Catalogo Articoli (Spogli Riviste)

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La ricerca find articoli where soggetti phrase all words 'LIGATED-T' sort by level,fasc_key/DESCEND, pagina_ini_num/ASCEND ha restituito 9 riferimenti
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    1. Jin, L; Stec, B; Lipscomb, WN; Kantrowitz, ER
      Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 angstrom

      PROTEINS-STRUCTURE FUNCTION AND GENETICS
    2. Dubecq, V; Thia-Toong, TL; Charlier, D; Villeret, V; Roovers, M; Wattiez, R; Legrain, C; Glansdorff, N
      Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius - Cloning, sequence analysis, enzyme purification and characterization

      EUROPEAN JOURNAL OF BIOCHEMISTRY
    3. HA Y; ALLEWELL NM
      INTERSUBUNIT HYDROGEN-BOND ACTS AS A GLOBAL MOLECULAR SWITCH IN ESCHERICHIA-COLI ASPARTATE TRANSCARBAMOYLASE

      Proteins
    4. Williams, MK; Kantrowitz, ER
      Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase

      BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
    5. WILLIAMS MK; STEC B; KANTROWITZ ER
      A SINGLE MUTATION IN THE REGULATORY CHAIN OF ESCHERICHIA-COLI ASPARTATE TRANSCARBAMOYLASE RESULTS IN AN EXTREME T-STATE STRUCTURE

      Journal of Molecular Biology
    6. DUTTA M; KANTROWITZ ER
      THE INFLUENCE OF THE REGULATORY CHAIN AMINO-ACIDS GLU-62 AND ILE-12 ON THE HETEROTROPIC PROPERTIES OF ESCHERICHIA-COLI ASPARTATE TRANSCARBAMOYLASE

      Biochemistry
    7. LIU LY; WALES ME; WILD JR
      CONVERSION OF THE ALLOSTERIC REGULATORY PATTERNS OF ASPARTATE TRANSCARBAMOYLASE BY EXCHANGE OF A SINGLE BETA-STRAND BETWEEN DIVERGED REGULATORY CHAINS

      Biochemistry
    8. BAKER DP; FETLER L; KEISER RT; VACHETTE P; KANTROWITZ ER
      WEAKENING OF THE INTERFACE BETWEEN ADJACENT CATALYTIC CHAINS PROMOTESDOMAIN CLOSURE IN ESCHERICHIA-COLI ASPARTATE TRANSCARBAMOYLASE

      Protein science
    9. BAKER DP; STEBBINS JW; DESENA E; KANTROWITZ ER
      GLUTAMIC-ACID-86 IS IMPORTANT FOR POSITIONING THE 80S LOOP AND ARGININE-54 AT THE ACTIVE-SITE OF ESCHERICHIA-COLI ASPARTATE TRANSCARBAMOYLASE AND FOR THE STRUCTURAL STABILIZATION OF THE C1-C2 INTERFACE

      The Journal of biological chemistry


ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/10/20 alle ore 14:13:24