SPKK, a new nucleic acid-binding unit of protein found in histone (Q28339810)

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scientific article (publication date: March 1989)

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English	SPKK, a new nucleic acid-binding unit of protein found in histone	scientific article (publication date: March 1989)

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instance of

scholarly article

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title

SPKK, a new nucleic acid-binding unit of protein found in histone (English)

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author name string

M Suzuki

series ordinal

1

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language of work or name

English

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publication date

March 1989

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published in

The EMBO Journal

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volume

8

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issue

3

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page(s)

797-804

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cites work

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Prediction of protein conformation

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Chain reversals in proteins

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Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes

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Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme

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The c-erb-A protein is a high-affinity receptor for thyroid hormone

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Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A

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Nucleosomal structure of sea urchin and starfish sperm chromatin. Histone H2B is possibly involved in determining the length of linker DNA.

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Hydrogen bonding in globular proteins

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Sequence of a Drosophila segmentation gene: protein structure homology with DNA-binding proteins

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DNA-Binding Proteins

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Isolation and characterization of the gene encoding the testis specific histone protein H2B-2 from the sea urchin Lytechinus pictus

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Physico-chemical study of the complexes of ‘33258 Hoechst’ with DNA and nucleohistone

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Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion

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Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule

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A low resolution structure for the histone core of the nucleosome

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Higher order structure of chromatin: orientation of nucleosomes within the 30 nm chromatin solenoid is independent of species and spacer length

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Structure of the nucleosome core particle at 7 Å resolution

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Identifiers

OpenCitations bibliographic resource ID

3186102

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3186102

PMC publication ID

400876

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3186102

PubMed publication ID

2470589

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3186102

 

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