Points of contact between histone H1 and the histone octamer. - Wikidata - awgldk - TriplyDB

Points of contact between histone H1 and the histone octamer.

Points of contact between histone H1 and the histone octamer.

http://www.wikidata.org/entity/Q36350495

about

Histone H1 and HMG 14/17 are deposited nonrandomly in the nucleus Competition between histone H1 and HMGN proteins for chromatin binding sites.Correlation between endogenous nucleosomal hyper(ADP-ribosyl)ation of histone H1 and the induction of chromatin relaxation.Use of histone antibodies for studying chromatin topography and the phosphorylation of chromatin subunits Chromatin fiber structure: morphology, molecular determinants, structural transitions.Contributions of linker histones and histone H3 to chromatin structure: scanning force microscopy studies on trypsinized fibers.The ninth Frederick H. Verhoeff lecture. The life history of retinal cells.Structure of chromatin and the linking number of DNA.Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei.Transferring DNA from electrophoretically resolved nucleosomes to diazobenzyloxymethyl cellulose: properties of nucleosomes along mouse satellite DNA Rearrangement of the histone H2A C-terminal domain in the nucleosome.Contacts of the globular domain of histone H5 and core histones with DNA in a "chromatosome".DNA and nucleosomes direct distinct folding of a linker histone H1 C-terminal domain.Immunodetection of histone epitopes correlates with early stages of apoptosis in activated human peripheral T lymphocytes.Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression.Participation of core histone "tails" in the stabilization of the chromatin solenoid Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome Aggregation of small oligonucleosomal chains into 300-A globular particles.Histone H2A variants in nucleosomes and chromatin: more or less stable?Laser Raman spectra of calf thymus chromatin and its constituents.The higher-order structure of chromatin: evidence for a helical ribbon arrangement.Histone H1 expressed in Saccharomyces cerevisiae binds to chromatin and affects survival, growth, transcription, and plasmid stability but does not change nucleosomal spacing Regulation of the higher-order structure of chromatin by histones H1 and H5 Drosophila melanogaster H1 histone is phosphorylated stably p53 chromatin epigenetic domain organization and p53 transcription.5-methylcytosine is localized in nucleosomes that contain histone H1.Structural insights into the histone H1-nucleosome complex A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: restriction by linker histones.Chromosome condensation induced by fostriecin does not require p34cdc2 kinase activity and histone H1 hyperphosphorylation, but is associated with enhanced histone H2A and H3 phosphorylation.Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations.Effects of cell cycle dependent histone H1 phosphorylation on chromatin structure and chromatin replication.Binding of NF1 to the MMTV promoter in nucleosomes: influence of rotational phasing, translational positioning and histone H1.The roles of H1, the histone core and DNA length in the unfolding of nucleosomes at low ionic strength.Cell-cycle-dependent dissociation of histone H1 from chromatin in nuclei of P. polycephalum.Iodination of nucleosomes at low ionic strength: conformational changes in H4 and stabilization by H1.Nucleosomal structure at hyperacetylated loci probed in nuclei by DNA-histone crosslinking.A lysine-rich protein functions as an H1 histone in Dictyostelium discoideum chromatin.Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini.At least 60 ADP-ribosylated variant histones are present in nuclei from dimethylsulfate-treated and untreated cells.

P2860

Q24626596-E3BD508F-154E-4507-8C26-CF2116AEA9BD Q33758098-AA619AB7-B147-426D-8206-2BC0DB76F543 Q33933862-04D648FC-0B39-4F19-90E5-D7AA7CC5F2A6 Q33940001-5E5387B3-0E9A-4F54-8169-E11B6FD3D8C9 Q34167910-4240308F-8921-4CDC-98FC-63470F98B308 Q34168034-66160E8E-7A01-41D6-BAC5-D825CE9E12E7 Q34212967-EF833B07-A50F-46DB-AC77-2240046FFE23 Q34273632-0BF807B7-730E-4D7B-AD30-A1E92586941F Q34450980-D7A7176E-183D-49FA-AD53-7CB9B4AABEF6 Q35490007-F50D7B56-AF92-49C5-AB33-C527901A61D2 Q35599382-D4BB3D8C-4F06-4E7F-853E-289193158DF6 Q35665946-DD1E2383-EF91-4629-B4B0-2E03C73ABB83 Q35780116-2534CBD2-4A13-4E78-B7C2-D90793F3CDBA Q35782613-A13CE3E7-1BF3-4CAF-8BCE-9982B953D08F Q35844218-210E4FA4-CF91-4947-8260-1FA3E3E6507A Q35908824-8F989DD0-440B-462E-A742-EDE7913F2A37 Q36208922-51BCF0D5-0C2E-4979-B0AA-058D223274E0 Q36411435-E951A459-0EB1-4816-8063-0B25B9E36D13 Q36414167-F89BE902-7EB0-4D80-BA4B-2078A47171A2 Q36435083-35C166F1-D4BE-44FE-9B05-BA6549867B2E Q36494586-FE5883E3-D41F-4373-B0F6-33795074F536 Q36510381-6D5800F5-2BE7-4858-B08A-5B25D2ECF4FC Q36651265-0F364B69-5D06-4B50-B328-7322ECA78CC9 Q36659577-53548904-DDDC-4FC3-B531-B09CC8822A13 Q36924186-AEF3BFCD-2139-4718-9EDB-F0A9B9126351 Q37033608-9394B04C-09D9-4900-8229-E9E7D62EEB6A Q37348455-4446C381-BA77-4C94-BE3C-4499513A41B4 Q37352963-15810163-15D8-4FC9-ADAB-CC11E1C8F7E1 Q37621095-CBB95DB8-C1D3-464D-A8E7-095736593870 Q37694723-A334F743-66F6-4662-9EE6-CF5525F2456D Q38684964-6958EAAC-68C9-4432-BD67-3C7F54A45199 Q39716084-E5964041-AE5C-46E0-A50F-06A64F35AB9C Q39721088-40E140C0-65EF-48F7-9402-65DF78DE4726 Q40482491-02AD1CCD-696B-4FB6-BA90-BD27DF9782DC Q40499508-5DDA2335-3D7A-4AE7-8C22-438132F2D3AB Q40499721-16C8D091-2D9B-489C-987E-9ED88EC3F12F Q40520078-763FF51E-B77D-4AE0-B8E3-713E5060FE14 Q40567607-EE0C8F53-642C-4AC0-91F6-AF961B5EEE29 Q40794274-C777F0A9-F3E7-4FD6-9AFA-1B0E07F1C384 Q41090533-EBEA566F-BD97-4C5C-BACD-2215FD2A25EF

