Articles - 1px3 mentioned but not cited (2)
- Defining the Design Parameters for in Vivo Enzyme Delivery Through Protein Spherical Nucleic Acids. Kusmierz CD, Bujold KE, Callmann CE, Mirkin CA. ACS Cent Sci 6 815-822 (2020)
- Transferrin Aptamers Increase the In Vivo Blood-Brain Barrier Targeting of Protein Spherical Nucleic Acids. Kusmierz CD, Callmann CE, Kudruk S, Distler ME, Mirkin CA. Bioconjug Chem 33 1803-1810 (2022)
Reviews citing this publication (1)
- LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance. Juers DH, Matthews BW, Huber RE. Protein Sci 21 1792-1807 (2012)
Articles citing this publication (15)
- Cost-benefit tradeoffs in engineered lac operons. Eames M, Kortemme T. Science 336 911-915 (2012)
- Studies of translational misreading in vivo show that the ribosome very efficiently discriminates against most potential errors. Manickam N, Nag N, Abbasi A, Patel K, Farabaugh PJ. RNA 20 9-15 (2014)
- Structural basis of specificity in tetrameric Kluyveromyces lactis β-galactosidase. Pereira-Rodríguez A, Fernández-Leiro R, González-Siso MI, Cerdán ME, Becerra M, Sanz-Aparicio J. J Struct Biol 177 392-401 (2012)
- Protein engineering of a cold-active beta-galactosidase from Arthrobacter sp. SB to increase lactose hydrolysis reveals new sites affecting low temperature activity. Coker JA, Brenchley JE. Extremophiles 10 515-524 (2006)
- Structural explanation for allolactose (lac operon inducer) synthesis by lacZ β-galactosidase and the evolutionary relationship between allolactose synthesis and the lac repressor. Wheatley RW, Lo S, Jancewicz LJ, Dugdale ML, Huber RE. J Biol Chem 288 12993-13005 (2013)
- 1.8 Å resolution structure of β-galactosidase with a 200 kV CRYO ARM electron microscope. Merk A, Fukumura T, Zhu X, Darling JE, Grisshammer R, Ognjenovic J, Subramaniam S. IUCrJ 7 639-643 (2020)
- 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 88 861-869 (2010)
- Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site. Sutendra G, Wong S, Fraser ME, Huber RE. Biochem Biophys Res Commun 352 566-570 (2007)
- Crystal structure of β1→6-galactosidase from Bifidobacterium bifidum S17: trimeric architecture, molecular determinants of the enzymatic activity and its inhibition by α-galactose. Godoy AS, Camilo CM, Kadowaki MA, Muniz HD, Espirito Santo M, Murakami MT, Nascimento AS, Polikarpov I. FEBS J 283 4097-4112 (2016)
- Analysis of intracellular enzyme activity by surface enhanced Raman scattering. Stevenson R, McAughtrie S, Senior L, Stokes RJ, McGachy H, Tetley L, Nativo P, Brewer JM, Alexander J, Faulds K, Graham D. Analyst 138 6331-6336 (2013)
- 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 88 969-979 (2010)
- Diversity in lac Operon Regulation among Diverse Escherichia coli Isolates Depends on the Broader Genetic Background but Is Not Explained by Genetic Relatedness. Phillips KN, Widmann S, Lai HY, Nguyen J, Ray JCJ, Balázsi G, Cooper TF. mBio 10 e02232-19 (2019)
- 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 93 531-540 (2015)
- Structure-activity relationships on the study of β-galactosidase folding/unfolding due to interactions with immobilization additives: Triton X-100 and ethanol. Soto D, Escobar S, Guzmán F, Cárdenas C, Bernal C, Mesa M. Int J Biol Macromol 96 87-92 (2017)
- The functional mutational landscape of the lacZ gene. Beal MA, Meier MJ, Dykes A, Yauk CL, Lambert IB, Marchetti F. iScience 26 108407 (2023)