Results 101 to 110 of about 28,191 (215)

The Core Histone-binding Region of the Murine Cytomegalovirus 89K Immediate Early Protein [PDF]

, 1991
The gene regulatory immediate early protein, pp89, of murine cytomegalovirus interacts with both DNA-associated and isolated histones in vitro. We characterized the histone-binding region of pp89 and its cellular localization during cell division to ...
Bühler, Bernhard, Koszinowski, Ulrich H., Messerle, Martin, Münch, Konrad   +3 more
core   +1 more source

Phase Separation: A New Dimension to Understanding Tumor Biology and Therapy

MedComm – Oncology, Volume 4, Issue 2, June 2025.
Liquid–liquid phase separation (LLPS) facilitates the assembly of biomolecular condensates by leveraging weak multivalent interactions. The low‐complexity domains, foldable domains of proteins, and nucleic acids provide multivalent interaction sites among different molecules and contribute to the formation of condensates.
Xingwen Wang, Minqiao Lu, Yi Zhang, Jiangwen Ma, Ying Hu   +4 more
wiley   +1 more source

Locus-specific control of DNA resection and suppression of subtelomeric VSG recombination by HAT3 in the African trypanosome [PDF]

, 2014
The African trypanosome, Trypanosoma brucei, is a parasitic protozoan that achieves antigenic varia-tion through DNA-repair processes involving Variant Surface Glycoprotein (VSG) gene rearrangements at subtelomeres.
Alsford, Alsford, Baker, Bird, Boothroyd, Brun, Callejas, David Horn, Dreesen, Ersfeld, Garcia-Salcedo, Glover, Glover, Glover, Glover, Glover, Gong, Graf, Haldar, Harrison, Horn, Hovel-Miner, Huyen, Ingram, Ivanov, Jackson, Jehi, Kawahara, Kim, Kostriken, Kranz, Lee, Lee, Li, Li, Longhese, Lucy Glover, Marcello, Martin, McCulloch, McCulloch, Miyazaki, Oberdoerffer, Paques, Pays, Price, Proudfoot, Robinson, Sfeir, Sharma, Siegel, Sinha, Soria, Sugawara, Sun, Sun, Symington, Tamburini, Tang, Trovesi, Uhl, Vickerman, Vincent, Yamagata   +63 more
core   +4 more sources

Yeast genetic analysis reveals the involvement of chromatin reassembly factors in repressing HIV-1 basal transcription. [PDF]

PLoS Genetics, 2009
Rebound of HIV viremia after interruption of anti-retroviral therapy is due to the small population of CD4+ T cells that remain latently infected. HIV-1 transcription is the main process controlling post-integration latency.
Manuela Vanti, Edurne Gallastegui, Iñaki Respaldiza, Alfonso Rodríguez-Gil, Fernando Gómez-Herreros, Silvia Jimeno-González, Albert Jordan, Sebastián Chávez   +7 more
doaj   +1 more source

Functional analysis of chromatin-associated proteins in Sordaria macrospora reveals similar roles for RTT109 and ASF1 in development and DNA damage response

bioRxiv
We performed a functional analysis of two potential partners of ASF1, a highly conserved histone chaperone that plays a crucial role in the sexual development and DNA damage resistance in the ascomycete Sordaria macrospora.
Jan Breuer, David Emanuel Antunes Ferreira, Mike Kramer, Jonas Bollermann, M. Nowrousian   +4 more
semanticscholar   +1 more source

A sea urchin cell-free system to study male pronuclear assembly and activation.

International Journal of Developmental Biology, 2016
Typically sperm nuclei are genetically inert and contain extremely compacted chromatin. Following fertilization, the first steps in their conversion to somatic nuclei (male pronuclei) which will support further development involve chromatin ...
D. Poccia
semanticscholar   +1 more source

Importin-beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function [PDF]

, 2017
Protein conjugation with small ubiquitin-related modifier (SUMO) is a post-translational modification that modulates protein interactions and localisation.
Damizia, Michela, DE SANTIS, RICCARDO, DE TURRIS, VALERIA, GILISTRO, EUGENIA, Lavia, Patrizia, MORONI, SARA, ROSA, ALESSANDRO, VERRICO, ANNALISA   +7 more
core   +1 more source

Chromosome Duplication in Saccharomyces cerevisiae [PDF]

