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Posttranslational NH2-Terminal Aminoacylation
scientific article published on January 1, 1978
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scholarly article
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Europe PubMed Central
PubMed ID
352619
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14 September 2017
review article
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Europe PubMed Central
title
Posttranslational NH2-Terminal Aminoacylation
(English)
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Crossref
DOI
10.1016/B978-0-12-152813-3.50005-7
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https://api.crossref.org/works/10.1016/B978-0-12-152813-3.50005-7
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25 June 2022
author name string
C. E. Deutch
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1
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PubMed ID
352619
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25 June 2022
R. C. Scarpulla
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2
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Europe PubMed Central
PubMed ID
352619
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A352619
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25 June 2022
R. L. Soffer
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3
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Europe PubMed Central
PubMed ID
352619
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A352619
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25 June 2022
language of work or name
English
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National Center for Biotechnology Information
PubMed ID
352619
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=352619
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25 June 2022
publication date
1 January 1978
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Europe PubMed Central
PubMed ID
352619
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14 September 2017
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https://api.elsevier.com/content/article/PII:B9780121528133500057?httpAccept=text/xml
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DOI
10.1016/B978-0-12-152813-3.50005-7
reference URL
https://api.crossref.org/works/10.1016/B978-0-12-152813-3.50005-7
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25 June 2022
https://api.elsevier.com/content/article/PII:B9780121528133500057?httpAccept=text/plain
1 reference
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Crossref
DOI
10.1016/B978-0-12-152813-3.50005-7
reference URL
https://api.crossref.org/works/10.1016/B978-0-12-152813-3.50005-7
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25 June 2022
published in
Current Topics in Cellular Regulation
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Europe PubMed Central
PubMed ID
352619
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14 September 2017
volume
13
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Europe PubMed Central
PubMed ID
352619
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14 September 2017
page(s)
1-28
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Europe PubMed Central
PubMed ID
352619
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14 September 2017
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A soluble preparation from rat brain that incorporates into its own proteins ( 14 C)arginine by a ribonuclease-sensitive system and ( 14 C)tyrosine by a ribonuclease-insensitive system
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Mechanism of tryptophanase induction in Escherichia coli
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Bovine parathyroid hormone: amino acid sequence
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The N-terminal region of soluble proteins from procaryotes and eucaryotes
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Amino terminal amino acid sequences and carbohydrate of the two major forms of rabbit plasminogen
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Regulation of Proline Degradation inSalmonella typhimurium
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Regulation of proline catabolism by leucyl,phenylalanyl-tRNA-protein transferase
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Pleiotropic phenotype of an Escherichia coli mutant lacking leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase
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Relationship between the tonB locus and iron transport in Escherichia coli
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Occurrence of arginyl-tRNA:Protein arginyl transferase in baker's yeast
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Incorporation of methionine by a soluble enzyme system from Escherichia coli
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A soluble amino acid incorporating system
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Further studies on the soluble amino acid incorporating system from rat liver
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Amino acid sequence of Escherichia coli alkaline phosphatase. Amino- and carboxyl-terminal sequences and variations between two isoenzymes
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Non-ribosomal incorporation of arginine into a specific protein by a cell-free extract of parathyroid tissue
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A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins
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Modification of a specific ribosomal protein catalyzed by leucyl, phenylalanyl-tRNA: protein transferase
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An arginyl-transfer ribonucleic Acid protein transferase from cereal embryos.
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The structure of enterochelin and related 2,3-dihydroxy-N-benzoyne conjugates from Eschericha Coli
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The incorporation of amino acids into proteins of chloramphenicol particles in Escherichia coli
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Protein Methylation
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Acetylation of ribosome-associated proteins in vitro by an acetyltransferase bound to rat liver ribosomes
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10.1016/B978-0-12-152813-3.50005-7
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Utilization of isoaccepting leucyl-tRNA in the soluble incorporation system and protein synthesizing systems from E.coli
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NH2-Terminal Residues ofNeurospora crassaProteins
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Histidine decarboxylase of Lactobacillus 30a. V. Origin of enzyme-bound pyruvate and separation of nonidentical subunits
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5 April 2023
Effects of Tris and dimethylsulfoxide on the aminoacylation of Escherichia coli valine transfer RNA by Neurospora crassa phenylalanyl transfer RNA synthetase
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10.1016/B978-0-12-152813-3.50005-7
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Processing of newly synthesized histone molecules
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Taxonomic Comparison of the Amino Termini of Microbial Cell Proteins
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5 April 2023
Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase
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5 April 2023
Post-translational modification of proteins catalyzed by aminoacyl-tRNA-protein transferases
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10.1016/B978-0-12-152813-3.50005-7
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5 April 2023
Origin of the Alps and Western Mediterranean
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10.1016/B978-0-12-152813-3.50005-7
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5 April 2023
Arginyl-tRNA-protein transferase in eucaryotic protists
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10.1016/B978-0-12-152813-3.50005-7
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5 April 2023
Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm
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5 April 2023
Incorporation of arginine by a soluble system from sheep thyroid
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5 April 2023
A Mutant of Escherichia coli Defective in Leucyl, Phenylalanyl-tRNA-Protein Transferase
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79
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10.1016/B978-0-12-152813-3.50005-7
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5 April 2023
Polypeptide Chain Initiation: Nucleotide Sequences of the Three Ribosomal Binding Sites in Bacteriophage R17 RNA
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81
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10.1016/B978-0-12-152813-3.50005-7
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5 April 2023
Synthesis of Lens Protein in vitro. N-Terminal Acetylation of alpha-Crystallin
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10.1016/B978-0-12-152813-3.50005-7
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5 April 2023
Cancer Research
series ordinal
85
volume
34
page(s)
2204
author name string
Tanaka
publication date
1974
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DOI
10.1016/B978-0-12-152813-3.50005-7
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THE NH2-TERMINAL RESIDUES OF THE PROTEINS FROM CELL-FREE EXTRACTS OF E. COLI
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5 April 2023
Studies on the composition of the protein from Escherichia coli ribosomes
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10.1016/B978-0-12-152813-3.50005-7
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Studies on the primary structure of 20 proteins fromEscherichia coliribosomes by means of an improved protein sequenator
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89
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10.1016/B978-0-12-152813-3.50005-7
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5 April 2023
Identifiers
DOI
10.1016/B978-0-12-152813-3.50005-7
1 reference
stated in
National Center for Biotechnology Information
PubMed ID
352619
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=352619
retrieved
25 June 2022
PubMed ID
352619
1 reference
stated in
Europe PubMed Central
PubMed ID
352619
retrieved
14 September 2017
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