DNA-induced secondary structure of the carboxyl-terminal domain of histone H1 (Q28910207)

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30 December 2019

title

DNA-induced secondary structure of the carboxyl-terminal domain of histone H1 (English)

2 references

7 March 2017

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30 December 2019

1 reference

GOA release 2020-03-11

H1.6 linker histone, cluster member

1 reference

GOA release 2020-03-11

author

Alicia Roque

1

1 reference

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30 December 2019

Ibón Iloro

2

1 reference

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30 December 2019

Inma Ponte

3

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30 December 2019

Pedro Suau

5

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30 December 2019

author name string

José Luis R Arrondo

4

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30 December 2019

language of work or name

English

0 references

publication date

8 July 2005

1 reference

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Journal of Biological Chemistry

30 December 2019

published in

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7 March 2017

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30 December 2019

volume

280

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7 March 2017

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30 December 2019

issue

37

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30 December 2019

page(s)

32141-32147

1 reference

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Developmentally regulated expression of linker-histone variants in vertebrates.

30 December 2019

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Modulation in proportions of H1 histone subfractions by differential changes in synthesis and turnover during butyrate treatment of neuroblastoma cells

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H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain

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Evolution of the vertebrate H1 histone class: evidence for the functional differentiation of the subtypes.

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In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor

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The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo

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The structure of histone H1 and its location in chromatin

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The preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domain

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The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA fragmentation factor (DFF40/CAD) and stimulates DNA cleavage.

21 January 2018

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Prediction of an HMG-box fold in the C-terminal domain of histone H1: insights into its role in DNA condensation.

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Induction of secondary structure in a COOH-terminal peptide of histone H1 by interaction with the DNA: an infrared spectroscopy study

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DNA-induced alpha-helical structure in the NH2-terminal domain of histone H1.

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An inducible helix-Gly-Gly-helix motif in the N-terminal domain of histone H1e: a CD and NMR study

21 January 2018

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Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.

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A bacterial TrwC relaxase domain contains a thermally stable alpha-helical core.

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Short alanine-based peptides may form 3(10)-helices and not alpha-helices in aqueous solution

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Protein motifs that recognize structural features of DNA

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Cooperative interaction of the C-terminal domain of histone H1 with DNA.

21 January 2018

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Counterion-induced condensation of deoxyribonucleic acid. A light-scattering study

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21 January 2018

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The importance of intrinsic disorder for protein phosphorylation

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Highly preferential nucleation of histone H1 assembly on scaffold-associated regions

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Identifiers

DOI

10.1074/JBC.M505636200

2 references

Consolidated OpenCitations Corpus – April 2017

4716948

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30 December 2019

4716948

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

4716948