This is a default text for your page Sandbox GGC9. Click above on edit this page to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Introduction
Telomerase is essential for continuous cellular proliferation. Substantial insights have come from studies of budding yeast telomerase. In cells that lack telomerase, gradual erosion due to incomplete replication of duplex telomeric DNA leads to an eventual Block to cellular proliferation.[3]
Function
A single pathway for telomere replication in the yeast Saccharomyces cerevisiae [4]
They have been studies about individual functions of the components of the S. cerevisiae telomerase.[5]
Component of telomerase complex involved in telomere replication. Stimulates RNA/DNA heteroduplex unwinding which favors the telomere replication by the telomerase.[6]
Est3 protein surface has an important opening up in the structurally similar human TPP1 protein. [7]
Disease
Saccharomyces cerevisiae is a species of yeast that is known in baking and brewing. Also, it is used as a probiotic in humans but it very uncommon infection in humans.[8]
Relevance
Studies have found Est3 adopts OB-fold with certain distinctive features. In most cases, the most notable discrepancy between Est and other OB-fold protein is OB-fold ligand-binding.[9]
Structural highlights
This is <scene name='75/752271/2f6a/2'>2f6a [10]
- ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:https://dx.doi.org/10.1073/pnas.1316453111
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:https://dx.doi.org/10.1073/pnas.1316453111
- ↑ doi: https://dx.doi.org/10.1016/s0960-9822(00)00562-5
- ↑ Lee J, Mandell EK, Rao T, Wuttke DS, Lundblad V. Investigating the role of the Est3 protein in yeast telomere replication. Nucleic acids research. 2010 Apr 1. doi: 10.1093/nar/gkp1173. PMID: 20047960.
- ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:https://dx.doi.org/10.1073/pnas.1316453111
- ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:https://dx.doi.org/10.1073/pnas.1316453111
- ↑ https://doi.org/10.1086/429916
- ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:https://dx.doi.org/10.1073/pnas.1316453111
- ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:https://dx.doi.org/10.1073/pnas.1316453111
