| Year |
Citation |
Score |
| 2020 |
Mehaffey MR, Ahn Y-C, Rivera DD, Thomas PW, Cheng Z, Crowder MW, Pratt RF, Fast W, Brodbelt JS. Elusive structural changes of New Delhi metallo-β-lactamase revealed by ultraviolet photodissociation mass spectrometry Chemical Science. 11: 8999-9010. DOI: 10.1039/D0Sc02503H |
0.366 |
|
| 2019 |
Thomas PW, Cammarata MB, Brodbelt JS, Monzingo AF, Pratt RF, Fast W. A Lysine-Targeted Affinity Label for Serine β-Lactamase Also Covalently Modifies New Delhi Metallo-β-Lactamase-1 (NDM-1). Biochemistry. PMID 31145588 DOI: 10.1021/Acs.Biochem.9B00393 |
0.512 |
|
| 2019 |
Malico AA, Dave K, Adediran SA, Pratt RF. Specificity of extended O-aryloxycarbonyl hydroxamates as inhibitors of a class C β-lactamase. Bioorganic & Medicinal Chemistry. PMID 30792103 DOI: 10.1016/J.Bmc.2019.02.023 |
0.495 |
|
| 2019 |
Cabaret D, Adediran SA, Garcia Gonzalez MJ, Pratt RF, Wakselman M. Synthesis and Reactivity with beta-Lactamases of "Penicillin-like" Cyclic Depsipeptides. The Journal of Organic Chemistry. 64: 713-720. PMID 11674137 DOI: 10.1021/jo980564 |
0.54 |
|
| 2018 |
Adediran SA, Sarkar KS, Pratt RF. Kinetic Evidence for a Second Ligand Binding Site on Streptococcus pneumoniae Penicillin-Binding Protein 2x. Biochemistry. PMID 29485264 DOI: 10.1021/Acs.Biochem.7B01209 |
0.532 |
|
| 2016 |
Adediran SA, Pratt RF. Penicillin acylase and O-Acyl hydroxamates: Two acyl-enzymes, one leading to hydrolysis, the other to inactivation. Archives of Biochemistry and Biophysics. PMID 28038956 DOI: 10.1016/J.Abb.2016.12.009 |
0.478 |
|
| 2016 |
Nemmara VV, Nicholas RA, Pratt RF. Synthesis and Kinetic Analysis of Two Conformationally Restricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5. Biochemistry. PMID 27420403 DOI: 10.1021/Acs.Biochem.6B00576 |
0.402 |
|
| 2016 |
Pratt RF. β-Lactamases: Why and How. Journal of Medicinal Chemistry. 59: 8207-20. PMID 27232275 DOI: 10.1021/acs.jmedchem.6b00448 |
0.329 |
|
| 2015 |
Tilvawala R, Cammarata M, Adediran SA, Brodbelt JS, Pratt RF. A New Covalent Inhibitor of Class C β-Lactamases Reveals Extended Active Site Specificity. Biochemistry. PMID 26651220 DOI: 10.1021/Acs.Biochem.5B01149 |
0.565 |
|
| 2014 |
Dzhekieva L, Adediran SA, Pratt RF. Interactions of "bora-penicilloates" with serine β-lactamases and DD-peptidases. Biochemistry. 53: 6530-8. PMID 25302576 DOI: 10.1021/Bi500970F |
0.507 |
|
| 2014 |
Dave K, Palzkill T, Pratt RF. Neutral β-Lactams Inactivate High Molecular Mass Penicillin-Binding Proteins of Class B1, Including PBP2a of MRSA. Acs Medicinal Chemistry Letters. 5: 154-7. PMID 24900789 DOI: 10.1021/Ml400408C |
0.386 |
|
| 2013 |
Tilvawala R, Pratt RF. Kinetics of action of a two-stage pro-inhibitor of serine β-lactamases. Biochemistry. 52: 7060-70. PMID 24070199 DOI: 10.1021/Bi400873R |
0.515 |
|
| 2013 |
Tilvawala R, Pratt RF. Covalent inhibition of serine β-lactamases by novel hydroxamic acid derivatives. Biochemistry. 52: 3712-20. PMID 23679223 DOI: 10.1021/Bi4003887 |
0.534 |
|
| 2013 |
Nemmara VV, Adediran SA, Dave K, Duez C, Pratt RF. Dual substrate specificity of Bacillus subtilis PBP4a. Biochemistry. 52: 2627-37. PMID 23560856 DOI: 10.1021/Bi400211Q |
0.543 |
|
| 2013 |
Dzhekieva L, Adediran SA, Herman R, Kerff F, Duez C, Charlier P, Sauvage E, Pratt RF. Inhibition of DD-peptidases by a specific trifluoroketone: crystal structure of a complex with the Actinomadura R39 DD-peptidase. Biochemistry. 52: 2128-38. PMID 23484909 DOI: 10.1021/Bi400048S |
0.534 |
|
| 2012 |
Shilabin AG, Dzhekieva L, Misra P, Jayaram B, Pratt RF. 4-quinolones as noncovalent inhibitors of high molecular mass penicillin-binding proteins. Acs Medicinal Chemistry Letters. 3: 592-5. PMID 24900515 DOI: 10.1021/Ml3001006 |
0.453 |
|
| 2012 |
Adediran SA, Lin G, Pelto RB, Pratt RF. Crossover inhibition as an indicator of convergent evolution of enzyme mechanisms: a β-lactamase and a N-terminal nucleophile hydrolase. Febs Letters. 586: 4186-9. PMID 23098756 DOI: 10.1016/J.Febslet.2012.10.019 |
0.816 |
|
| 2012 |
Pelto RB, Pratt RF. Kinetics and stereochemistry of hydrolysis of an N-(phenylacetyl)-α-hydroxyglycine ester catalyzed by serine β-lactamases and DD-peptidases. Organic & Biomolecular Chemistry. 10: 7356-62. PMID 22851054 DOI: 10.1039/C2Ob25585E |
0.814 |
|
| 2012 |
Dzhekieva L, Kumar I, Pratt RF. Inhibition of bacterial DD-peptidases (penicillin-binding proteins) in membranes and in vivo by peptidoglycan-mimetic boronic acids. Biochemistry. 51: 2804-11. PMID 22443299 DOI: 10.1021/Bi300148V |
0.478 |
|
| 2011 |
Nemmara VV, Dzhekieva L, Sarkar KS, Adediran SA, Duez C, Nicholas RA, Pratt RF. Substrate specificity of low-molecular mass bacterial DD-peptidases. Biochemistry. 50: 10091-101. PMID 22029692 DOI: 10.1021/Bi201326A |
0.508 |
|
| 2011 |
Zervosen A, Herman R, Kerff F, Herman A, Bouillez A, Prati F, Pratt RF, Frère JM, Joris B, Luxen A, Charlier P, Sauvage E. Unexpected tricovalent binding mode of boronic acids within the active site of a penicillin-binding protein. Journal of the American Chemical Society. 133: 10839-48. PMID 21574608 DOI: 10.1021/Ja200696Y |
0.44 |
|
| 2011 |
Adediran SA, Kumar I, Nagarajan R, Sauvage E, Pratt RF. Kinetics of reactions of the Actinomadura R39 DD-peptidase with specific substrates. Biochemistry. 50: 376-87. PMID 21182324 DOI: 10.1021/Bi101760P |
0.695 |
|
| 2010 |
