PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11796337-1 2002 RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci. Cephalosporins 32-45 AT695_RS11765 Staphylococcus aureus 60-86 11796337-1 2002 RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci. Cephalosporins 32-45 AT695_RS11765 Staphylococcus aureus 88-91 11796337-1 2002 RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci. Cephalosporins 32-45 AT695_RS11765 Staphylococcus aureus 93-96 11796337-1 2002 RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci. Cephalosporins 32-45 AT695_RS11765 Staphylococcus aureus 93-96 19180259-1 2008 Ceftobiprole is a novel parenteral cephalosporin with high affinity for most penicillin-binding proteins, including the mecA product penicillin-binding protein (PBP) 2a, rendering it active against methicillin-resistant staphylococci. Cephalosporins 35-48 AT695_RS11765 Staphylococcus aureus 77-103 19180259-1 2008 Ceftobiprole is a novel parenteral cephalosporin with high affinity for most penicillin-binding proteins, including the mecA product penicillin-binding protein (PBP) 2a, rendering it active against methicillin-resistant staphylococci. Cephalosporins 35-48 AT695_RS11765 Staphylococcus aureus 161-164 16459335-8 2006 These cephalosporins exhibit substantially smaller dissociation constants for the preacylation complex compared with the case of typical cephalosporins, but their pseudo-second-order rate constants for encounter with PBP 2a (k(2)/K(s)) are not very large (< or =200 m(-1) s(-1)). Cephalosporins 6-20 AT695_RS11765 Staphylococcus aureus 217-220 16459335-9 2006 It is documented herein that these cephalosporins facilitate a conformational change in PBP 2a, a process that is enhanced in the presence of a synthetic surrogate for cell wall, resulting in increases in the k(2)/K(s) parameter and in more facile enzyme inhibition. Cephalosporins 35-49 AT695_RS11765 Staphylococcus aureus 88-91 16459335-10 2006 These findings argue that the novel cephalosporins are able to co-opt interactions between PBP 2a and the cell wall in gaining access to the active site in the inhibition process, a set of events that leads to effective inhibition of PBP 2a and the attendant killing of the MRSA strains. Cephalosporins 36-50 AT695_RS11765 Staphylococcus aureus 91-94 16459335-10 2006 These findings argue that the novel cephalosporins are able to co-opt interactions between PBP 2a and the cell wall in gaining access to the active site in the inhibition process, a set of events that leads to effective inhibition of PBP 2a and the attendant killing of the MRSA strains. Cephalosporins 36-50 AT695_RS11765 Staphylococcus aureus 234-237