Results 171 to 180 of about 15,224 (199)

Identification of regulatory sequences in Aca11 and Aca13 for detection of anti-CRISPR and protein-protein interaction. [PDF]

Nucleic Acids Res
Song G, Li J, Han J, Gao X, Tian C, Zhang F, Tian Y.   +6 more
europepmc   +1 more source

Computational Kinetic Study on the Intramolecular H-Migration of Hydroperoxyalkylperoxy Radicals (•OOQOOH) in Normal-Alkyl Cyclohexanes. [PDF]

Molecules
Yao X, Li J, Li Z.
europepmc   +1 more source

Gluten Contamination of Rice: Analytical Testing <i>vs</i>. Consumer Perception - Is Rice Really Gluten Free? [PDF]

Food Technol Biotechnol
Bituh M, Gulin M, Marković K, Panjkota Krbavčić I, Vahčić N.   +4 more
europepmc   +1 more source

Regulation of anti-CRISPR operons by structurally distinct families of Aca proteins. [PDF]

Commun Biol
Lee SY, Birkholz N, Lee JH, Fineran PC, Park HH.   +4 more
europepmc   +1 more source

Localized 2'-OH Acylation at Poly(A) Extends RNA Translation. [PDF]

J Am Chem Soc
Fang L, Zhong W, Xiao L, Shioi R, Lee A, Bravo CH, Kool ET.   +6 more
europepmc   +1 more source

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R39 Rib Cage Stabilisation With 3D-Printed High-Density Polyethylene Sternal Prosthesis Post-Sternotomy Mediastinitis

Heart, Lung and Circulation, 2021
M. Prakash, Q. Ong, Casey Lo, A. E. Gamel   +3 more
semanticscholar   +2 more sources

Synthesis and evaluation of 3-(dihydroxyboryl)benzoic acids as D,D-carboxypeptidase R39 inhibitors.

Journal of Medicinal Chemistry, 2009
Penicillin binding proteins (PBPs) catalyze steps in the biosynthesis of bacterial cell walls and are the targets for the beta-lactam antibiotics. Non-beta-lactam based antibiotics that target PBPs are of interest because bacteria have evolved resistance to the beta-lactam antibiotics.
S. Inglis, A. Zervosen, E. Woon, T. Gerards, N. Teller, D. Fischer, A. Luxen, C. Schofield   +7 more
semanticscholar   +5 more sources

Actinomadura R39 d-Ala-d-Ala Carboxypeptidase [PDF]

, 2013
E. Sauvage, J. Frère
semanticscholar   +2 more sources

Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39 [PDF]

Nature, 1975
THE killing target of penicillin in bacteria is a membrane-bound transpeptidase which catalyses peptide cross linking during wall peptidoglycan synthesis1,2. Streptomyces R61 and R39 excrete during growth DD-carboxypeptidase-transpeptidase enzymes3,4 which seem to be soluble forms of the corresponding membrane-bound transpeptidases5.
J. Frère, J. Ghuysen, J. Degelaen, A. Loffet, H. Perkins   +4 more
semanticscholar   +4 more sources

Crystal structure of a complex between the Actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: interpretation of a transition state analogue in terms of catalytic mechanism.

Biochemistry, 2010
The Actinomadura R39 DD-peptidase is a bacterial low molecular weight class C penicillin-binding protein. It has previously been shown to catalyze hydrolysis and aminolysis of small D-alanyl-D-alanine terminating peptides, especially those with a side chain that mimics the amino terminus of the stem peptide precursor to the bacterial cell wall.
Liudmila Dzhekieva, M. Rocaboy, F. Kerff, P. Charlier, E. Sauvage, R. Pratt   +5 more
semanticscholar   +3 more sources