Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex (Q24673361): Difference between revisions

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Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex
description / hydescription / hy
գիտական հոդված
1999 թվականի ապրիլին հրատարակված գիտական հոդված
description / pt-brdescription / pt-br
artigo científico
artigo científico (publicado na 1999)
description / hywdescription / hyw
 
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
description / bndescription / bn
 
১৯৯৯-এ প্রকাশিত বৈজ্ঞানিক নিবন্ধ
description / fadescription / fa
 
مقالهٔ علمی
description / urdescription / ur
 
سائنسی مضمون
Property / cites work
 
Property / cites work: The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties / rank
 
Normal rank
Property / cites work: The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
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based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Antheprot: An interactive graphics software for analyzing protein structures from sequences / rank
 
Normal rank
Property / cites work: Antheprot: An interactive graphics software for analyzing protein structures from sequences / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro / rank
 
Normal rank
Property / cites work: Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. II. Structural characterization of the polypeptide components and immunological identification of the methionyl-tRNA synthetase subunit / rank
 
Normal rank
Property / cites work: Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. II. Structural characterization of the polypeptide components and immunological identification of the methionyl-tRNA synthetase subunit / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Perturbation of the aminoacyl-tRNA synthetase complex by salts and detergents. Importance of hydrophobic interactions and possible involvement of lipids / rank
 
Normal rank
Property / cites work: Perturbation of the aminoacyl-tRNA synthetase complex by salts and detergents. Importance of hydrophobic interactions and possible involvement of lipids / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase / rank
 
Normal rank
Property / cites work: Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex / rank
 
Normal rank
Property / cites work: A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Leucyl-tRNA and lysyl-tRNA synthetases, derived from the high-Mr complex of sheep liver, are hydrophobic proteins / rank
 
Normal rank
Property / cites work: Leucyl-tRNA and lysyl-tRNA synthetases, derived from the high-Mr complex of sheep liver, are hydrophobic proteins / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Expression of the aminoacyl-tRNA synthetase complex in cultured Chinese hamster ovary cells. Specific depression of the methionyl-tRNA synthetase component upon methionine restriction / rank
 
Normal rank
Property / cites work: Expression of the aminoacyl-tRNA synthetase complex in cultured Chinese hamster ovary cells. Specific depression of the methionyl-tRNA synthetase component upon methionine restriction / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Aspartyl-tRNA synthetase from rat: in vitro functional analysis of its assembly into the multisynthetase complex / rank
 
Normal rank
Property / cites work: Aspartyl-tRNA synthetase from rat: in vitro functional analysis of its assembly into the multisynthetase complex / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: The two-hybrid system: an assay for protein-protein interactions / rank
 
Normal rank
Property / cites work: The two-hybrid system: an assay for protein-protein interactions / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Characterization of a novel N-terminal peptide in human aspartyl-tRNA synthetase. Roles in the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha / rank
 
Normal rank
Property / cites work: Characterization of a novel N-terminal peptide in human aspartyl-tRNA synthetase. Roles in the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / cites work
 
Property / cites work: Modular design of components of the operational RNA code for alanine in evolution / rank
 
Normal rank
Property / cites work: Modular design of components of the operational RNA code for alanine in evolution / reference
 
stated in: PubMed
reference URL: https://pubmed.ncbi.nlm.nih.gov/10200289
retrieved: 12 December 2020
Timestamp+2020-12-12T00:00:00Z
Timezone+00:00
CalendarGregorian
Precision1 day
Before0
After0

based on heuristic: inferred from PubMed ID database lookup
Property / main subject
 
Property / main subject: protein-protein interaction / rank
 
Normal rank
Property / main subject: protein-protein interaction / reference
 
Property / ADS bibcode
 
Property / ADS bibcode: 1999PNAS...96.4488R / rank
 
Normal rank

Latest revision as of 04:06, 23 August 2023

scientific article
Language Label Description Also known as
English
Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex
scientific article

    Statements

    title
    Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex (English)
    0 references
    author name string
    S B Rho
    series ordinal
    1
    0 references
    M J Kim
    series ordinal
    2
    0 references
    J S Lee
    series ordinal
    3
    0 references
    W Seol
    series ordinal
    4
    0 references
    H Motegi
    series ordinal
    5
    0 references
    S Kim
    series ordinal
    6
    0 references
    K Shiba
    series ordinal
    7
    0 references
    publication date
    13 April 1999
    0 references
    volume
    96
    0 references
    issue
    8
    0 references
    page(s)
    4488-93
    0 references
    cites work

    Identifiers

    PMC publication ID
    16359
    0 references
     
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