Pelto RB, Pratt RF. Serendipitous discovery of α-hydroxyalkyl esters as β-lactamase substrates. Biochemistry. 49: 10496-506. PMID 21087009 DOI: 10.1021/Bi101071R |
0.818 |
|
| 2010 |
Pratt RF, McLeish MJ. Structural relationship between the active sites of β-lactam-recognizing and amidase signature enzymes: convergent evolution? Biochemistry. 49: 9688-97. PMID 20977193 DOI: 10.1021/Bi1012222 |
0.521 |
|
| 2010 |
Nicola G, Tomberg J, Pratt RF, Nicholas RA, Davies C. Crystal structures of covalent complexes of β-lactam antibiotics with Escherichia coli penicillin-binding protein 5: toward an understanding of antibiotic specificity. Biochemistry. 49: 8094-104. PMID 20726582 DOI: 10.1021/Bi100879M |
0.472 |
|
| 2010 |
Dzhekieva L, Rocaboy M, Kerff F, Charlier P, Sauvage E, Pratt RF. 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. 49: 6411-9. PMID 20608745 DOI: 10.1021/Bi100757C |
0.489 |
|
| 2010 |
Adediran SA, Cabaret D, Lohier JF, Wakselman M, Pratt RF. Substituted aryl malonamates as new serine β-lactamase substrates: Structure-activity studies Bioorganic and Medicinal Chemistry. 18: 282-291. PMID 19932622 DOI: 10.1016/J.Bmc.2009.10.056 |
0.492 |
|
| 2009 |
Sauvage E, Zervosen A, Dive G, Herman R, Amoroso A, Joris B, Fonzé E, Pratt RF, Luxen A, Charlier P, Kerff F. Structural basis of the inhibition of class A beta-lactamases and penicillin-binding proteins by 6-beta-iodopenicillanate. Journal of the American Chemical Society. 131: 15262-9. PMID 19919161 DOI: 10.1021/Ja9051526 |
0.568 |
|
| 2009 |
Majumdar S, Pratt RF. Intramolecular cooperativity in the reaction of diacyl phosphates with serine beta-lactamases. Biochemistry. 48: 8293-8. PMID 19678666 DOI: 10.1021/Bi900808X |
0.692 |
|
| 2009 |
Majumdar S, Pratt RF. Inhibition of class A and C beta-lactamases by diaroyl phosphates. Biochemistry. 48: 8285-92. PMID 19678665 DOI: 10.1021/Bi900807E |
0.715 |
|
| 2009 |
Ganta SR, Perumal S, Pagadala SR, Samuelsen O, Spencer J, Pratt RF, Buynak JD. Approaches to the simultaneous inactivation of metallo- and serine-beta-lactamases. Bioorganic & Medicinal Chemistry Letters. 19: 1618-22. PMID 19243936 DOI: 10.1016/J.Bmcl.2009.02.018 |
0.786 |
|
| 2008 |
Pelto RB, Pratt RF. Kinetics and mechanism of inhibition of a serine beta-lactamase by O-aryloxycarbonyl hydroxamates. Biochemistry. 47: 12037-46. PMID 18942857 DOI: 10.1021/Bi8015247 |
0.825 |
|
| 2008 |
Adediran SA, Pratt RF. Inhibition of serine β-lactamases by vanadate-catechol complexes Biochemistry. 47: 9467-9474. PMID 18702503 DOI: 10.1021/bi801153j |
0.318 |
|
| 2008 |
Sauvage E, Powell AJ, Heilemann J, Josephine HR, Charlier P, Davies C, Pratt RF. Crystal structures of complexes of bacterial DD-peptidases with peptidoglycan-mimetic ligands: the substrate specificity puzzle. Journal of Molecular Biology. 381: 383-93. PMID 18602645 DOI: 10.1016/J.Jmb.2008.06.012 |
0.824 |
|
| 2008 |
Perumal SK, Adediran SA, Pratt RF. Beta-ketophosphonates as beta-lactamase inhibitors: Intramolecular cooperativity between the hydrophobic subsites of a class D beta-lactamase. Bioorganic & Medicinal Chemistry. 16: 6987-94. PMID 18572409 DOI: 10.1016/J.Bmc.2008.05.045 |
0.8 |
|
| 2008 |
Pratt RF. Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins) Cellular and Molecular Life Sciences. 65: 2138-2155. PMID 18408890 DOI: 10.1007/S00018-008-7591-7 |
0.484 |
|
| 2007 |
Kumar I, Josephine HR, Pratt RF. Reactions of peptidoglycan-mimetic beta-lactams with penicillin-binding proteins in vivo and in membranes. Acs Chemical Biology. 2: 620-4. PMID 17894439 DOI: 10.1021/Cb7001347 |
0.823 |
|
| 2007 |
Wyrembak PN, Babaoglu K, Pelto RB, Shoichet BK, Pratt RF. O-aryloxycarbonyl hydroxamates: new beta-lactamase inhibitors that cross-link the active site. Journal of the American Chemical Society. 129: 9548-9. PMID 17628063 DOI: 10.1021/Ja072370U |
0.811 |
|
| 2007 |
Sauvage E, Duez C, Herman R, Kerff F, Petrella S, Anderson JW, Adediran SA, Pratt RF, Frère JM, Charlier P. Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptide. Journal of Molecular Biology. 371: 528-39. PMID 17582436 DOI: 10.1016/J.Jmb.2007.05.071 |
0.394 |
|
| 2007 |
Moulin A, Bell JH, Pratt RF, Ringe D. Inhibition of chymotrypsin by a complex of ortho-vanadate and benzohydroxamic acid: structure of the inert complex and its mechanistic interpretation. Biochemistry. 46: 5982-90. PMID 17469803 DOI: 10.1021/Bi6025209 |
0.494 |
|
| 2006 |
Josephine HR, Charlier P, Davies C, Nicholas RA, Pratt RF. Reactivity of penicillin-binding proteins with peptidoglycan-mimetic beta-lactams: what's wrong with these enzymes? Biochemistry. 45: 15873-83. PMID 17176110 DOI: 10.1021/Bi061804F |
0.821 |
|
| 2006 |
Adediran SA, Kumar I, Pratt RF. Deacylation transition states of a bacterial DD-peptidase. Biochemistry. 45: 13074-82. PMID 17059224 DOI: 10.1021/Bi061341D |
0.48 |
|
| 2006 |
Adediran SA, Cabaret D, Flavell RR, Sammons JA, Wakselman M, Pratt RF. Synthesis and β-lactamase reactivity of α-substituted phenaceturates Bioorganic and Medicinal Chemistry. 14: 7023-7033. PMID 16806948 DOI: 10.1016/J.Bmc.2006.06.023 |
0.461 |
|
| 2006 |
Perumal SK, Pratt RF. Synthesis and evaluation of ketophosph(on)ates as beta-lactamase inhibitors. The Journal of Organic Chemistry. 71: 4778-85. PMID 16776502 DOI: 10.1021/Jo060364V |
0.766 |
|
| 2006 |
Adediran SA, Lohier JF, Cabaret D, Wakselman M, Pratt RF. Synthesis and reactivity with β-lactamases of a monobactam bearing a retro-amide side chain Bioorganic and Medicinal Chemistry Letters. 16: 869-871. PMID 16300942 DOI: 10.1016/J.Bmcl.2005.11.006 |
