Results 71 to 80 of about 14,462 (190)

Cohesin's cohesion [PDF]

open access: yesThe Journal of Cell Biology, 2001
![Graphic][1] Cohesin (red) keeps centromeres together. Peters/AAAS Cohesin was a long sought-after protein complex: a glue for sister chromatids that is dissolved at the onset of anaphase thanks to cleavage of its SCC1 subunit by the protease separase.
openaire   +1 more source

Recent advances in cohesin biology [PDF]

open access: yesF1000Research, 2016
Sister chromatids are tethered together from the time they are formed in S-phase until they separate at anaphase. A protein complex called cohesin is responsible for holding the sister chromatids together and serves important roles in chromosome condensation, gene regulation, and the repair of DNA damage.
Rankin, Susannah, Dawson, Dean S.
openaire   +2 more sources

Targeting Cell Cycle Vulnerabilities in Cancers: Emerging Strategies for Therapeutic Development

open access: yesCancer Science, EarlyView.
Dysregulated cell cycle control often involves alternative compensatory pathways in cancers to maintain its robustness but provide unique targetable vulnerabilities. We overview recent insights on cancer‐specific vulnerabilities across the cell cycle and discuss how these can be used to develop new therapeutic strategies.
Nana Kamakura   +3 more
wiley   +1 more source

RAD21 is the core subunit of the cohesin complex involved in directing genome organization

open access: yesGenome Biology, 2023
Background The ring-shaped cohesin complex is an important factor for the formation of chromatin loops and topologically associating domains (TADs) by loop extrusion.
Yuao Sun   +16 more
doaj   +1 more source

Homologous recombination mutants cause differing lethality between h− and h+ Schizosaccharomyces pombe strains due to mat1 heterochromatin

open access: yesThe FEBS Journal, EarlyView.
Homologous recombination (HR) in Schizosaccharomyces pombe is essential when mating‐type switching–induced double‐strand breaks (DSBs) form at the mat1 locus. In h90 and h− strains, efficient mat1 DSB formation renders HR indispensable unless suppressors block these breaks.
Peter Kolesar   +3 more
wiley   +1 more source

Cohesin positions the epigenetic reader Phf2 within the genome

open access: yesThe EMBO Journal
Genomic DNA is assembled into chromatin by histones, and extruded into loops by cohesin. These mechanisms control important genomic functions, but whether histones and cohesin cooperate in genome regulation is poorly understood.
Wen Tang   +7 more
doaj   +1 more source

Dissecting Pirtobrutinib Resistance in Mantle Cell Lymphoma Through Single‐Cell Multi‐Omics

open access: yesAmerican Journal of Hematology, Volume 101, Issue 7, Page 1632-1649, July 2026.
ABSTRACT Pirtobrutinib (PBN), a non‐covalent BTK inhibitor, has been approved by the FDA for relapsed/refractory mantle cell lymphoma (MCL); however, resistance to PBN has been observed. To dissect the molecular dynamics driving PBN resistance, we performed integrative single‐cell multi‐omic profiling (scRNA‐seq, scATAC‐seq, and scDNA‐seq) on ...
Fangfang Yan   +10 more
wiley   +1 more source

A multi-step pathway for the establishment of sister chromatid cohesion.

open access: yesPLoS Genetics, 2007
The cohesion of sister chromatids is mediated by cohesin, a protein complex containing members of the structural maintenance of chromosome (Smc) family. How cohesins tether sister chromatids is not yet understood.
Mark Milutinovich   +4 more
doaj   +1 more source

Cohesin Mutations in Myeloid Malignancies [PDF]

open access: yesTrends in Cancer, 2017
Acute Myeloid Leukemia (AML) is a hematologic malignancy with a poor prognosis. Recent genome-wide sequencing studies have identified frequent mutations in genes encoding members of the cohesin complex. Mutations in cohesin contribute to myeloid malignancies by conferring enhanced self-renewal of hematopoietic stem and progenitor cells but the ...
Joseph B, Fisher   +4 more
openaire   +2 more sources

Integrative SAXS and AFM analysis of engineered carbohydrate‐active enzyme assemblies with tunable spatial organization

open access: yesProtein Science, Volume 35, Issue 7, July 2026.
Abstract Cellulosomes are multi‐enzyme assemblies whose catalytic efficiency depends on the spatial organization of their components. However, their pronounced conformational flexibility has precluded quantitative characterization of inter‐enzyme distances and overall topology.
Iker Pardo Larrabeiti   +11 more
wiley   +1 more source

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