RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1 (Q24316431)

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English	RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1	scientific article

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instance of

scholarly article

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title

RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1 (English)

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main subject

Karyopherin subunit alpha 1

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stated in

GOA release 2020-03-11

regulation of DNA recombination

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stated in

GOA release 2020-03-11

author name string

P Cortes

series ordinal

1

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Z S Ye

series ordinal

2

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D Baltimore

series ordinal

3

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language of work or name

English

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publication date

2 August 1994

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published in

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

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volume

91

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issue

16

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page(s)

7633-7

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cites work

Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites

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Association of the APC gene product with beta-catenin

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19 March 2017

Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein

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Expression and V(D)J recombination activity of mutated RAG-1 proteins

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Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites

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19 March 2017

A repeating amino acid motif shared by proteins with diverse cellular roles

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PubMed Central

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19 March 2017

RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination

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PubMed Central

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RAG-1-deficient mice have no mature B and T lymphocytes

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PubMed Central

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RAG-2-deficient mice lack mature lymphocytes owing to inability to initiate V(D)J rearrangement

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PubMed Central

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Production of high-titer helper-free retroviruses by transient transfection

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pEF-BOS, a powerful mammalian expression vector

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Somatic generation of antibody diversity

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Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination

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Stable expression of immunoglobulin gene V(D)J recombinase activity by gene transfer into 3T3 fibroblasts

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The V(D)J recombination activating gene, RAG-1.

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VDJ recombination

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PubMed Central

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Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae

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V(D)J recombination in mammalian cell mutants defective in DNA double-strand break repair

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30 May 2018

Impairment of V(D)J recombination in double-strand break repair mutants

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PubMed Central

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30 May 2018

Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J joining signals

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PubMed Central

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30 May 2018

Two pairs of recombination signals are sufficient to cause immunoglobulin V-(D)-J joining

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stated in

PubMed Central

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Molecular analysis of the armadillo locus: uniformly distributed transcripts and a protein with novel internal repeats are associated with a Drosophila segment polarity gene

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PubMed Central

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30 May 2018

V(D)J recombination: a functional definition of the joining signals

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/8052633

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Visualization of replication factories attached to nucleoskeleton

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/8052633

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.91.16.7633

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3097432

ADS bibcode

1994PNAS...91.7633C

0 references

OpenCitations bibliographic resource ID

3097432

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3097432

PMC publication ID

44456

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3097432

PubMed publication ID

8052633

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3097432

ResearchGate publication ID

15145881

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