0.407 |
|
| 2005 |
Majumdar S, Adediran SA, Nukaga M, Pratt RF. Inhibition of class D beta-lactamases by diaroyl phosphates. Biochemistry. 44: 16121-9. PMID 16331972 DOI: 10.1021/Bi051719S |
0.726 |
|
| 2005 |
Adediran SA, Nukaga M, Baurin S, Frère JM, Pratt RF. Inhibition of class D β-lactamases by Acyl phosphates and phosphonates Antimicrobial Agents and Chemotherapy. 49: 4410-4412. PMID 16189136 DOI: 10.1128/Aac.49.10.4410-4412.2005 |
0.451 |
|
| 2005 |
Kumar I, Pratt RF. Transpeptidation reactions of a specific substrate catalyzed by the streptomyces R61 DD-peptidase: characterization of a chromogenic substrate and acyl acceptor design. Biochemistry. 44: 9971-9. PMID 16042374 DOI: 10.1021/Bi050542Z |
0.495 |
|
| 2005 |
Kumar I, Pratt RF. Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 DD-peptidase: the structural basis of acyl acceptor specificity. Biochemistry. 44: 9961-70. PMID 16042373 DOI: 10.1021/Bi0505417 |
0.496 |
|
| 2005 |
Adediran SA, Zhang Z, Nukaga M, Palzkill T, Pratt RF. The D-methyl group in β-lactamase evolution: Evidence from the Y221G and GC1 mutants of the class C β-lactamase of Enterobacter cloacae P99 Biochemistry. 44: 7543-7552. PMID 15895997 DOI: 10.1021/Bi050136F |
0.506 |
|
| 2005 |
Silvaggi NR, Josephine HR, Kuzin AP, Nagarajan R, Pratt RF, Kelly JA. Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin". Journal of Molecular Biology. 345: 521-33. PMID 15581896 DOI: 10.1016/J.Jmb.2004.10.076 |
0.812 |
|
| 2004 |
Nagarajan R, Pratt RF. Synthesis and evaluation of new substrate analogues of streptomyces R61 DD-peptidase: dissection of a specific ligand. The Journal of Organic Chemistry. 69: 7472-8. PMID 15497971 DOI: 10.1021/Jo048885A |
0.654 |
|
| 2004 |
Adediran SA, Cabaret D, Lohier JF, Wakselman M, Pratt RF. Benzopyranones with retro-amide side chains as (inhibitory) β-lactamase substrates Bioorganic and Medicinal Chemistry Letters. 14: 5117-5120. PMID 15380211 DOI: 10.1016/J.Bmcl.2004.07.067 |
0.487 |
|
| 2004 |
Nagarajan R, Pratt RF. Thermodynamic evaluation of a covalently bonded transition state analogue inhibitor: inhibition of beta-lactamases by phosphonates. Biochemistry. 43: 9664-73. PMID 15274621 DOI: 10.1021/Bi049309B |
0.663 |
|
| 2004 |
Josephine HR, Kumar I, Pratt RF. The perfect penicillin? Inhibition of a bacterial DD-peptidase by peptidoglycan-mimetic beta-lactams. Journal of the American Chemical Society. 126: 8122-3. PMID 15225046 DOI: 10.1021/Ja048850S |
0.811 |
|
| 2004 |
Silvaggi NR, Kaur K, Adediran SA, Pratt RF, Kelly JA. Toward better antibiotics: crystallographic studies of a novel class of DD-peptidase/beta-lactamase inhibitors. Biochemistry. 43: 7046-53. PMID 15170342 DOI: 10.1021/Bi049612C |
0.598 |
|
| 2004 |
Ahn YM, Pratt RF. Kinetic and structural consequences of the leaving group in substrates of a class C β-lactamase Bioorganic and Medicinal Chemistry. 12: 1537-1542. PMID 15018927 DOI: 10.1016/J.Bmc.2003.12.042 |
0.461 |
|
| 2004 |
Kumar S, Adediran SA, Nukaga M, Pratt RF. Kinetics of turnover of cefotaxime by the Enterobacter cloacae P99 and GCl beta-lactamases: two free enzyme forms of the P99 beta-lactamase detected by a combination of pre- and post-steady state kinetics. Biochemistry. 43: 2664-72. PMID 14992604 DOI: 10.1021/Bi030212J |
0.651 |
|
| 2004 |
Nukaga M, Kumar S, Nukaga K, Pratt RF, Knox JR. Hydrolysis of third-generation cephalosporins by class C beta-lactamases. Structures of a transition state analog of cefotoxamine in wild-type and extended spectrum enzymes. The Journal of Biological Chemistry. 279: 9344-52. PMID 14660590 DOI: 10.1074/jbc.M312356200 |
0.67 |
|
| 2003 |
Cabaret D, Adediran SA, Pratt RF, Wakselman M. New substrates for β-lactam-recognizing enzymes: Aryl malonamates Biochemistry. 42: 6719-6725. PMID 12779326 DOI: 10.1021/bi0300478 |
0.516 |
|
| 2003 |
Anderson JW, Adediran SA, Charlier P, Nguyen-Distèche M, Frère JM, Nicholas RA, Pratt RF. On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides. The Biochemical Journal. 373: 949-55. PMID 12723972 DOI: 10.1042/Bj20030217 |
0.441 |
|
| 2003 |
Kaur K, Adediran SA, Lan MJK, Pratt RF. Inhibition of β-lactamases by monocyclic acyl phosph(on)ates Biochemistry. 42: 1529-1536. PMID 12578365 DOI: 10.1021/Bi020602Q |
0.522 |
|
| 2003 |
Silvaggi NR, Anderson JW, Brinsmade SR, Pratt RF, Kelly JA. The crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state. Biochemistry. 42: 1199-208. PMID 12564922 DOI: 10.1021/Bi0268955 |
0.553 |
|
| 2002 |
McDonough MA, Anderson JW, Silvaggi NR, Pratt RF, Knox JR, Kelly JA. Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins. Journal of Molecular Biology. 322: 111-22. PMID 12215418 DOI: 10.1016/S0022-2836(02)00742-8 |
0.563 |
|
| 2002 |
Bell JH, Pratt RF. Mechanism of inhibition of the beta-lactamase of Enterobacter cloacae P99 by 1:1 complexes of vanadate with hydroxamic acids. Biochemistry. 41: 4329-38. PMID 11914079 DOI: 10.1021/Bi012096V |
0.479 |
|
| 2002 |
Pratt RF. Functional evolution of the serine β-lactamase active site Journal of the Chemical Society, Perkin Transactions 2. 851-861. DOI: 10.1039/B107097P |
0.512 |
|
| 2001 |
Morrison MJ, Li N, Pratt RF. Inverse acyl phosph(on)ates: substrates or inhibitors of beta-lactam-recognizing enzymes? Bioorganic Chemistry. 29: 271-81. PMID 16256697 DOI: 10.1006/Bioo.2001.1218 |
0.617 |
|
| 2001 |
