006) Antagonistic effects of cofilin, beryllium fluoride complex, and phalloidin on subdomain 2 and nucleotide-binding cleft in F-actin. Biophys J 91(12):4490-9 | |
| Tagwerker C, et al. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48 | |
| Bobkov AA, et al. (2004) Cofilin (ADF) affects lateral contacts in F-actin. J Mol Biol 337(1):93-104 | |
| Mattila PK, et al. (2004) A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein. Mol Biol Cell 15(11):5158-71 | |
| Voegtli WC, et al. (2003) The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization. J Biol Chem 278(36):34373-9 | |
| Bobkov AA, et al. (2002) Structural effects of cofilin on longitudinal contacts in F-actin. J Mol Biol 323(4):739-50 | |
| Galkin VE, et al. (2002) A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure. Curr Biol 12(7):570-5 | |
| Guan JQ, et al. (2002) Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting. Biochemistry 41(18):5765-75 | |
| Ojala PJ, et al. (2001) Identification of yeast cofilin residues specific for actin monomer and PIP2 binding. Biochemistry 40(51):15562-9 | |
| Wolven AK, et al. (2000) In vivo importance of actin nucleotide exchange catalyzed by profilin. J Cell Biol 150(4):895-904 | |
| Wriggers W, et al. (1998) Cofilin and gelsolin segment-1: molecular dynamics simulation and biochemical analysis predict a similar actin binding mode. J Mol Biol 282(5):921-32 | |



