BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

273 related articles for article (PubMed ID: 22155115)

  • 1. Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop.
    Jancewicz LJ; Wheatley RW; Sutendra G; Lee M; Fraser ME; Huber RE
    Arch Biochem Biophys; 2012 Jan; 517(2):111-22. PubMed ID: 22155115
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Importance of Arg-599 of β-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop.
    Dugdale ML; Vance ML; Wheatley RW; Driedger MR; Nibber A; Tran A; Huber RE
    Biochem Cell Biol; 2010 Dec; 88(6):969-79. PubMed ID: 21102659
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Substitution for Asn460 cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability.
    Wheatley RW; Kappelhoff JC; Hahn JN; Dugdale ML; Dutkoski MJ; Tamman SD; Fraser ME; Huber RE
    Arch Biochem Biophys; 2012 May; 521(1-2):51-61. PubMed ID: 22446164
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase (Escherichia coli).
    Dugdale ML; Dymianiw DL; Minhas BK; D'Angelo I; Huber RE
    Biochem Cell Biol; 2010 Oct; 88(5):861-9. PubMed ID: 20921997
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase.
    Juers DH; Hakda S; Matthews BW; Huber RE
    Biochemistry; 2003 Nov; 42(46):13505-11. PubMed ID: 14621996
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Catalytic role for arginine 188 in the C-C hydrolase catalytic mechanism for Escherichia coli MhpC and Burkholderia xenovorans LB400 BphD.
    Li C; Li JJ; Montgomery MG; Wood SP; Bugg TD
    Biochemistry; 2006 Oct; 45(41):12470-9. PubMed ID: 17029402
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer.
    Huber RE; Hakda S; Cheng C; Cupples CG; Edwards RA
    Biochemistry; 2003 Feb; 42(6):1796-803. PubMed ID: 12578395
    [TBL] [Abstract][Full Text] [Related]  

  • 8. His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis.
    Roth NJ; Rob B; Huber RE
    Biochemistry; 1998 Jul; 37(28):10099-107. PubMed ID: 9665715
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.
    Poyner RR; Larsen TM; Wong SW; Reed GH
    Arch Biochem Biophys; 2002 May; 401(2):155-63. PubMed ID: 12054465
    [TBL] [Abstract][Full Text] [Related]  

  • 10. A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase.
    Xu J; McRae MA; Harron S; Rob B; Huber RE
    Biochem Cell Biol; 2004 Apr; 82(2):275-84. PubMed ID: 15060622
    [TBL] [Abstract][Full Text] [Related]  

  • 11. An allolactose trapped at the lacZ β-galactosidase active site with its galactosyl moiety in a (4)H3 conformation provides insights into the formation, conformation, and stabilization of the transition state.
    Wheatley RW; Huber RE
    Biochem Cell Biol; 2015 Dec; 93(6):531-40. PubMed ID: 26291713
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism.
    Kang YN; Tanabe A; Adachi M; Utsumi S; Mikami B
    Biochemistry; 2005 Apr; 44(13):5106-16. PubMed ID: 15794648
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance of hydrophobic side chains and a helix N-capping position for stability and catalysis.
    Lassila JK; Keeffe JR; Kast P; Mayo SL
    Biochemistry; 2007 Jun; 46(23):6883-91. PubMed ID: 17506527
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Kinetic characterization of the Escherichia coli oligopeptidase A (OpdA) and the role of the Tyr(607) residue.
    Lorenzon RZ; Cunha CE; Marcondes MF; Machado MF; Juliano MA; Oliveira V; Travassos LR; Paschoalin T; Carmona AK
    Arch Biochem Biophys; 2010 Aug; 500(2):131-6. PubMed ID: 20513640
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Characterization of the side-chain hydroxyl moieties of residues Y56, Y111, Y238, Y338, and S339 as determinants of specificity in E. coli cystathionine β-lyase.
    Lodha PH; Aitken SM
    Biochemistry; 2011 Nov; 50(45):9876-85. PubMed ID: 21958132
    [TBL] [Abstract][Full Text] [Related]  

  • 16. The role of the L2 loop in the regulation and maintaining the proteolytic activity of HtrA (DegP) protein from Escherichia coli.
    Sobiecka-Szkatula A; Gieldon A; Scire A; Tanfani F; Figaj D; Koper T; Ciarkowski J; Lipinska B; Skorko-Glonek J
    Arch Biochem Biophys; 2010 Aug; 500(2):123-30. PubMed ID: 20515644
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Catalytic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: site-directed mutagenesis and biochemical studies.
    Li Y; Wu Y; Blaszczyk J; Ji X; Yan H
    Biochemistry; 2003 Feb; 42(6):1581-8. PubMed ID: 12578371
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.
    Kityk R; Kopp J; Sinning I; Mayer MP
    Mol Cell; 2012 Dec; 48(6):863-74. PubMed ID: 23123194
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: a flexible loop stabilizes the transition state.
    Lee M; Maher MJ; Christopherson RI; Guss JM
    Biochemistry; 2007 Sep; 46(37):10538-50. PubMed ID: 17711307
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase.
    Yamashita K; Nakajima Y; Matsushita H; Nishiya Y; Yamazawa R; Wu YF; Matsubara F; Oyama H; Ito K; Yoshimoto T
    J Mol Biol; 2010 Mar; 396(4):1081-96. PubMed ID: 20043918
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 14.