Kaur K, Lan MJK, Pratt RF. Mechanism of inhibition of the class C β-lactamase of Enterobacter cloacae P99 by cyclic acyl phosph(on)ates: Rescue by return Journal of the American Chemical Society. 123: 10436-10443. PMID 11673973 DOI: 10.1021/Ja011094V |
0.55 |
|
| 2001 |
Kumar S, Pearson AL, Pratt RF. Design, synthesis, and evaluation of alpha-ketoheterocycles as class C beta-lactamase inhibitors. Bioorganic & Medicinal Chemistry. 9: 2035-44. PMID 11504640 DOI: 10.1016/S0968-0896(01)00107-9 |
0.651 |
|
| 2001 |
Adediran SA, Cabaret D, Drouillat B, Pratt RF, Wakselman M. The synthesis and evaluation of benzofuranones as β-lactamase substrates Bioorganic and Medicinal Chemistry. 9: 1175-1183. PMID 11377176 DOI: 10.1016/S0968-0896(00)00345-X |
0.458 |
|
| 2001 |
Bebrone C, Moali C, Mahy F, Rival S, Docquier JD, Rossolini GM, Fastrez J, Pratt RF, Frère JM, Galleni M. CENTA as a chromogenic substrate for studying β-lactamases Antimicrobial Agents and Chemotherapy. 45: 1868-1871. PMID 11353639 DOI: 10.1128/Aac.45.6.1868-1871.2001 |
0.389 |
|
| 2001 |
Kaur K, Pratt RF. Mechanism of reaction of acyl phosph(on)ates with the β-lactamase of Enterobacter cloacae P99 Biochemistry. 40: 4610-4621. PMID 11294628 DOI: 10.1021/BI002243+ |
0.519 |
|
| 2001 |
Cabaret D, Garcia Gonzalez M, Wakselman M, Adediran SA, Pratt RF. Synthesis, hydrolysis, and evaluation of 3-acylamino-3,4-dihydro-2-oxo-2H-1,3-benzoxazinecarboxylic acids and linear azadepsipeptides as potential substrates/inhibitors of β-lactam-recognizing enzymes European Journal of Organic Chemistry. 141-149. DOI: 10.1002/1099-0690(200101)2001:1<141::Aid-Ejoc141>3.0.Co;2-J |
0.412 |
|
| 2000 |
Anderson JW, Pratt RF. Dipeptide binding to the extended active site of the Streptomyces R61 D-alanyl-D-alanine-peptidase: The path to a specific substrate Biochemistry. 39: 12200-12209. PMID 11015198 DOI: 10.1021/Bi001295W |
0.492 |
|
| 2000 |
Bell JH, Curley K, Pratt RF. Inhibition of serine amidohydrolases by complexes of vanadate with hydroxamic acids Biochemical and Biophysical Research Communications. 274: 732-735. PMID 10924345 DOI: 10.1006/Bbrc.2000.3195 |
0.44 |
|
| 2000 |
Curley K, Pratt RF. The oxyanion hole in serine β-lactamase catalysis: Interactions of thiono substrates with the active site Bioorganic Chemistry. 28: 338-356. DOI: 10.1006/Bioo.2000.1184 |
0.5 |
|
| 1999 |
Graves-Woodward K, Pratt RF. Interactions of soluble penicillin-binding protein 2a of methicillin- resistant Staphylococcus aureus with moenomycin Biochemistry. 38: 10533-10542. PMID 10441150 DOI: 10.1021/Bi982309P |
0.375 |
|
| 1999 |
Bernstein NJ, Pratt RF. On the importance of a methyl group in β-lactamase evolution: Free energy profiles and molecular modeling Biochemistry. 38: 10499-10510. PMID 10441146 DOI: 10.1021/bi990428e |
0.384 |
|
| 1999 |
Adediran SA, Cabaret D, Pratt RF, Wakselman M. A 'cephalosporin-like' cyclic depsipeptide: Synthesis and reaction with β-lactam-recognizing enzymes Bioorganic and Medicinal Chemistry Letters. 9: 341-346. PMID 10091681 DOI: 10.1016/S0960-894X(98)00739-2 |
0.514 |
|
| 1999 |
Adediran SA, Pratt RF. β-secondary and solvent deuterium kinetic isotope effects on catalysis by the streptomyces R61 DD-peptidase: Comparisons with a structurally similar class C β-lactamase Biochemistry. 38: 1469-1477. PMID 9931012 DOI: 10.1021/bi982308x |
0.387 |
|
| 1999 |
Cabaret D, Adediran SA, Garcia Gonzalez MJ, Pratt RF, Wakselman M. Synthesis and reactivity with β-lactamases of 'penicillin-like' cyclic depsipeptides Journal of Organic Chemistry. 64: 713-720. DOI: 10.1021/Jo980564+ |
0.548 |
|
| 1998 |
Graves-Woodward K, Pratt RF. Reaction of soluble penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus with β-lactams and acyclic substrates: Kinetics in homogeneous solution Biochemical Journal. 332: 755-761. PMID 9620879 DOI: 10.1042/Bj3320755 |
0.441 |
|
| 1998 |
Maveyraud L, Pratt RF, Samama JP. Crystal structure of an acylation transition-state analog of the TEM-1 β-lactamase. Mechanistic implications for class A β-lactamases Biochemistry. 37: 2622-2628. PMID 9485412 DOI: 10.1021/Bi972501B |
0.373 |
|
| 1998 |
Li N, Pratt RF. Inhibition of serine β-lactamases by acyl phosph(on)ates: A new source of inert acyl [and phosphyl] enzymes Journal of the American Chemical Society. 120: 4264-4268. DOI: 10.1021/ja9741537 |
0.365 |
|
| 1998 |
Pratt RF, Hammar NJ. Salicyloyl cyclic phosphate, a 'penicillin-like' inhibitor of β- lactamases Journal of the American Chemical Society. 120: 3004-3006. DOI: 10.1021/ja973313b |
0.419 |
|
| 1997 |
Li N, Rahil J, Wright ME, Pratt RF. Structure-activity studies of the inhibition of serine β-lactamases by phosphonate monoesters Bioorganic and Medicinal Chemistry. 5: 1783-1788. PMID 9354233 DOI: 10.1016/S0968-0896(97)00103-X |
0.449 |
|
| 1997 |
Curley K, Pratt RF. Structure of an α-Keto β-Amido Acid, 3-(Phenylacetamido)pyruvic Acid, and Its Methyl Ester in the Solid State and in Organic and Aqueous Solvents Journal of Organic Chemistry. 62: 4479-4483. DOI: 10.1021/Jo970223G |
0.304 |
|
| 1997 |
Curley K, Pratt RF. Effectiveness of tetrahedral adducts as transition-state analogs and inhibitors of the class C β-lactamase of Enterobacter cloacae P99 Journal of the American Chemical Society. 119: 1529-1538. DOI: 10.1021/Ja9634942 |
0.449 |
|
| 1996 |
Adediran SA, Deraniyagala SA, Xu Y, Pratt RF. β-Secondary and solvent deuterium kinetic isotope effects on β-lactamase catalysis Biochemistry. 35: 3604-3613. PMID 8639512 DOI: 10.1021/Bi952107I |
