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Modular recognition of RNA by a human pumilio-homology domain
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scholarly article
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title
Modular recognition of RNA by a human pumilio-homology domain
(English)
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author name string
Xiaoqiang Wang
series ordinal
1
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Juanita McLachlan
series ordinal
2
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Phillip D Zamore
series ordinal
3
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Traci M Tanaka Hall
series ordinal
4
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language of work or name
English
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publication date
23 August 2002
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published in
Cell
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volume
110
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page(s)
501-12
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issue
4
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cites work
Control of the sperm–oocyte switch in Caenorhabditis elegans hermaphrodites by the fem-3 3′ untranslated region
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Maternal Pumilio acts together with Nanos in germline development in Drosophila embryos.
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Pumilio is essential for function but not for distribution of the Drosophila abdominal determinant Nanos.
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Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins
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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
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Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha
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A conserved RNA-binding protein controls germline stem cells in Caenorhabditis elegans
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Structure of Pumilio reveals similarity between RNA and peptide binding motifs
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Three-dimensional structure of the armadillo repeat region of beta-catenin
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Improved methods for building protein models in electron density maps and the location of errors in these models
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NANOS-3 and FBF proteins physically interact to control the sperm-oocyte switch in Caenorhabditis elegans.
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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PROCHECK: a program to check the stereochemical quality of protein structures
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Involvement of the pumilio gene in the transport of an abdominal signal in the Drosophila embryo
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Binding of pumilio to maternal hunchback mRNA is required for posterior patterning in Drosophila embryos
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Biochemical identification of Xenopus Pumilio as a sequence-specific cyclin B1 mRNA-binding protein that physically interacts with a Nanos homolog, Xcat-2, and a cytoplasmic polyadenylation element-binding protein.
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AMoRe: an automated package for molecular replacement
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The Puf3 protein is a transcript-specific regulator of mRNA degradation in yeast
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inferred from DOI database lookup
Recruitment of Nanos to hunchback mRNA by Pumilio
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reference URL
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inferred from DOI database lookup
Drosophila Brain Tumor is a translational repressor
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inferred from DOI database lookup
Post-transcriptional regulation through the HO 3'-UTR by Mpt5, a yeast homolog of Pumilio and FBF
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Crossref
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inferred from DOI database lookup
MOLREP: an Automated Program for Molecular Replacement
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Crossref
reference URL
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inferred from DOI database lookup
Crystal structure of a Pumilio homology domain
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The Pumilio RNA-binding domain is also a translational regulator.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2802%2900873-5
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The PUMILIO-RNA interaction: a single RNA-binding domain monomer recognizes a bipartite target sequence
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2802%2900873-5
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germ line
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2802%2900873-5
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S0092-8674(02)00873-5
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1751392
Fatcat ID
release_zp4binqvlzbrlkvfql42dvdeni
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OpenCitations bibliographic resource ID
1751392
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1751392
PubMed ID
12202039
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1751392
ResearchGate publication ID
11186594
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