Telomere-Binding Proteins

"Telomere-Binding Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

Proteins that specifically bind to TELOMERES. Proteins in this class include those that perform functions such as telomere capping, telomere maintenance and telomere stabilization.

Descriptor ID	D034501
MeSH Number(s)	D12.776.260.735 D12.776.660.235.700
Concept/Terms	Telomere-Binding Proteins Telomere-Binding Proteins Telomere Binding Proteins Telomere End-Binding Protein (TEBP) Telomere Repeat Binding Proteins Telomere Repeat Binding Proteins Telomere Repeat Binding Factors Telomere Repeat Binding Factor Telomer-Binding Protein, alpha-Subunit Telomer-Binding Protein, alpha-Subunit Telomer Binding Protein, alpha Subunit alpha-Subunit Telomer-Binding Protein alpha-Telomere-Binding Protein alpha Telomere Binding Protein Telomer-Binding Protein, beta-Subunit Telomer-Binding Protein, beta-Subunit Telomer Binding Protein, beta Subunit beta-Subunit Telomer-Binding Protein beta-Telomere-Binding Protein beta Telomere Binding Protein Double-Stranded Telomere-Binding Proteins Double-Stranded Telomere-Binding Proteins Double Stranded Telomere Binding Proteins Telomere-Binding Proteins, Double-Stranded Telomere-Binding Proteins, Double Stranded Telomere Binding Proteins, Double Stranded Double-Stranded Telomeric Binding Protein Double Stranded Telomeric Binding Protein Single-Stranded Telomere-Binding Proteins Single-Stranded Telomere-Binding Proteins Single Stranded Telomere Binding Proteins Telomere-Binding Proteins, Single-Stranded Telomere Binding Proteins, Single Stranded Single-Stranded Telomere-Binding Protein Single Stranded Telomere Binding Protein Telomere-Binding Protein, Single-Stranded

Below are MeSH descriptors whose meaning is more general than "Telomere-Binding Proteins".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
DNA-Binding Proteins [D12.776.260]
Telomere-Binding Proteins [D12.776.260.735]
Nuclear Proteins [D12.776.660]
Chromosomal Proteins, Non-Histone [D12.776.660.235]
Telomere-Binding Proteins [D12.776.660.235.700]

Below are MeSH descriptors whose meaning is related to "Telomere-Binding Proteins".

Below are MeSH descriptors whose meaning is more specific than "Telomere-Binding Proteins".

Telomere-Binding Proteins
Heterogeneous-Nuclear Ribonucleoprotein Group A-B
Telomeric Repeat Binding Protein 1
Telomeric Repeat Binding Protein 2

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Telomere-Binding Proteins" by people in this website by year, and whether "Telomere-Binding Proteins" was a major or minor topic of these publications.

Bar chart showing 10 publications over 8 distinct years, with a maximum of 2 publications in 2004 and 2011

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
2003	1	0	1
2004	2	0	2
2010	1	0	1
2011	1	1	2
2014	1	0	1
2015	0	1	1
2017	0	1	1
2019	1	0	1

Below are the most recent publications written about "Telomere-Binding Proteins" by people in Profiles.

Yorichika N, Baba Y, Shimada BK, Thakore M, Wong SM, Kobayashi M, Higa JK, Matsui T. The effects of Tel2 on cardiomyocyte survival. Life Sci. 2019 Sep 01; 232:116665.