0.436 |
|
| 1996 |
Xu Y, Soto G, Hirsch KR, Pratt RF. Kinetics and mechanism of the hydrolysis of depsipeptides catalyzed by the β-lactamase of Enterobacter cloacae P99 Biochemistry. 35: 3595-3603. PMID 8639511 DOI: 10.1021/Bi952106Q |
0.527 |
|
| 1996 |
Pratt RF, Dryjanski M, Wun ES, Marathias VM. 8-Hydroxypenillic acid from 6-aminopenicillanic acid: A new reaction catalyzed by a class C β-lactamase Journal of the American Chemical Society. 118: 8207-8212. DOI: 10.1021/ja961685z |
0.389 |
|
| 1995 |
Pratt RF. Inactivation of the enterobacter cloacae P99 β-lactamase by a fluorescent phosphonate: Direct detection of ligand binding at the second site Biochemistry®. 34: 3569-3575. PMID 7893653 |
0.376 |
|
| 1995 |
Pratt RF. Steady-state kinetics of the binding of β-lactams and penicilloates to the second binding site of the enterobacter cloacae P99 β-lactamase Biochemistry®. 34: 3561-3568. PMID 7893652 |
0.346 |
|
| 1994 |
Rahil J, Pratt RF. Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: Phosphonate monoester inhibitors of a β-lactamase Biochemistry. 33: 116-125. PMID 8286328 DOI: 10.1021/Bi00167A015 |
0.439 |
|
| 1994 |
Lobkovsky E, Billings EM, Moews PC, Rahil J, Pratt RF, Knox JR. Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a β-lactamase transition-state analog Biochemistry. 33: 6762-6772. PMID 8204611 DOI: 10.1021/Bi00188A004 |
0.468 |
|
| 1994 |
Xu Y, Soto G, Adachi H, Van der Linden MPG, Keck W, Pratt RF. Relative specificities of a series of β-lactam recognizing enzymes towards the side chains of penicillins and of acyclic thioldepsipeptides Biochemical Journal. 302: 851-856. PMID 7945212 DOI: 10.1042/Bj3020851 |
0.476 |
|
| 1994 |
Cabaret D, Liu J, Wakselman M, Pratt RF, Xub Y. Functionalized depsipeptides, substrates and inhibitors of β-lactamases and DD-peptidases Bioorganic and Medicinal Chemistry. 2: 757-771. PMID 7894969 DOI: 10.1016/S0968-0896(00)82175-6 |
0.534 |
|
| 1994 |
Xu Y, Pratt RF. β-lactam-recognizing enzymes exhibit different structural specificity in acyclic amide and ester substrates: a starting point in β-lactamase evolution? Bioorganic and Medicinal Chemistry Letters. 4: 2291-2296. DOI: 10.1016/0960-894X(94)85027-5 |
0.38 |
|
| 1993 |
Pratt RF. Kinetics and mechanism of β-lactamase inhibition by phosphonamidates: The quest for a proton Biochemistry. 32: 10763-10772. PMID 8399224 DOI: 10.1021/Bi00091A030 |
0.455 |
|
| 1993 |
Rahil J, Pratt RF. Structure-activity relationships in the inhibition of serine β-lactamases by phosphonic acid derivatives Biochemical Journal. 296: 389-393. PMID 8257429 DOI: 10.1042/Bj2960389 |
0.501 |
|
| 1993 |
Chen CC, Rahil J, Pratt RF, Herzberg O. Structure of a phosphonate-inhibited beta-lactamase. An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis. Journal of Molecular Biology. 234: 165-78. PMID 8230196 DOI: 10.1006/Jmbi.1993.1571 |
0.51 |
|
| 1992 |
Rahil J, Pratt RF. Mechanism of inhibition of the class C β-lactamase of Enterobacter cloacae P99 by phosphonate monoesters Biochemistry. 31: 5869-5878. PMID 1610830 DOI: 10.1021/Bi00140A024 |
0.557 |
|
| 1992 |
Pratt RF, Krishnaraj R, Xu H. Effect of side-chain amide thionation on turnover of β-lactam substrates by β-lactamases. Further evidence on the question of side-chain hydrogen-bonding in catalysis Biochemical Journal. 286: 857-862. PMID 1417747 DOI: 10.1042/Bj2860857 |
0.464 |
|
| 1992 |
Pratt RF. On the definition and classification of mechanism-based Enzyme Inhibitors Bioorganic and Medicinal Chemistry Letters. 2: 1323-1326. DOI: 10.1016/S0960-894X(00)80506-5 |
0.423 |
|
| 1991 |
Murphy BP, Pratt RF. N-(phenylacetyl)glycyl-D-aziridine-2-carboxylate, an acyclic amide substrate of beta-lactamases: importance of the shape of the substrate in beta-lactamase evolution. Biochemistry. 30: 3640-9. PMID 2015222 DOI: 10.1021/Bi00229A008 |
0.594 |
|
| 1991 |
Mazzella LJ, Pazhanisamy S, Pratt RF. Evidence from a mutant β-lactamase for the mechanism of β-lactamase-catalysed depsipeptide aminolysis Biochemical Journal. 274: 855-859. PMID 2012612 DOI: 10.1042/Bj2740855 |
0.484 |
|
| 1991 |
Knap AK, Pratt RF. Inactivation of the RTEM-1 cysteine β-lactamase by iodoacetate. The nature of active-site functional groups and comparisons with the native enzyme Biochemical Journal. 273: 85-91. PMID 1989590 DOI: 10.1042/Bj2730085 |
0.475 |
|
| 1991 |
Rahil J, Pratt RF. Phosphonate monoester inhibitors of class A β-lactamases Biochemical Journal. 275: 793-795. PMID 1903928 DOI: 10.1042/Bj2750793 |
0.525 |
|
| 1991 |
Rahil J, Pratt RF. Intramolecular participation of the amide group in acid- and base-catalysed phosphonate monoester hydrolysis Journal of the Chemical Society, Perkin Transactions 2. 947-950. DOI: 10.1039/P29910000947 |
0.408 |
|
| 1990 |
Knox JR, Pratt RF. Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein Antimicrobial Agents and Chemotherapy. 34: 1342-1347. PMID 2386365 |
0.307 |
|
| 1989 |
Pazhanisamy S, Pratt RF. β-Lactamase-catalyzed aminolysis of depsipeptides: Peptide inhibition and a new kinetic mechanism Biochemistry. 28: 6875-6882. PMID 2819040 |
0.41 |
|
| 1989 |
Pazhanisamy S, Govardhan CP, Pratt RF. β-Lactamase-catalyzed aminolysis of depsipeptides: Amine specificity and steady-state kinetics Biochemistry. 28: 6863-6870. PMID 2819039 |
0.351 |
|
| 1989 |
Pratt RF. Inhibition of a class C β-lactamase by a specific phosphonate monoester Science. 246: 917-919. PMID 2814513 |
