Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ema Stokasimov"'
Autor:
Stamatis Papathanasiou, Nikos A. Mynhier, Shiwei Liu, Etai Jacob, Ema Stokasimov, Bas van Steensel, Cheng-Zhong Zhang, David Pellman
Transcriptional heterogeneity from plasticity of the epigenetic state of chromatin is thought to contribute to tumor evolution, metastasis, and drug resistance 1–3. However, the mechanisms leading to nongenetic cell-to-cell variation in gene expres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::46570abf64f3888b2b2af7c06fd42907
https://doi.org/10.1101/2022.01.12.475869
https://doi.org/10.1101/2022.01.12.475869
Publikováno v:
Nature. 606(7916)
Chromothripsis is a catastrophic mutational process that promotes tumorigenesis and causes congenital disease
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9eb3ce51dd8227d587743b10c245752a
https://pubmed.ncbi.nlm.nih.gov/35803217
https://pubmed.ncbi.nlm.nih.gov/35803217
Autor:
Sue L. Jaspersen, Ema Stokasimov, Joseph M. Varberg, Etai Jacob, David Pellman, Nathaniel Dempsey, I-Ju Lee
Publikováno v:
The Journal of Cell Biology
ESCRT makes a partial contribution to nuclear envelope fusion at the end of mitosis. Using Schizosaccharomyces japonicus, a fission yeast that undergoes mitotic NE breakdown, a forward genetic screen was performed to identify sealing mechanisms indep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0baa880a130b09fe4919563273a8d891
https://doi.org/10.1083/jcb.201908232
https://doi.org/10.1083/jcb.201908232
Autor:
Luke M. Rice, Elisabeth A. Geyer, William O. Hancock, Hugo Arellano-Santoyo, Xiaolei Su, Ema Stokasimov, Geng-Yuan Chen, David Pellman
Summary Kinesin-8 motors regulate the size of microtubule structures, using length-dependent accumulation at the plus end to preferentially disassemble long microtubules. Despite extensive study, the kinesin-8 depolymerase mechanism remains under deb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfe23c6b76ace609ae173cab5f04f57c
https://europepmc.org/articles/PMC5573156/
https://europepmc.org/articles/PMC5573156/
Autor:
Peter A. Rubenstein, Ema Stokasimov
Publikováno v:
Journal of Biological Chemistry. 284:25421-25430
Actin can exist in multiple conformations necessary for normal function. Actin isoforms, although highly conserved in sequence, exhibit different biochemical properties and cellular roles. We used amide proton hydrogen/deuterium (HD) exchange detecte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::211544b75b870c2c66547f7c77a49d9b
https://doi.org/10.1074/jbc.m109.013078
https://doi.org/10.1074/jbc.m109.013078
Publikováno v:
Journal of Biological Chemistry. 283:34844-34854
Filament formation is required for most of the functions of actin. However, the intermonomer interactions that stabilize F-actin have not been elucidated because of a lack of an F-actin crystal structure. The Holmes muscle actin model suggests that a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2c61755ff2f7dd4d5f8f90cc28f7cb1
https://doi.org/10.1074/jbc.m804419200
https://doi.org/10.1074/jbc.m804419200
Publikováno v:
Molecular Biology of the Cell
The septin-associated kinase Gin4 is required for the localization and activation of Bnr1, and the septin Shs1 is essential for Bnr1 activation. The loss of Gin4 or Shs1 phenocopies the loss of Bnr1; these defects are suppressed by constitutive activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31097f5a6c874147ff7c156741087974
https://pubmed.ncbi.nlm.nih.gov/22918953
https://pubmed.ncbi.nlm.nih.gov/22918953
In the Saccharomyces cerevisiae actin-profilin interface, Ala(167) of the actin barbed end W-loop and His(372) near the C terminus form a clamp around a profilin segment containing residue Arg(81) and Tyr(79). Modeling suggests that altering steric p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1070fc2b3e680af44e20f4f29349df3
https://europepmc.org/articles/PMC3339942/
https://europepmc.org/articles/PMC3339942/
Publikováno v:
The Journal of biological chemistry. 285(27)
Intramolecular allosteric interactions responsible for actin conformational regulation are largely unknown. Previous work demonstrated that replacing yeast actin Val-76 with muscle actin Ile caused decreased nucleotide exchange. Residue 76 abuts Trp-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6e2ba7c3f44952b88a1c134d5ac89b7
https://pubmed.ncbi.nlm.nih.gov/20442407
https://pubmed.ncbi.nlm.nih.gov/20442407