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1 proteins, and SpoVD, a nonessential class B penicillin binding protein.
2 gene that encodes the methicillin-resistant penicillin binding protein.
3 is a bacterial low molecular weight class C penicillin-binding protein.
4 tro and in vivo with the major bi-functional penicillin-binding protein.
5 lysine to 8.0-8.5 from that of the parental penicillin-binding protein.
6 values was found for a beta-lactam-resistant penicillin-binding protein.
7 ally encodes a high-molecular-weight class A penicillin-binding protein.
8 d scoring against the crystal structure of a penicillin-binding protein.
9 d-Ala analogues and to prevent the action of penicillin binding proteins.
10 amidases, or any of the low-molecular-weight penicillin binding proteins.
11 ocks peptidoglycan polymerization by class A penicillin-binding proteins.
12 eB promotes the transglycosylase activity of penicillin-binding proteins.
13 milarity to a noncatalytic domain of class B penicillin-binding proteins.
14 cellular multiprotein complexes that include penicillin-binding proteins.
15 to any other beta-lactamases or the related penicillin-binding proteins.
16 g all active-site serine beta-lactamases and penicillin-binding proteins.
17 ding determinations for penicillin-sensitive penicillin-binding proteins.
18 ated by structural changes in transpeptidase penicillin-binding proteins.
19 th sequence homology to low-molecular-weight penicillin-binding proteins.
20 biosynthesis and one encodes a homologue of penicillin-binding proteins.
22 ptibility to penicillin: ponA, which encodes penicillin-binding protein 1 (PBP 1), and the pilMNOPQ o
23 e shown that Bacillus subtilis cells lacking penicillin-binding protein 1 (PBP1), encoded by ponA, ha
25 work has shown that the ponA gene, encoding penicillin-binding protein 1 (PBP1), is in a two-gene op
26 n through recombination events involving the penicillin binding protein 1a (pbp1a) gene, have cpsB se
29 ffects of inactivation of the genes encoding penicillin-binding protein 1a (PBP1a), PBP1b, and PBP2a
30 ng the Rcs stress response and those lacking penicillin binding protein 1B (PBP1B) or LpoB could not
32 examined the inhibition of Escherichia coli penicillin-binding protein 1b (PBP1b) by moenomycin as w
35 inhibits the cell elongation transpeptidase penicillin binding protein 2 in Escherichia coli, exhibi
36 ) on Mueller-Hinton agar, an immunoassay for penicillin binding protein 2' (Denka Seiken Co., Tokyo,
41 antibiotic with high selective affinity for penicillin-binding protein 2 (PBP2) of Staphylococcus au
42 ting cells with amdinocillin, which inhibits penicillin-binding protein 2 (PBP2), allowed PG glycan s
43 ired for cell division, or in the absence of penicillin-binding protein 2 (PBP2), which is required f
45 y be the product of the abnormal activity of penicillin-binding protein 2 which has grossly reduced a
49 d, Basingstoke, United Kingdom) that detects penicillin binding protein 2a (PBP2a) with MicroScan con
50 S. aureus is the production of a distinctive penicillin binding protein 2a (PBP2a), which exhibits lo
52 us infection in which a false-positive rapid penicillin binding protein 2a latex test in conjunction
54 onferring beta-lactam antibiotic resistance, penicillin-binding protein 2A (encoded by the mecA gene)
55 enzymes, and the other is the expression of penicillin-binding protein 2a (PBP 2a), which is not sus
58 glycan, down-regulation of the production of penicillin-binding protein 2A (PBP2A) and PBP4, and hype
59 hylococcus aureus (MRSA), is able to inhibit penicillin-binding protein 2a (PBP2a) by triggering an a
64 (eg, oxacillin) depends on the production of penicillin-binding protein 2a (PBP2a), encoded by mecA M
65 ith monoclonal antibody prepared against the penicillin-binding protein 2A (PBP2A), i.e., the gene pr