0.402 |
|
| 1989 |
Mazzella LJ, Pratt RF. Effect of the 3'-leaving group on turnover of cephem antibiotics by a class C β-lactamse Biochemical Journal. 259: 255-260. PMID 2785791 DOI: 10.1042/Bj2590255 |
0.467 |
|
| 1989 |
Knap AK, Pratt RF. Chemical modifications of the RTEM-1 thiol β-lactamase by thiol-selective reagents: Evidence for activation of the primary nucleophile of the β-lactamase active site by adjacent functional groups Proteins: Structure, Function and Genetics. 6: 316-323. PMID 2695930 DOI: 10.1002/Prot.340060314 |
0.47 |
|
| 1989 |
Pazhanisamy S, Pratt RF. β-Lactamase-catalyzed aminolysis of depsipeptides: Proof of the nonexistence of a specific D-phenylalanine/enzyme complex by double-label isotope trapping Biochemistry. 28: 6870-6875. PMID 2684267 |
0.354 |
|
| 1989 |
Murphy BP, Pratt RF. A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate. The Biochemical Journal. 258: 765-8. PMID 2499308 DOI: 10.1042/Bj2580765 |
0.501 |
|
| 1988 |
Pratt RF, McConnell TS, Murphy SJ. Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A β-lactamase of Staphylococcus aureus PC1 Biochemical Journal. 254: 919-922. PMID 3264153 DOI: 10.1042/Bj2540919 |
0.471 |
|
| 1988 |
Murphy BP, Pratt RF. Evidence for an oxyanion hole in serine beta-lactamases and DD-peptidases. The Biochemical Journal. 256: 669-72. PMID 3066349 DOI: 10.1042/Bj2560669 |
0.563 |
|
| 1988 |
Pratt RF, Cahn DJ. On the mechanism of rearrangement of 6-halopenicilloates to 2,3-dihydro-1,4-thiazines Journal of the American Chemical Society. 110: 5096-5104. DOI: 10.1021/Ja00223A030 |
0.348 |
|
| 1987 |
Faraci WS, Pratt RF. Nucleophilic re-activation of the PC1 β-lactamase of Staphylococcus aureus and of the DD-peptidase of Streptomyces R61 after their inactivation by cephalosporins and cephamycins Biochemical Journal. 246: 651-658. PMID 3500712 DOI: 10.1042/Bj2460651 |
0.526 |
|
| 1987 |
Grace ME, Schenkein DP, Pratt RF. Kinetics and mechanism of inactivation of the RTEM-2 β-lactamase by phenylpropynal. Identification of the characteristic chromophore Journal of Biological Chemistry. 262: 16778-16785. PMID 3119590 |
0.37 |
|
| 1987 |
Govardhan CP, Pratt RF. Kinetics and mechanism of the serine β-lactamase catalyzed hydrolysis of depsipeptides Biochemistry. 26: 3385-3395. PMID 3115289 |
0.457 |
|
| 1987 |
Knap AK, Pratt RF. Inactivation of the thiol RTEM-1 beta-lactamase by 6-beta-bromopenicillanic acid. Identity of the primary active-site nucleophile Biochemical Journal. 247: 29-33. PMID 2825657 DOI: 10.1042/Bj2470029 |
0.554 |
|
| 1986 |
Faraci WS, Pratt RF. Mechanism of inhibition of RTEM-2 β-lactamase by cephamycins: Relative importance of the 7α-methoxy group and the 3′ leaving group Biochemistry. 25: 2934-2941. PMID 3487346 DOI: 10.1021/BI00358A030 |
0.426 |
|
| 1986 |
Pratt RF, Faraci WS. Direct observation by proton NMR of cephalosporoate intermediates in aqueous solution during the hydrazinolysis and .beta.-lactamase-catalyzed hydrolysis of cephalosporins with 3' leaving groups: kinetics and equilibria of the 3' elimination reaction Journal of the American Chemical Society. 108: 5328-5333. DOI: 10.1021/Ja00277A044 |
0.447 |
|
| 1985 |
Faraci WS, Pratt RF. Mechanism of inhibition of the PC1 β-lactamase of Staphylococcus aureus by cephalosporins: Importance of the 3′-leaving group Biochemistry. 24: 903-910. PMID 3873255 |
0.412 |
|
| 1984 |
Pratt RF, Govardhan CP. β-Lactamase-catalyzed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptors Proceedings of the National Academy of Sciences of the United States of America. 81: 1302-1306. PMID 6424114 |
0.358 |
|
| 1984 |
Faraci WS, Pratt RF. Elimination of a good leaving group from the 3'-position of a cephalosporin need not be concerted with .beta.-lactam ring opening: TEM-2 .beta.-lactamase-catalyzed hydrolysis of pyridine-2-azo-4'-(N',N'-dimethylaniline) cephalosporin (PADAC) and of cephaloridine Journal of the American Chemical Society. 106: 1489-1490. DOI: 10.1021/Ja00317A053 |
0.457 |
|
| 1983 |
Anderson EG, Pratt RF. Pre-steady state beta-lactamase kinetics. The trapping of a covalent intermediate and the interpretation of pH rate profiles. The Journal of Biological Chemistry. 258: 13120-6. PMID 6605346 |
0.407 |
|
| 1982 |
Wolozin BL, Myerowitz R, Pratt RF. Specific chemical modification of the readily nitrated tyrosine of the RTEM β-lactamase and of bacillus cereus β-lactamase I. The role of this tyrosine in β-lactamase catalysis Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 701: 153-163. PMID 6803835 DOI: 10.1016/0167-4838(82)90108-X |
0.466 |
|
| 1981 |
Anderson EG, Pratt RF. Pre-steady state beta-lactamase kinetics. Observation of a covalent intermediate during turnover of a fluorescent cephalosporin by the beta-lactamase of STaphylococcus aureus PC1. The Journal of Biological Chemistry. 256: 11401-4. PMID 6975275 |
0.427 |
|
| 1980 |
Cohen SA, Pratt RF. Inactivation of Bacillus cereus β-lactamase I by 6β-bromopencillanic acid: Mechanism Biochemistry. 19: 3996-4003. PMID 6773559 DOI: 10.1021/bi00558a017 |
0.313 |
|
| 1980 |
Pratt RF, Anderson EG, Odeh I. Certain monocyclic beta-lactams are beta-lactamase substrates: nocardicin A and desthiobenzylpenicillin. Biochemical and Biophysical Research Communications. 93: 1266-73. PMID 6772177 DOI: 10.1016/0006-291X(80)90626-9 |
0.485 |
|
| 1980 |
