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The following term was not found in PubMed: 104558-30-7
Page 1
Centrin/Cdc31 is a novel regulator of protein degradation.
Chen L, Madura K. Chen L, et al. Mol Cell Biol. 2008 Mar;28(5):1829-40. doi: 10.1128/MCB.01256-07. Epub 2007 Dec 26. Mol Cell Biol. 2008. PMID: 18160718 Free PMC article.
Based on the dual function of Rad23, in both DNA repair and protein degradation, we questioned if Cdc31 also participated in protein degradation. ...These findings reveal for the first time a new role for centrin/Cdc31 in protein degradation....
Based on the dual function of Rad23, in both DNA repair and protein degradation, we questioned if Cdc31 also participated in …
A role for Saccharomyces cerevisiae Centrin (Cdc31) in mitochondrial function and biogenesis.
Chen L, Bian S, Li H, Madura K. Chen L, et al. Mol Microbiol. 2018 Dec;110(5):831-846. doi: 10.1111/mmi.14128. Epub 2018 Oct 28. Mol Microbiol. 2018. PMID: 30251372 Free article.
We also found that Cdc31 is involved in the ubiquitin/proteasome system, and mutations interfere with intracellular protein turnover. In this report, we describe new findings that indicate a role for Cdc31 in the energy metabolism pathway. Cdc31 and …
We also found that Cdc31 is involved in the ubiquitin/proteasome system, and mutations interfere with intracellular protein tu …
Structure and Function of the TREX-2 Complex.
Stewart M. Stewart M. Subcell Biochem. 2019;93:461-470. doi: 10.1007/978-3-030-28151-9_15. Subcell Biochem. 2019. PMID: 31939161 Review.
In Saccharomyces cerevisiae the TREX-2 complex is based on a Sac3 scaffold to which Thp1, Sem1, Cdc31 and two Sus1 chains are bound. A combination of X-ray crystallography and electron microscopy studies have established the structure of two major regions of this complex: …
In Saccharomyces cerevisiae the TREX-2 complex is based on a Sac3 scaffold to which Thp1, Sem1, Cdc31 and two Sus1 chains are bound. …
Transcription at the proximity of the nuclear pore: a role for the THP1-SAC3-SUS1-CDC31 (THSC) complex.
Luna R, González-Aguilera C, Aguilera A. Luna R, et al. RNA Biol. 2009 Apr-Jun;6(2):145-8. doi: 10.4161/rna.6.2.7803. Epub 2009 Apr 8. RNA Biol. 2009. PMID: 19229139 Review.
The use of new techniques based on tandem affinity purification (TAP) and chromatin immunoprecipitation (ChIP), and of genetic and cell biology approaches has contributed to the beginning of deciphering the network of protein-mRNA interactions accompanying this coupling. A …
The use of new techniques based on tandem affinity purification (TAP) and chromatin immunoprecipitation (ChIP), and of genetic and cell biol …
Kar1 binding to Sfi1 C-terminal regions anchors the SPB bridge to the nuclear envelope.
Seybold C, Elserafy M, Rüthnick D, Ozboyaci M, Neuner A, Flottmann B, Heilemann M, Wade RC, Schiebel E. Seybold C, et al. J Cell Biol. 2015 Jun 22;209(6):843-61. doi: 10.1083/jcb.201412050. Epub 2015 Jun 15. J Cell Biol. 2015. PMID: 26076691 Free PMC article.
Its cytoplasmic components are the membrane-anchored Kar1, the yeast centrin Cdc31, and the Cdc31-binding protein Sfi1. In G1, the half bridge expands into the bridge through Sfi1 C-terminal (Sfi1-CT) dimerization, the licensing step for SPB duplication. ... …
Its cytoplasmic components are the membrane-anchored Kar1, the yeast centrin Cdc31, and the Cdc31-binding protein Sfi1. …
The N-terminus of Sfi1 and yeast centrin Cdc31 provide the assembly site for a new spindle pole body.
Rüthnick D, Vitale J, Neuner A, Schiebel E. Rüthnick D, et al. J Cell Biol. 2021 Mar 1;220(3):e202004196. doi: 10.1083/jcb.202004196. J Cell Biol. 2021. PMID: 33523111 Free PMC article.
The first step in SPB duplication is the half-bridge to bridge conversion via the antiparallel dimerization of the centrin (Cdc31)-binding protein Sfi1 in anaphase. The bridge, which is anchored to the old SPB on the proximal end, exposes free Sfi1 N-termini (N-Sfi1 …
The first step in SPB duplication is the half-bridge to bridge conversion via the antiparallel dimerization of the centrin (Cdc31)-bi …
A role for centrin 3 in centrosome reproduction.
Middendorp S, Küntziger T, Abraham Y, Holmes S, Bordes N, Paintrand M, Paoletti A, Bornens M. Middendorp S, et al. J Cell Biol. 2000 Feb 7;148(3):405-16. doi: 10.1083/jcb.148.3.405. J Cell Biol. 2000. PMID: 10662768 Free PMC article.
Furthermore, HsCEN3 does not complement mutations or deletion of CDC31 in S. cerevisiae, but specifically blocks SPB duplication, indicating that the human protein acts as a dominant negative mutant of CDC31. Several lines of evidence indicate that HsCen3p ac …
Furthermore, HsCEN3 does not complement mutations or deletion of CDC31 in S. cerevisiae, but specifically blocks SPB duplication, ind …
Fission yeast cdc31p is a component of the half-bridge and controls SPB duplication.
Paoletti A, Bordes N, Haddad R, Schwartz CL, Chang F, Bornens M. Paoletti A, et al. Mol Biol Cell. 2003 Jul;14(7):2793-808. doi: 10.1091/mbc.e02-10-0661. Epub 2003 Apr 4. Mol Biol Cell. 2003. PMID: 12857865 Free PMC article.
Here, we report the identification and characterization of Schizosaccharomyces pombe cdc31p, a member of the conserved calcium-binding centrin/CDC31 family. Immunofluorescence and immunoelectron microscopy show that cdc31p is a SPB component localized at the half-bridge st …
Here, we report the identification and characterization of Schizosaccharomyces pombe cdc31p, a member of the conserved calcium-binding centr …
Molecular cloning of cDNA for caltractin, a basal body-associated Ca2+-binding protein: homology in its protein sequence with calmodulin and the yeast CDC31 gene product.
Huang B, Mengersen A, Lee VD. Huang B, et al. J Cell Biol. 1988 Jul;107(1):133-40. doi: 10.1083/jcb.107.1.133. J Cell Biol. 1988. PMID: 2839516 Free PMC article.
The primary protein sequence of the 20-kD CaBP and its predicted secondary structure suggests that the protein is likely to contain four homologous calcium-binding domains that conform to the helix-loop-helix (or EF hand) structure found in calmodulin and related ca …
The primary protein sequence of the 20-kD CaBP and its predicted secondary structure suggests that the protein is likely to co …
Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic.
Myers MD, Payne GS. Myers MD, et al. J Cell Biol. 2017 Feb;216(2):299-301. doi: 10.1083/jcb.201612026. Epub 2017 Jan 25. J Cell Biol. 2017. PMID: 28122956 Free PMC article.
Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmental disorders. ...Cell Biol. https://doi.org/10.1083/jcb.201606078) establish direct roles for Vps13 and its surprising binding partner, the …
Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmen …
63 results