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Phelan CM, Kuchenbaecker KB, Tyrer JP, Kar SP, Lawrenson K, Winham SJ, Dennis J, Pirie A, Riggan MJ, Chornokur G, Earp MA, Lyra PC, Lee JM, Coetzee S, Beesley J, McGuffog L, Soucy P, Dicks E, Lee A, Barrowdale D, Lecarpentier J, Leslie G, Aalfs CM, Aben KKH, Adams M, Adlard J, Andrulis IL, Anton-Culver H, Antonenkova N, Aravantinos G, Arnold N, Arun BK, Arver B, Azzollini J, Balma?a J, Banerjee SN, Barjhoux L, Barkardottir RB, Bean Y, Beckmann MW, Beeghly-Fadiel A, Benitez J, Bermisheva M, Bernardini MQ, Birrer MJ, Bjorge L, Black A, Blankstein K, Blok MJ, Bodelon C, Bogdanova N, Bojesen A, Bonanni B, Borg ?, Bradbury AR, Brenton JD, Brewer C, Brinton L, Broberg P, Brooks-Wilson A, Bruinsma F, Brunet J, Buecher B, Butzow R, Buys SS, Caldes T, Caligo MA, Campbell I, Cannioto R, Carney ME, Cescon T, Chan SB, Chang-Claude J, Chanock S, Chen XQ, Chiew YE, Chiquette J, Chung WK, Claes KBM, Conner T, Cook LS, Cook J, Cramer DW, Cunningham JM, D'Aloisio AA, Daly MB, Damiola F, Damirovna SD, Dansonka-Mieszkowska A, Dao F, Davidson R, DeFazio A, Delnatte C, Doheny KF, Diez O, Ding YC, Doherty JA, Domchek SM, Dorfling CM, D?rk T, Dossus L, Duran M, D?rst M, Dworniczak B, Eccles D, Edwards T, Eeles R, Eilber U, Ejlertsen B, Ekici AB, Ellis S, Elvira M, Eng KH, Engel C, Evans DG, Fasching PA, Ferguson S, Ferrer SF, Flanagan JM, Fogarty ZC, Fortner RT, Fostira F, Foulkes WD, Fountzilas G, Fridley BL, Friebel TM, Friedman E, Frost D, Ganz PA, Garber J, Garc?a MJ, Garcia-Barberan V, Gehrig A, Gentry-Maharaj A, Gerdes AM, Giles GG, Glasspool R, Glendon G, Godwin AK, Goldgar DE, Goranova T, Gore M, Greene MH, Gronwald J, Gruber S, Hahnen E, Haiman CA, H?kansson N, Hamann U, Hansen TVO, Harrington PA, Harris HR, Hauke J, Hein A, Henderson A, Hildebrandt MAT, Hillemanns P, Hodgson S, H?gdall CK, H?gdall E, Hogervorst FBL, Holland H, Hooning MJ, Hosking K, Huang RY, Hulick PJ, Hung J, Hunter DJ, Huntsman DG, Huzarski T, Imyanitov EN, Isaacs C, Iversen ES, Izatt L, Izquierdo A, Jakubowska A, James P, Janavicius R, Jernetz M, Jensen A, Jensen UB, John EM, Johnatty S, Jones ME, Kannisto P, Karlan BY, Karnezis A, Kast K, Kennedy CJ, Khusnutdinova E, Kiemeney LA, Kiiski JI, Kim SW, Kjaer SK, K?bel M, Kopperud RK, Kruse TA, Kupryjanczyk J, Kwong A, Laitman Y, Lambrechts D, Larra?aga N, Larson MC, Lazaro C, Le ND, Le Marchand L, Lee JW, Lele SB, Leminen A, Leroux D, Lester J, Lesueur F, Levine DA, Liang D, Liebrich C, Lilyquist J, Lipworth L, Lissowska J, Lu KH, Lubinnski J, Luccarini C, Lundvall L, Mai PL, Mendoza-Fandi?o G, Manoukian S, Massuger LFAG, May T, Mazoyer S, McAlpine JN, McGuire V, McLaughlin JR, McNeish I, Meijers-Heijboer H, Meindl A, Menon U, Mensenkamp AR, Merritt MA, Milne RL, Mitchell G, Modugno F, Moes-Sosnowska J, Moffitt M, Montagna M, Moysich KB, Mulligan AM, Musinsky J, Nathanson KL, Nedergaard L, Ness RB, Neuhausen SL, Nevanlinna H, Niederacher D, Nussbaum RL, Odunsi K, Olah E, Olopade OI, Olsson H, Olswold C, O'Malley DM, Ong KR, Onland-Moret NC, Orr N, Orsulic S, Osorio A, Palli D, Papi L, Park-Simon TW, Paul J, Pearce CL, Pedersen IS, Peeters PHM, Peissel B, Peixoto A, Pejovic T, Pelttari LM, Permuth JB, Peterlongo P, Pezzani L, Pfeiler G, Phillips KA, Piedmonte M, Pike MC, Piskorz AM, Poblete SR, Pocza T, Poole EM, Poppe B, Porteous ME, Prieur F, Prokofyeva D, Pugh E, Pujana MA, Pujol P, Radice P, Rantala J, Rappaport-Fuerhauser C, Rennert G, Rhiem K, Rice P, Richardson A, Robson M, Rodriguez GC, Rodr?guez-Antona C, Romm J, Rookus MA, Rossing MA, Rothstein JH, Rudolph A, Runnebaum IB, Salvesen HB, Sandler DP, Schoemaker MJ, Senter L, Setiawan VW, Severi G, Sharma P, Shelford T, Siddiqui N, Side LE, Sieh W, Singer CF, Sobol H, Song H, Southey MC, Spurdle AB, Stadler Z, Steinemann D, Stoppa-Lyonnet D, Sucheston-Campbell LE, Sukiennicki G, Sutphen R, Sutter C, Swerdlow AJ, Szabo CI, Szafron L, Tan YY, Taylor JA, Tea MK, Teixeira MR, Teo SH, Terry KL, Thompson PJ, Thomsen LCV, Thull DL, Tihomirova L, Tinker AV, et al. Identification of 12 new susceptibility loci for different histotypes of epithelial ovarian cancer. Nat Genet. 2017 May; 49(5):680-691.