Schenkein DP, Pratt RF. Phenylpropynal, a specific, irreversible, non-β-lactam inhibitor of β-lactamases Journal of Biological Chemistry. 255: 45-48. PMID 6765945 |
0.322 |
|
| 1980 |
Loosemore MJ, Cohen SA, Pratt RF. Inactivation of Bacillus cereus β-lactamase I by 6β-bromopenicillanic acid: Kinetics Biochemistry. 19: 3990-3995. PMID 6250581 DOI: 10.1021/bi00558a016 |
0.352 |
|
| 1980 |
Grace ME, Loosemore MJ, Semmel ML, Pratt RF. Kinetics and mechanism of the bamberger cleavage of imidazole and of histidine derivatives by diethyl pyrocarbonate in aqueous solution Journal of the American Chemical Society. 102: 6784-6789. DOI: 10.1021/Ja00542A020 |
0.307 |
|
| 1978 |
Pratt RF, Loosemore MJ. 6-β-Bromopenicillanic acid, a potent β-lactamase inhibitor Proceedings of the National Academy of Sciences of the United States of America. 75: 4145-4149. PMID 212736 DOI: 10.1073/Pnas.75.9.4145 |
0.414 |
|
| 1978 |
Loosemore MJ, Pratt RF. Epimerization of 6.alpha.-bromopenicillanic acid and preparation of 6.beta.-bromopenicillanic acid Journal of Organic Chemistry. 43: 3611-3613. DOI: 10.1021/Jo00412A047 |
0.361 |
|
| 1977 |
Rahil J, Pratt RF. THE ALKALINE HYDROLYSIS OF β-DICARBONYL COMPOUNDS Cheminform. 8. DOI: 10.1002/Chin.197727104 |
0.331 |
|
| 1976 |
Loosemore MJ, Pratt RF. The irreversible cleavage of histidine residues by diethylpyrocarbonate (ethoxyformic anhydride) Febs Letters. 72: 155-158. PMID 1001460 DOI: 10.1016/0014-5793(76)80834-4 |
0.391 |
|
| 1976 |
Lowe G, Pratt RF. Proton exchange of the Pro S hydrogen at C 1 in dihydroxyacetone phosphate, D fructose 1,6 bisphosphate and D fructose 1 phosphate catalysed by rabbit muscle aldolase European Journal of Biochemistry. 66: 95-104. PMID 954748 DOI: 10.1111/J.1432-1033.1976.Tb10429.X |
0.318 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 2002 |
Bell JH, Pratt RF. Formation and structure of 1:1 complexes between aryl hydroxamic acids and vanadate at neutral pH. Inorganic Chemistry. 41: 2747-53. PMID 12005499 DOI: 10.1021/Ic011193+ |
0.299 |
|
| 1971 |
Pratt RF, Bruice TC. Reactions of S-acylisothioureas. I. S- to N-acyl migrations in S-benzoylisothiobiotin and analogs Biochemistry. 10: 3178-3185. PMID 5119245 DOI: 10.1021/BI00793A003 |
0.295 |
|
| 1979 |
Loosemore MJ, Pratt RF. EPIMERIZATION OF 6α-BROMOPENICILLANIC ACID AND PREPARATION OF 6β-BROMOPENICILLANIC ACID Cheminform. 10. DOI: 10.1002/Chin.197907340 |
0.293 |
|
| 1985 |
Pratt RF, Faraci WS, Govardhan CP. A direct spectrophotometric assay for d-alanine carboxypeptidases and for the esterase activity of β-lactamases Analytical Biochemistry. 144: 204-206. PMID 3872609 DOI: 10.1016/0003-2697(85)90106-X |
0.289 |
|
| 1986 |
Pratt RF, Faraci WS. Direct observation by 1H NMR of cephalosporoate intermediates in aqueous solution during the hydrazinolysis and β-lactamase-catalyzed hydrolysis of cephalosporins with 3′ leaving groups: Kinetics and equilibria of the 3′ elimination reaction Journal of the American Chemical Society. 108: 5328-5333. |
0.289 |
|
| 1983 |
Pratt RF, Surh YS, Shaskus JJ. Products and mechanism of the oxyanion- and β-lactamase-catalyzed hydrolyses of (phenoxymethyl)anhydropenicillin Journal of the American Chemical Society. 105: 1006-1014. |
0.27 |
|
| 1991 |
Popieniek PH, Pratt RF. Kinetics and Mechanism of Binding of Specific Peptides to Vancomycin and Other Glycopeptide Antibiotics Journal of the American Chemical Society. 113: 2264-2270. |
0.261 |
|
| 1970 |
Pratt RF, Bruice TC. The carbanion mechanism (E1cB) of ester hydrolysis. III. Some structure-reactivity studies and the ketene intermediate Journal of the American Chemical Society. 92: 5956-5964. |
0.249 |
|
| 1984 |
Faraci WS, Pratt RF. Elimination of a good leaving group from the 3′-position of a cephalosporin need not be concerted with β-lactam ring opening: TEM-2 β-lactamase-catalyzed hydrolysis of pyridine-2-azo-4′-(N′,N′-dimethylaniline) cephalosporin (PADAC) and of cephaloridine Journal of the American Chemical Society. 106: 1489-1490. |
0.248 |
|
| 1995 |
Deraniyagala SA, Adediran SA, Pratt RF. β-Secondary and solvent deuterium kinetic isotope effects and the mechanisms of base- and acid-catalyzed hydrolysis of penicillanic acid Journal of Organic Chemistry. 60: 1619-1625. |
0.229 |
|
| 1971 |
Hegarty AF, Pratt RF, Giudici T, Bruice TC. Acyl transfer reactions from and to the ureido functional group. IV. Neighboring carboxyl group general acid catalysis in the hydrolysis of an O-acylisourea (2-amino-8-carboxy-4-oxo-3,1,4-benzoxazine) Journal of the American Chemical Society. 93: 1428-1434. |
0.229 |
|
| 1972 |
Pratt RF, Bruice TC. Reactions of S-acylisothioureas. II. Effects of structure and stereochemistry on the rates of hydrolysis, thiol elimination, and S to N acyl migration in acylic systems Journal of the American Chemical Society. 94: 2823-2837. |
0.221 |
|
| 1977 |
Rahil J, Pratt RF. On the alkaline hydrolysis of β-dicarbonyl compounds Journal of the American Chemical Society. 99: 2661-2665. PMID 14983 DOI: 10.1021/JA00450A043 |
0.218 |
|
| 1980 |
McNeil KJ, DiCaprio JA, Walsh DA, Pratt RF. Kinetics and mechanism of hydrolysis of a silicate triester, tris(2-methoxyethoxy)phenylsilane Journal of the American Chemical Society. 102: 1859-1865. |
0.217 |
|
| 1987 |
Popieniek PH, Pratt RF. A fluorescent ligand for binding studies with glycopeptide antibiotics of the vancomycin class Analytical Biochemistry. 165: 108-113. PMID 3688425 DOI: 10.1016/0003-2697(87)90207-7 |
