about
An inducible helix-Gly-Gly-helix motif in the N-terminal domain of histone H1e: a CD and NMR studyThe preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domainInduction of secondary structure in a COOH-terminal peptide of histone H1 by interaction with the DNA: an infrared spectroscopy studyDNA-induced secondary structure of the carboxyl-terminal domain of histone H1Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin.Complex Evolutionary History of the Mammalian Histone H1.1-H1.5 Gene FamilyInterplay between histone H1 structure and function.Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Identification of novel post-translational modifications in linker histones from chicken erythrocytes.DNA sequence of the gene encoding the Zc1 protein from Zea mays W64 A.Sequence analysis of a genomic clone encoding a Zc2 protein from Zea mays W64 A.Sequence conservation of linker histones between chicken and mammalian species.Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation.Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1.Linker histone partial phosphorylation: effects on secondary structure and chromatin condensation.Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1.DNA-induced alpha-helical structure in the NH2-terminal domain of histone H1.Cloning and analysis of the coding region of the histone H1(0)-encoding gene from rat PC12 cells.Narrow A/T-rich zones present at the distal 5'-flanking sequences of the zein genes Zc1 and Zc2 bind a unique 30 kDa HMG-like protein.Contribution of hydrophobic interactions to the folding and fibrillation of histone H1 and its carboxy-terminal domain.Sequence complexity of histone H1 subtypes.Histone H1 Favors Folding and Parallel Fibrillar Aggregation of the 1–42 Amyloid-β PeptideA CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
P50
Q28345102-293A46E4-2C19-40DF-B4E1-F33A36B6C6E6Q28507683-03CF53AE-8C53-4547-A02B-C9FBC4989B78Q28910176-ADEE1714-88F1-4AD2-8DE8-24A143B0298DQ28910207-1755B433-9A6B-4620-B60E-3441CDDA9D15Q33284453-5B91359A-8C58-4246-A158-8EC88C13CAE9Q33590771-B8719FC1-BB59-475F-813D-4B77B9F8A3D6Q38594778-8C04D8BF-60A5-4B12-AAFA-98B8C512D826Q38813372-7E867046-661A-40AF-9A7E-3F8F4B74437EQ39089328-AD704AEE-B6B1-4CEB-B207-8CDB1F7C9D59Q40525705-9ED116EF-4BB8-4C40-AECA-D7177E596A6CQ40525717-115F873B-20A3-4D78-B82F-0B934EC2FA16Q40688282-479BDDFF-5619-4EF8-A3C2-8D0BCA592248Q41727351-F92B0416-CFCA-4EB5-A7D4-21D584B55ABEQ42078371-D90CF108-C024-4D63-A5D1-402B049F1D24Q42400861-9D193836-9E88-49D0-A853-FD56E5EFB52EQ43296549-695E50DA-DF4A-4FDE-AB20-DC320162E556Q43754780-85879B0A-2219-4EA8-8CE6-532355D1D12EQ48068537-D07E978A-DA95-49B2-848C-414BD7F2C26DQ48077473-F905433A-879A-4083-8F2E-A04F6CEE61ACQ50506566-ED3B8FA8-35EE-4893-AE92-4998EA715A76Q52604168-916D0ECD-E505-4BFC-AA3A-9664D382BF38Q58434267-9ECDDEEF-8CBA-4EA2-8239-23AD95C82DBDQ58565627-C08D08D0-5656-485B-8071-B59619D60309
P50
description
researcher ORCID 0000-0002-9448-6915
@en
wetenschapper
@nl
name
Inma Ponte
@ast
Inma Ponte
@en
Inma Ponte
@es
Inma Ponte
@nl
type
label
Inma Ponte
@ast
Inma Ponte
@en
Inma Ponte
@es
Inma Ponte
@nl
prefLabel
Inma Ponte
@ast
Inma Ponte
@en
Inma Ponte
@es
Inma Ponte
@nl
P106
P1153
6601983272
P31
P496
0000-0002-9448-6915