about
Histone H1 and HMG 14/17 are deposited nonrandomly in the nucleusPhosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei.The elusive structural role of ubiquitinated histones.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.Regulated protein turnover: snapshots of the proteasome in action.Organizational changes in chromatin at different malignant stages of Friend erythroleukemiaIsopeptidase: a novel eukaryotic enzyme that cleaves isopeptide bonds.Points of contact between histone H1 and the histone octamer.Reversible dissociation of linker histone from chromatin with preservation of internucleosomal repeat.High-resolution fractionation of nucleosomes: minor particles, "whiskers," and separation of mononucleosomes containing and lacking A24 semihistoneHistone H2A variants in nucleosomes and chromatin: more or less stable?Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae.Regulation of the higher-order structure of chromatin by histones H1 and H5Drosophila melanogaster H1 histone is phosphorylated stablyThe roles of H1, the histone core and DNA length in the unfolding of nucleosomes at low ionic strength.Iodination of nucleosomes at low ionic strength: conformational changes in H4 and stabilization by H1.Differential accessibility of (+/-) trans-7 beta, 8 alpha-dihydroxy-9 alpha, 10 alpha-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene to histone proteins.
P2860
Q24626596-76BD48AF-B8C2-48D8-89FA-F98D6ABF465CQ34450980-4F0F0093-E443-4E0A-A261-A18DE2A2A8AAQ34746899-EB70FDE3-2994-4DD8-B2E2-E0741C08C659Q34990282-4CEE1F52-B8D8-4455-8D91-26459A9F24B0Q35257872-102B5FB3-1E15-4487-8420-E364DC5B6E81Q35624674-995334E6-E9A6-459C-AC54-25BC6221147DQ36285091-06145E3F-02D3-4AE1-BE85-DBD72E48B68DQ36350495-04B0AF8A-AE93-444D-AE23-5B6FF5CDFF46Q36355826-683E2664-4C56-4929-BDE8-EFAD0246CD92Q36392424-973DBEF4-F932-4E95-841D-0C999025D22EQ36435083-89E48815-9B97-47F4-A326-1E6DD7D5089BQ36560155-37BFEBC1-119A-4561-A12C-0E032DB2A962Q36659577-CFBEEC74-6999-4A0E-9E71-60F2C85A854FQ36924186-99193A0C-B424-4017-ABAD-32877BB5C939Q40482491-A8F63D27-456D-4939-8284-CC002C8A3299Q40499721-E00B0B6B-2EA6-4386-BA5B-9DF3064B07DEQ44505115-A0E414AC-423B-4AE3-87E7-9588E9C77A7B
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1979
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Histone 1 is proximal to histone 2A and to A24.
@en
Histone 1 is proximal to histone 2A and to A24.
@nl
type
label
Histone 1 is proximal to histone 2A and to A24.
@en
Histone 1 is proximal to histone 2A and to A24.
@nl
prefLabel
Histone 1 is proximal to histone 2A and to A24.
@en
Histone 1 is proximal to histone 2A and to A24.
@nl
P2860
P356
P1476
Histone 1 is proximal to histone 2A and to A24.
@en
P2093
P2860
P304
P356
10.1073/PNAS.76.5.2190
P407
P577
1979-05-01T00:00:00Z