0.216 |
|
| 1971 |
Hegarty AF, Pratt RF, Giudici T, Bruice TC. Acyl transfer reactions from and to the Ureido functional group. IV. Neighboring carboxyl group general acid catalysis in the hydrolysis of an O-acylisourea (2-amino-8-carboxy-4-oxo-3,1,4-benzoxazine Journal of the American Chemical Society. 93: 1428-1434. DOI: 10.1021/Ja00735A018 |
0.213 |
|
| 1970 |
Pratt RF, Bruice TC. The carbanion mechanism (ElcB) of ester hydrolysis. III. Some structure-reactivity studies and the ketene intermediate Journal of the American Chemical Society. 92: 5956-5964. DOI: 10.1021/Ja00723A024 |
0.197 |
|
| 1995 |
Vijayakumar S, Ravishanker G, Pratt RF, Beveridge DL. Molecular dynamics simulation of a class A β-lactamase: Structural and mechanistic implications Journal of the American Chemical Society. 117: 1722-1730. |
0.19 |
|
| 1972 |
Pratt RF, Bruice TC. Reactions of S-acylisothioureas. II. Effects of structure and stereochemistry on the rates of hydrolysis, thiol elimination, and S to N acyl migration in acylic systems Journal of the American Chemical Society. 94: 2823-2837. DOI: 10.1021/Ja00763A048 |
0.187 |
|
| 1977 |
Pratt RF. Rabbit muscle aldolase catalyzed proton exchange of hydroxyacetone phosphate with solvent Biochemistry. 16: 3988-3994. PMID 911752 |
0.174 |
|
| 2013 |
Pratt RF, Frère JM. Streptomyces R61 d-Ala-d-Ala Carboxypeptidase Handbook of Proteolytic Enzymes. 3: 3458-3463. DOI: 10.1016/B978-0-12-382219-2.00766-3 |
0.172 |
|
| 1978 |
Loosemore MJ, Pratt RF. On the epimerization of 6α-bromopenicillanic acid and the preparation of 6β-bromopenicillanic acid Journal of Organic Chemistry. 43: 3611-3613. |
0.155 |
|
| 1986 |
Faraci WS, Pratt RF. Interactions of cephalosporins with the Streptomyces R61 DD-transpeptidase/carboxypeptidase. Influence of the 3'-substituent Biochemical Journal. 238: 309-312. PMID 3800940 |
0.155 |
|
| 1988 |
Popieniek PH, Pratt RF. Rates of specific peptide binding to the glycopeptide antibiotics vancomycin, ristocetin, and avoparcin Journal of the American Chemical Society. 110: 1285-1286. |
0.153 |
|
| 2006 |
Sauvage E, Kerff F, Pratt R, Charlier P. The penicillin-binding proteins of class C1 Acta Crystallographica Section a Foundations of Crystallography. 62: s162-s162. DOI: 10.1107/S0108767306096760 |
0.151 |
|
| 1971 |
Bruice TC, Pratt RF. An intramolecular acyl transfer reaction limited by substrate isomerization Journal of the Chemical Society D: Chemical Communications. 1259-1261. DOI: 10.1039/C29710001259 |
0.151 |
|
| 1969 |
Pratt RF, Lawlor JM. Catalysed hydrolysis of an acyl-activated anilide in buffered solutions Journal of the Chemical Society B: Physical Organic. 230-237. |
0.143 |
|
| 1981 |
Pratt RF, Kraus KK. Ring opening and closing reactions of imidazoles and other 1,3-diazaheterocycles with vinyl chloroformate and phenyl chloroformate Tetrahedron Letters. 22: 2431-2434. DOI: 10.1016/S0040-4039(01)92925-9 |
0.132 |
|
| 1968 |
Pratt RF, Lawlor JM. On the search for bifunctional catalysis of esterolytic reactions Chemical Communications (London). 522-524. DOI: 10.1039/C19680000522 |
0.114 |
|
| 1972 |
Pratt RF, Bruice TC. The lack of an α effect for proton abstraction from carbon acids Journal of Organic Chemistry. 37: 3563-3564. |
0.092 |
|
| 1988 |
PRATT RF, CAHN DJ. ChemInform Abstract: Mechanism of Rearrangement of 6-Halopenicilloates to 2,3-Dihydro-1,4-thiazines. Cheminform. 19. DOI: 10.1002/CHIN.198846097 |
0.083 |
|
| 1972 |
Whitehead VM, Pratt R, Viallet A, Cooper BA. Intestinal conversion of folinic acid to 5-methyltetrahydrofolate in man. British Journal of Haematology. 22: 63-72. PMID 4621839 DOI: 10.1111/j.1365-2141.1972.tb08787.x |
0.082 |
|
| 1972 |
Pratt RF, Bruice TC. Lack of an .alpha. effect for proton abstraction from carbon acids Journal of Organic Chemistry. 37: 3563-3564. DOI: 10.1021/Jo00795A049 |
0.079 |
|
| 1971 |
Pratt RF, Cooper BA. Folates in plasma and bile of man after feeding folic acid--3H and 5-formyltetrahydrofolate (folinic acid) Journal of Clinical Investigation. 50: 455-462. PMID 4992993 |
0.061 |
|
| 1972 |
Whitehead VM, Cooper BA, Pratt RF. Absorption of folic acid. Lancet (London, England). 1: 326. PMID 4109969 DOI: 10.1016/S0140-6736(72)90340-6 |
0.057 |
|
| 1977 |
Kasperek GJ, Pratt RF. The fumarase reaction: A nuclear magnetic resonance experiment for biological chemistry students Journal of Chemical Education. 54: 515-516. PMID 893568 |
0.053 |
|
| 1978 |
Klouda PT, Harris R, Price DA, Pucholt V, Fitzsimmons JS, Gelsthorpe K, Pratt RF, Doughty RW. HLA AND CONGENITAL ADRENAL HYPERPLASIA The Lancet. 312: 1046-1047. PMID 82057 DOI: 10.1016/S0140-6736(78)92364-4 |
0.051 |
|
| 1974 |
Norris JW, Pratt RF. Folic Acid Deficiency and Epilepsy Drugs. 8: 366-385. PMID 4455477 DOI: 10.2165/00003495-197408050-00005 |
0.041 |
|
| 1971 |
Norris JW, Pratt RF. A controlled study of folic acid in epilepsy Neurology. 21: 659-664. PMID 4934771 |
0.034 |
|
| 1962 |
ASHMORE PG, PRATT RF, MACGILLIVRAY RA, FORSENG EG. An experimental study of cardiopulmonary bypass in the small animal Canadian Journal of Surgery. Journal Canadien De Chirurgie. 5: 218-222. PMID 13862861 |
0.021 |
|
| 1977 |
Pietarinen GJ, Leichter J, Pratt RF. Dietary folate intake and concentration of folate in serum and erythrocytes in women using oral contraceptives. The American Journal of Clinical Nutrition. 30: 375-80. PMID 842488 |
0.01 |
|
| Hide low-probability matches. |