68 ous aqueous solution showed that solubilized penicillin-binding protein 2a (sPBP2a) of methicillin-re
72 d to monoclonal antibodies (MAb) specific to penicillin-binding-protein 2a of methicillin resistant (
73 The assay amplifies a lytA gene target and a penicillin binding protein 2b (pbp2b) gene target in pen
75 ntigen (SAG1350), lipoprotein (SAG0971), and penicillin-binding protein 2b (SAG0765) each bound to ME
76 antigen (SAG1350), a lipoprotein (SAG0971), penicillin-binding protein 2b (SAG0765), glyceraldehyde-
77 ctrophoresis, multilocus sequence typing and penicillin-binding protein 2b amplicon-restriction profi
78 ibiotics, we purified a penicillin-resistant penicillin-binding protein 2x (R-PBP2x) and a penicillin
80 that inactivation of the ftsI gene product, penicillin binding protein 3, by either beta-lactam anti
82 rict linkage disequilibrium in the S. aureus penicillin-binding protein 3 (pbp3) gene were also found
90 oglycan composition is related to defects in penicillin-binding protein 4 (PBP4); no PBP4 was detecta
91 tivity of a soluble form of Escherichia coli penicillin-binding protein 5 (PBP 5) against the classic
100 n enterococcal strain devoid of low-affinity penicillin-binding protein-5 (significantly increasing i
104 MreC controls the spatial orientation of the penicillin binding proteins and a lytic transglycosylase
106 (ECD) consists of four repeats homologous to penicillin-binding protein and serine/threonine kinase a
107 Both the PonA2 and PonA3 proteins contain a penicillin-binding protein and serine/threonine protein
108 ng of 1.2 million compounds for binding to a penicillin-binding protein and the subsequent demonstrat
110 treptococcus pneumoniae contain low affinity penicillin-binding proteins and often also produce abnor
111 ral non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases.
112 result from the presence of a reduced set of penicillin-binding proteins and the absence of a wblC ge
114 ansmembrane proteins that have extracellular penicillin-binding-protein and serine/threonine kinase-a
115 other than inhibition of protein synthesis, penicillin-binding proteins, and DNA topoisomerases; amo
116 wall assembly mechanism assume that class A penicillin-binding proteins (aPBPs), the targets of peni
118 DCW gene clusters, including the presence of penicillin-binding proteins at the left ends and ftsA an
119 MRSA strains have acquired a non-native penicillin-binding protein called PBP2a that cross-links
120 ces R61 dd-peptidase, a functional model for penicillin-binding proteins, catalyzes the hydrolysis an
121 erived genomes possess mutations targeting a penicillin-binding protein coding gene (mrcA) that had n
123 characterize the hydrolysis of the standard penicillin-binding protein/DD-carboxypeptidase substrate
124 ked by the pbp2x and pbp1a genes, coding for penicillin-binding proteins, enzymes involved in cell wa
125 as identified previously for genes encoding penicillin binding proteins, evolved by recombination wi
126 s for the direct detection of IgE and of the penicillin-binding protein from Staphylococcus aureus (P
127 ferase domain of class A high-molecular-mass penicillin-binding proteins from different species.
129 somal macrorestriction profile and identical penicillin-binding-protein gene restriction profiles cha
131 on fragmentation length polymorphisms of the penicillin-binding protein genes pbp1a, pbp2x, and pbp2b
133 , sometimes including the capsular locus and penicillin-binding protein genes, predated both vaccine
135 glycan synthesis and degradation mediated by penicillin binding proteins in the forespore and a cell
136 acylation and provide further evidence that penicillin-binding proteins in apo form can occupy diffe
137 of carbenicillin (Cb) to assess the role of penicillin-binding proteins in growth and cell division.