P2860

Points of contact between histone H1 and the histone octamer.

http://www.wikidata.org/entity/Q36350495

description

1980 nî lūn-bûn

@nan

1980年の論文

@ja

1980年学术文章

@wuu

1980年学术文章

@zh-cn

1980年学术文章

@zh-hans

1980年学术文章

@zh-my

1980年学术文章

@zh-sg

1980年學術文章

@yue

1980年學術文章

@zh

1980年學術文章

@zh-hant

name

Points of contact between histone H1 and the histone octamer.

@ast

Points of contact between histone H1 and the histone octamer.

@en

type

label

Points of contact between histone H1 and the histone octamer.

@ast

Points of contact between histone H1 and the histone octamer.

@en

prefLabel

Points of contact between histone H1 and the histone octamer.

@ast

Points of contact between histone H1 and the histone octamer.

@en

P1433

Q36350495-60732C7C-B22F-4AB4-8301-E0AF9734E8FE

P1476

Q36350495-88C23641-80E3-4863-8533-9E08E591BFB2

P2093

Q36350495-2AA4DC32-92F1-4365-B88B-5C4B1BF5FF38

Q36350495-CE23B177-B3FF-4959-8313-2A5FD1CC5CB0

Q36350495-CE3D3E8D-2A62-444E-89DA-9792F19AAA56

P2860

Q36350495-04B0AF8A-AE93-444D-AE23-5B6FF5CDFF46

Q36350495-11EE375D-DC84-42BB-8428-941F8EC1B2D3

Q36350495-16BDD896-E826-4E85-BDBC-CFF4F6ADEBAF

Q36350495-17877EB8-0CFA-4D85-9ECB-171AF8CEE3A3

Q36350495-28889569-6E9E-4C15-BA44-A600C0367497

Q36350495-2AEC40C7-DE4C-4576-A468-41D5A3281ADD

Q36350495-2F0A4850-5C53-4F23-8941-13CB23D248C6

Q36350495-50977375-BB40-4C59-B4B5-6BD31E79A8F4

Q36350495-5931AAF2-2667-4F4A-9C25-B855595CCC5C

Q36350495-5F527BE6-1963-4B75-BD95-74D8995B2D8E

P304

Q36350495-274F13BA-922D-4AF4-A66D-8D0C5BD3DA8E

P31

Q36350495-6F03C38B-12D5-4C74-A1ED-464EEA5ECD0E

P356

Q36350495-803B48B3-1AAF-4BA3-81CA-78FDDDC84142

P407

Q36350495-28A2262B-29DB-4694-A45D-DF767512D240

P433

Q36350495-65F5B527-35C7-46F4-BDE6-B4A5541BF204

P478

Q36350495-F7517DBB-9670-4247-AE7F-55CD676CD807

P577

Q36350495-AA47C0A4-778E-4C96-8A56-586F41123B62

P5875

Q36350495-D53B08A3-94DB-473E-BE37-C76F23C6297E

P698

Q36350495-28CDE74A-1323-45BA-8F86-B7C6D43DBE35

P932

Q36350495-8063FCF6-08AB-4812-87EC-359CBEEB55BE

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Points of contact between histone H1 and the histone octamer.

@en

P2093

Boulikas T

http://www.w3.org/2001/XMLSchema#string

Garrard WT

http://www.w3.org/2001/XMLSchema#string

Wiseman JM

http://www.w3.org/2001/XMLSchema#string

P2860

Influence of histone H1 on chromatin structure

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis

Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. The properties of the N-terminal and C-terminal halves of histone H1.

Chromosomal proteins and chromatin structure.

An octamer of histones in chromatin and free in solution.

Chromatin architecture: investigation of a subunit of chromatin by dark field electron microscopy

Proximity and accessibility studies of histones in nuclei and free nucleosomes.

The effect of H1 histone on the action of DNA-relaxing enzyme

Studies on the interaction of H1 histone with superhelical DNA: characterization of the recognition and binding regions of H1 histones

Histone 1 is proximal to histone 2A and to A24.

P304

127-131

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.77.1.127

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

77

http://www.w3.org/2001/XMLSchema#string

P577

1980-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

16269640

http://www.w3.org/2001/XMLSchema#string

P698

6928607

http://www.w3.org/2001/XMLSchema#string

P932

348221

http://www.w3.org/2001/XMLSchema#string