, 2016
The accurate and complete replication of genomic DNA is essential for all life. In eukaryotic cells, the assembly of the multi-enzyme replisomes that perform replication is divided into stages that occur at distinct phases of the cell cycle.
Abid Ali, Alabert, Alabert, Albert, Alcasabas, Allen, Amin, Antczak, Aparicio, Aparicio, Arias, Ayyagari, Bae, Bando, Bastos de Oliveira, Baxter, Bechhoefer, Bell, Bell, Belsky, Ben-Shahar, Berbenetz, Bermejo, Bermejo, Berndsen, Bianchi, Bleichert, Blitzblau, Blow, Bochman, Bochman, Boiteux, Borges, Bowers, Branzei, Branzei, Breier, Brewer, Brewer, Brewster, Broach, Bruck, Bruin, Buchman, Budd, Bylund, Calzada, Chan, Chang, Chang, Chen, Chen, Cheng, Chilkova, Choi, Clausen, Collins, Costa, Costa, Coster, Crabbe, Czajkowsky, Dahmann, Daigaku, Dalgaard, Das, Davey, Davé, De Koning, De Piccoli, Desany, Deshpande, Devault, Dewar, Diffley, Diffley, Diffley, Diffley, Dion, Dornreiter, Downs, Driscoll, Drury, Dua, Dutta, Eaton, Elledge, English, Evrin, Evrin, Evrin, Fachinetti, Fanning, Ferguson, Ferguson, Fernandez-Cid, Finley, Fiorani, Flanagan, Fletcher, Fletcher, Foltman, Francis, Friedel, Friedman, Frigola, Froelich, Fu, Gambus, Gambus, Gangloff, Garcia-Rodriguez, Garg, Gary, Ge, Georgescu, Georgescu, Ghodgaonkar, Godinho Ferreira, Green, Green, Greenfeder, Haering, Hanna, Hardy, Hartwell, Hawkins, Heller, Hennessy, Hickson, Hills, Hiraga, Hodgson, Hoege, Hogg, Hoggard, Hsiao, Huang, Huang, Huang, Huberman, Hurwitz, Iida, Ilves, Ivessa, Ivessa, Ivessa, Iyer, Jacob, Jacobson, Johnson, Kamimura, Kamimura, Kanellis, Kanemaki, Kanemaki, Kang, Kang, Kaplan, Katan-Khaykovich, Kato, Katou, Kaufman, Kaykov, Kegel, Kelly, Kesti, Khayrutdinov, Kim, Kitamura, Klein, Klemm, Knott, Knott, Kobayashi, Komata, Krings, Kubota, Kubota, Kunkel, Kunkel, Kunkel, Labib, Labib, Labib, Labib, Lahaye, Langston, Le, Lee, Lee, Lee, Lengronne, Li, Li, Li, Li, Liachko, Liachko, Linskens, Lipford, Liu, Liu, Looke, Lopez-Mosqueda, Lou, Lucchini, Lujan, Luke, Lydeard, Lyons, MacAlpine, Maculins, Maine, Makovets, Mantiero, Marahrens, Maric, Marston, Masumoto, Mattarocci, Mayer, Mayer, McGuffee, McInerney, Mohanty, Moldovan, Mori, Morohashi, Muramatsu, Nasmyth, Natsume, Natsume, Nguyen, Nguyen, Nick McElhinny, Nick McElhinny, Nick McElhinny, Oliveira, Oppikofer, Orphanides, Osborn, Paciotti, Paeschke, Paeschke, Pan, Papamichos-Chronakis, Papouli, Park, Parker, Pasero, Pavlov, Pellegrini, Perera, Pfander, Pohl, Prior, Pursell, Putnam, Quan, Radman-Livaja, Raghuraman, Ramer, Randell, Randell, Ransom, Rao, Rao, Reijns, Remus, Remus, Reyes-Lamothe, Richet, Ricke, Rolef Ben-Shahar, Rouse, Rowland, Rowley, Samel, Samora, Santocanale, Santocanale, Santocanale, Schalbetter, Schlesinger, Schneider, Scholes, Segal, Segurado, Segurado, Sekedat, Seki, Selth, Sengupta, Shcherbakova, Sheu, Sheu, Shimada, Shirahige, Shundrovsky, Siddiqui, Simmons, Simon, Simpson, Siow, Sjogren, Skibbens, Skibbens, Smith, Sogo, Speck, Stelter, Stevenson, Stinchcomb, Strom, Sun, Sun, Sun, Sundin, Szyjka, Szyjka, Takara, Takayama, Tanaka, Tanaka, Tanaka, Tanaka, Tanaka, Tanaka, Tercero, Tercero, Theis, Theis, Ticau, Toth, Tourriere, Travesa, Tsubota, Tsubota, Uhlmann, Uhlmann, Ulrich, Ulrich, Unal, Unal, van Attikum, van Deursen, Versini, Vestner, Villa, Vincent, Vogelauer, Waga, Wang, Warren, Watase, Weinert, Weinert, Weinreich, Wellinger, Whitehouse, Wilmes, Wilmes, Winkler, Wittmeyer, Wu, Wyrick, Wyrick, Xu, Yabuki, Yamasu, Yao, Yardimci, Yeeles, Yoshida, Yu, Yuan, Zegerman, Zegerman, Zegerman, Zhang, Zhang, Zhao, Zhao, Zhou, Zhou, Zhu, Zou, Zou, Zou, Zou   +390 more
core   +2 more sources

Tubulin Polymerization Promoting Proteins: Functional Diversity With Implications in Neurological Disorders

Journal of Neuroscience Research, Volume 103, Issue 5, May 2025.
A family of human proteins, encoded by Tubulin Polymerization Promoting Proteins (TPPP), is highly conserved across species. TPPP displays remarkable functional diversity and is implicated in various neurological disorders. Image created with BioRender.com.
Paloma J. Diaz, Qian Shi, Priscilla Y. McNeish, Swati Banerjee   +3 more
wiley   +1 more source

Degradation-linked ubiquitin signal and proteasome are integral components of DNA double strand break repair: New perspectives for anti-cancer therapy [PDF]

, 2011
Damaged DNA leads to genomic instability that causes many diseases such as cancer. Cells evolved the DNA damage response (DDR), which recognizes and efficiently repairs damaged DNA through the action of highly coordinated signalling mechanisms. Recently,
Meerang, Mayura, Ramadan, Kristijan
core   +1 more source