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NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors.

NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Research Abstract Details 

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  • NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Abstract Text:

    kiran kumar singarapuKiran Kumar Singarapu,rong xiaoRong Xiao,thomas actonThomas Acton,burkhard rostBurkhard Rost,gaetano t montelioneGaetano T Montelione,thomas szyperskiThomas Szyperski,

    NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Publishing Authors By Initials

    kk singarapuKK Singarapu,r xiaoR Xiao,t actonT Acton,b rostB Rost,gt montelioneGT Montelione,t szyperskiT Szyperski,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Proteins

    VOLUME: 71

    Page Numbers: 1027-31

    Journal Abbreviation: Proteins

    ISSN: 1097-0134

    DAY: 1

    MONTH: May

    YEAR: 2008

    NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 8700181

    NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Keywords Mesh Terms:

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    Chemical & Substance for Abstract: NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Information

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    Grant and Affiliation Information for NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors.

    AFFILIATION: Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260-3000, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: U54 GM074958-01

    ACRONYM: GM

    MEDLINETA: Proteins

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    NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors Related Publications

     

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