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Challagundla KB, Wise PM, Neviani P, Chava H, Murtadha M, Xu T, Kennedy R, Ivan C, Zhang X, Vannini I, Fanini F, Amadori D, Calin GA, Hadjidaniel M, Shimada H, Jong A, Seeger RC, Asgharzadeh S, Goldkorn A, Fabbri M. Exosome-mediated transfer of microRNAs within the tumor microenvironment and neuroblastoma resistance to chemotherapy. J Natl Cancer Inst. 2015 Jul; 107(7).

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Diotti R, Kalan S, Matveyenko A, Loayza D. DNA-Directed Polymerase Subunits Play a Vital Role in Human Telomeric Overhang Processing. Mol Cancer Res. 2015 Mar; 13(3):402-10.

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Sheppard SA, Savinova T, Loayza D. TRIP6 and LPP, but not Zyxin, are present at a subset of telomeres in human cells. Cell Cycle. 2011 Jun 01; 10(11):1726-30.

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Diotti R, Loayza D. Shelterin complex and associated factors at human telomeres. Nucleus. 2011 Mar-Apr; 2(2):119-35.

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Sheppard SA, Loayza D. LIM-domain proteins TRIP6 and LPP associate with shelterin to mediate telomere protection. Aging (Albany NY). 2010 Jul; 2(7):432-44.

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Ye JZ, Hockemeyer D, Krutchinsky AN, Loayza D, Hooper SM, Chait BT, de Lange T. POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex. Genes Dev. 2004 Jul 15; 18(14):1649-54.

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Loayza D, Parsons H, Donigian J, Hoke K, de Lange T. DNA binding features of human POT1: a nonamer 5'-TAGGGTTAG-3' minimal binding site, sequence specificity, and internal binding to multimeric sites. J Biol Chem. 2004 Mar 26; 279(13):13241-8.

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Loayza D, De Lange T. POT1 as a terminal transducer of TRF1 telomere length control. Nature. 2003 Jun 26; 423(6943):1013-8.

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