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Molecular architecture of the mouse DNA polymerase alpha-primase complex
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
title
Molecular architecture of the mouse DNA polymerase alpha-primase complex
(English)
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
main subject
Polymerase (DNA directed), alpha 2
1 reference
stated in
GOA release 2020-03-11
Polymerase (DNA directed), alpha 1
1 reference
stated in
GOA release 2020-03-11
DNA primase, p49 subunit
1 reference
stated in
GOA release 2020-03-11
author name string
T. Mizuno
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
K. Yamagishi
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
H. Miyazawa
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
F. Hanaoka
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
language of work or name
English
0 references
publication date
1 November 1999
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
volume
19
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stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
page(s)
7886–7896
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stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
issue
11
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stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
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The second-largest subunit of the mouse DNA polymerase alpha-primase complex facilitates both production and nuclear translocation of the catalytic subunit of DNA polymerase alpha
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Identification of a point mutation in the cDNA of the catalytic subunit of DNA polymerase alpha from a temperature-sensitive mouse FM3A cell line
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The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing
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Evidence for a Cdc6p-independent mitotic resetting event involving DNA polymerase alpha.
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Identification of the nuclear localization signal of mouse DNA primase: nuclear transport of p46 subunit is facilitated by interaction with p54 subunit.
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Primary structure of T4 DNA polymerase. Evolutionary relatedness to eucaryotic and other procaryotic DNA polymerases.
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Catalytic subunit of human DNA polymerase alpha overproduced from baculovirus-infected insect cells. Structural and enzymological characterization
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2 June 2018
A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction
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2 June 2018
A novel family of DNA-polymerase-associated B subunits
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Primase activity of human DNA polymerase alpha-primase. Divalent cations stabilize the enzyme activity of the p48 subunit.
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27 November 2018
Dissociation and reconstitution of a DNA polymerase alpha-primase complex
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10523676
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
DNA primase-DNA polymerase alpha assembly from mouse FM3A cells. Purification of constituting enzymes, reconstitution, and analysis of RNA priming as coupled to DNA synthesis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10523676
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Peptide mapping of the four subunits of the mouse DNA polymerase alpha-primase complex
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10523676
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Cardioviral internal ribosomal entry site is functional in a genetically engineered dicistronic poliovirus
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10523676
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.19.11.7886
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PMCID
84873
0 references
PubMed ID
10523676
1 reference
stated in
PubMed
PubMed ID
10523676
retrieved
25 January 2017
ResearchGate publication ID
12776228
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