138 r, these results identify a novel role for a penicillin-binding-protein in compartmentalizing a bacte
139 red substrate preference of transpeptidases (penicillin-binding proteins) in the pneumococcal variant
141 s the archetypal class C, low molecular mass penicillin binding protein (LMM-PBP) and possesses both
143 The biological roles of low molecular weight penicillin-binding proteins (LMW PBP) have been difficul
144 chia coli cells lacking low-molecular-weight penicillin-binding proteins (LMW PBPs) exhibit morpholog
145 ane, these new cell wall components regulate penicillin-binding proteins located at the inner membran
150 ence exceeds that observed for blocks in the penicillin-binding proteins of S. pneumoniae or in many
151 otluri et al. show that low molecular weight penicillin binding proteins, particularly PBP5, have a r
152 that controls activity of the bi-functional penicillin binding protein PBP A1, we discovered that Gp
155 ates also potently inhibit the non-essential penicillin-binding protein PBP 5 by the same mechanism o
157 nts for acylation and deacylation of soluble penicillin binding protein (PBP) constructs by compounds
158 ectrophoresis (PFGE) of chromosomal digests, penicillin binding protein (PBP) gene fingerprinting, an
159 onstructed a set of mutants from which eight penicillin binding protein (PBP) genes were deleted in 1
160 DNA fragments that do not contain any known penicillin binding protein (PBP) genes, indicating that
161 The approach uses a recombinant bacterial penicillin binding protein (PBP) tagged by an N-terminal
163 rmined that expression of the well-conserved penicillin-binding protein (PBP) 1A, prevented LOS-defic
164 erved heterogeneous localization dynamics of penicillin-binding protein (PBP) 1A, the synthase predom
165 otein LpoB is required for the activation of penicillin-binding protein (PBP) 1B, which is a major, b
166 Imipenem, which has a greater affinity for penicillin-binding protein (PBP) 2, induced less IL-6 re
173 n fragment length polymorphism (RFLP) of the penicillin-binding protein (PBP) genes 1A, 2X, and 2B, a
174 of Streptococcus pneumoniae contain altered penicillin-binding protein (PBP) genes and occasionally
175 osporin drug ceftazidime caused by loss of a penicillin-binding protein (PBP) in a Gram-negative baci
177 that inactivation of the major bi-functional penicillin-binding protein (PBP) PBP1 of B. subtilis res
179 Mycobacterium tuberculosis is a class B-like penicillin-binding protein (PBP) that is not essential f
180 ed motifs of a class B high-molecular-weight penicillin-binding protein (PBP), including the transpep
181 We report the first crystal structures of a penicillin-binding protein (PBP), PBP3, from Pseudomonas
182 of this resistance mechanism: the "acquired" penicillin-binding protein (PBP)-2A, which has unusual l
183 the United States, restriction profiles of 3 penicillin-binding protein (PBP)-gene amplicons and the
187 eptidase (TP) activities of Escherichia coli penicillin binding proteins PBP1A and PBP1B and show tha
188 Cell wall morphogenetic protein RodA and penicillin-binding protein PBP1a also change their spati
190 is model, we found that a surface-associated penicillin-binding protein (PBP1a), encoded by ponA, pla
191 cholerae high-molecular-weight bifunctional penicillin binding proteins, PBP1a and PBP1b, in the fit
195 is of tryptic peptides derived from purified penicillin-binding protein PBP2a of Bacillus subtilis id
196 istant S. aureus strain expressing the extra penicillin-binding protein PBP2A, a protein of extraspec
197 of the crystal structure of the low-affinity penicillin-binding protein PBP2a, which mediates beta-la
198 mediated by mecA and blaZ, genes encoding a penicillin-binding protein (PBP2a) with low beta-lactam
199 e acquisition of a nonnative gene encoding a penicillin-binding protein (PBP2a), with significantly l
200 ls and is catalyzed by the essential class B penicillin-binding protein PBP2b transpeptidase (TP).
