PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Keogh, M.C.* ; Almouzni, G.* ; Andrews, A.J.* ; Armache, K.J.* ; Arrowsmith, C.H.* ; Baek, S.H.* ; Bedford, M.T.* ; Bernstein, E.* ; Côté, J.-A.* ; David, Y.* ; Denu, J.M.* ; Fierz, B.* ; Garcia, B.A.* ; Glass, K.C.* ; Gozani, O.* ; Helin, K.* ; Henikoff, S.* ; Jensen, O.N.* ; Josefowicz, S.Z.* ; Kelleher, N.L.* ; Kutateladze, T.G.* ; Lindner, H.H.* ; Lu, C.* ; Luger, K.* ; Mallick, P.* ; Musselman, C.A.* ; Muir, T.W.* ; Pasa-Tolic, L.* ; Schneider, R. ; Shi, X.* ; Shi, Y.* ; Sidoli, S.* ; Smith, L.M.* ; Tyler, J.K.* ; Wolberger, C.* ; Workman, J.L.* ; Strahl, B.D.* ; Young, N.L.*

A needed nomenclature for nucleosomes.

Mol. Cell 85, 3554-3561 (2025)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Histone post-translational modifications (PTMs) are crucial to eukaryotic genome regulation, with a range of reported functions and mechanisms of action. Though often studied individually, it has long been recognized that the modifications function by combinatorial synergy or antagonism. Interplay may involve PTMs on the same histone, within the same nucleosome (containing a histone octamer), or between nucleosomes in higher-order chromatin. Given this, the field must distinguish ever greater complexity, and the context in which it is studied, with brevity and precision. The proteoform was introduced to define individual forms of a protein by sequence and PTMs, followed by the nucleoform to describe the particular gathering of histones within an individual nucleosome. There is now a need to define specific forms of these entities in prose while providing space for experimental nuance. To this end, we introduce a nomenclature that can express discrete PTMs, proteoforms, nucleoforms, or situations where defined PTMs exist in an uncertain context. Though specifically designed for the chromatin field, adaptions of the framework could be used to describe—and thus dissect—how proteoforms are configured in functionally distinct complexes across biology.
Impact Factor
Scopus SNIP
Altmetric
16.600
2.895
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Posttranslational Modification; Crystal-structure; Histone H3.3; Proteoform; Chromatin; Reveals
Sprache englisch
Veröffentlichungsjahr 2025
HGF-Berichtsjahr 2025
ISSN (print) / ISBN 1097-2765
e-ISSN 1097-4164
Zeitschrift Molecular Cell
Quellenangaben Band: 85, Heft: 19, Seiten: 3554-3561 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Functional Epigenetics (IFE)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Helmholtz Diabetes Center
PSP-Element(e) G-502800-001
DOI 10.1016/j.molcel.2025.08.029
WOS ID 001589254400001
Scopus ID 105017234334
PubMed ID 41043390
Erfassungsdatum 2025-10-16
[➜Korrektur melden]