201 he relative localization patterns of class B penicillin-binding proteins Pbp2x and Pbp2b were used as
202 al sideromimic conjugated compounds bound to penicillin binding proteins PBP3 and PBP1a from Pseudomo
207 g a forward genetics approach, we identify a penicillin-binding-protein, PbpC, which is required for
208 precise temporal and spatial organization of penicillin binding proteins (PBPs) and associated protei
211 depends not only on the reduced affinity of penicillin binding proteins (PBPs) but also on the funct
212 isolated from strains lacking three or four penicillin binding proteins (PBPs) but not from a mutant
214 at Escherichia coli mutants lacking multiple penicillin binding proteins (PBPs) display extensive mor
216 iotics, the transpeptidase activity of their penicillin binding proteins (PBPs) is lost as a result o
217 e been ascribed to the high-molecular-weight penicillin binding proteins (PBPs) of Escherichia coli,
220 al targets are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the c
224 ation rates for acyl-enzyme intermediates in penicillin-binding proteins (PBPs) and beta-lactamases h
225 d low throughput assays of the activities of penicillin-binding proteins (PBPs) and beta-lactamases,
226 nal d,d-transpeptidases belonging to class B penicillin-binding proteins (PBPs) and monofunctional gl
241 subtilis, where it plays a role in shuttling penicillin-binding proteins (PBPs) between septal and si
246 the first crystal structures of A. baumannii penicillin-binding proteins (PBPs) covalently inactivate
247 fluorescent protein (GFP) fusions to all 11 penicillin-binding proteins (PBPs) expressed during vege
248 iotics is the D,D-transpeptidase activity of penicillin-binding proteins (PBPs) for synthesis of 4-->
249 -tagged beta-lactam antibiotics to visualize penicillin-binding proteins (PBPs) in sporulating cultur
253 mutants in Escherichia coli lacking multiple penicillin-binding proteins (PBPs) produce misshapen cel
254 erence affects the cross-linking activity of penicillin-binding proteins (PBPs) that assemble peptido
255 ave long been known to target enzymes called penicillin-binding proteins (PBPs) that build the bacter
256 crescentus, MreC physically associates with penicillin-binding proteins (PBPs) which catalyse the in
261 at MreC Interacts with high-molecular-weight penicillin-binding proteins (PBPs), rather than with low
262 ne of very few compound classes that inhibit penicillin-binding proteins (PBPs), SBLs and, as recentl
263 The Bacillus subtilis genome encodes 16 penicillin-binding proteins (PBPs), some of which are in
267 The bifunctional high molecular weight (HMW) penicillin-binding proteins (PBPs), which contain both g
268 pressing variants of its target enzymes, the penicillin-binding proteins (PBPs), with many amino acid
279 is of the bacterial cell wall (also known as penicillin-binding proteins, PBPs) have evolved to bind
280 ors), aceA (isocitrate lyase), ponA (class I penicillin-binding protein), pks2 (polyketide synthase),
281 an additional gene encoding a third class A penicillin-binding protein, PonA3, which is a paralog of
283 The Bacillus subtilis spoVD gene encodes a penicillin-binding protein required for spore morphogene
284 to different target enzymes (DNA gyrase and penicillin-binding proteins, respectively) and in 41 sin
285 ent that preferentially binds to the altered penicillin binding protein responsible for diminished pe
286 n that provides high-affinity binding to the penicillin-binding proteins responsible for bacterial re
287 elevant class A, C and D beta-lactamases and penicillin-binding proteins, resulting in intrinsic anti
289 demonstrates that the high-molecular-weight penicillin-binding protein SpoVD, which contains two exp
290 can cell wall is synthesized by bifunctional penicillin-binding proteins such as PBP1b that have both
291 BP2 co-immunoprecipitated with several other penicillin-binding proteins, suggesting that these prote
292 cillin-binding protein A (PBPA) is a class B penicillin-binding protein that is important for cell di
293 that link the cytoskeletal elements with the penicillin-binding proteins that carry out peptidoglycan
294 These enzymes are members of the family of penicillin-binding proteins, the targets of beta-lactam
295 is the first purified gram-positive class A penicillin-binding protein to show good transglycosylase
297 an approximately 59-kDa membrane-associated penicillin-binding protein which is highly toxic when ov
298 nce in staphylococci is mediated by PBP2a, a penicillin binding protein with low affinity for beta-la
300 ional members of the sigma(X) regulon, pbpX (penicillin-binding protein), ywnJ, the dlt operon (D-ala
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