On the public citation graph
Substrate Specificity of Low-Molecular Mass Bacterial dd -Peptidases
0 signed · 104 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/047120918x.emb1092openalex-snapshot
Penicillin‐Binding Proteins
inferredcites →https://doi.org/10.1006/bbrc.1999.1509openalex-snapshot
Identification of Two Penicillin-Binding Multienzyme Complexes in Haemophilus influenzae
inferredcites →https://doi.org/10.1007/978-1-60327-853-9_23openalex-snapshot
What Antimicrobial Resistance Has Taught Us About Horizontal Gene Transfer
inferredcites →https://doi.org/10.1007/s00018-008-7591-7openalex-snapshot
Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)
inferredcites →https://doi.org/10.1007/s000180050160openalex-snapshot
Resistant penicillin-binding proteins
inferredcites →https://doi.org/10.1016/0022-2836(71)90393-7openalex-snapshot
Conformation of penicillin as a transition-state analog of the substrate of peptidoglycan transpeptidase
inferredcites →https://doi.org/10.1016/j.bbamem.2007.06.007openalex-snapshot
Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
inferredcites →https://doi.org/10.1016/j.bbamem.2009.04.010openalex-snapshot
Membrane interactions of a self-assembling model peptide that mimics the self-association, structure and toxicity of Aβ(1–40)
inferredcites →https://doi.org/10.1016/j.cell.2010.11.038openalex-snapshot
Regulation of Peptidoglycan Synthesis by Outer-Membrane Proteins
inferredcites →https://doi.org/10.1016/j.jmb.2007.05.071openalex-snapshot
Crystal Structure of the Bacillus subtilis Penicillin-binding Protein 4a, and its Complex with a Peptidoglycan Mimetic Peptide
inferredcites →https://doi.org/10.1016/j.jmb.2007.10.066openalex-snapshot
Trapping of an Acyl–Enzyme Intermediate in a Penicillin-binding Protein (PBP)-catalyzed Reaction
inferredcites →https://doi.org/10.1016/j.jmb.2008.06.012openalex-snapshot
Crystal Structures of Complexes of Bacterial dd-Peptidases with Peptidoglycan-Mimetic Ligands: The Substrate Specificity Puzzle
inferredcites →https://doi.org/10.1016/j.jmgm.2010.11.009openalex-snapshot
Differences in active-site microarchitecture explain the dissimilar behaviors of PBP5 and 6 in Escherichia coli
inferredcites →https://doi.org/10.1016/j.mib.2003.10.002openalex-snapshot
Role of penicillin-binding proteins in bacterial cell morphogenesis
inferredcites →https://doi.org/10.1016/j.sbi.2010.09.014openalex-snapshot
Bridging cell wall biosynthesis and bacterial morphogenesis
inferredcites →https://doi.org/10.1016/j.tim.2008.04.006openalex-snapshot
Physiological functions of D-alanine carboxypeptidases in Escherichia coli
inferredcites →https://doi.org/10.1016/s0021-9258(18)47739-3openalex-snapshot
Structure of the peptide network of pneumococcal peptidoglycan.
inferredcites →https://doi.org/10.1016/s0021-9258(19)70271-3openalex-snapshot
Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes.
inferredcites →https://doi.org/10.1016/s0022-2836(02)00742-8openalex-snapshot
Structures of Two Kinetic Intermediates Reveal Species Specificity of Penicillin-binding Proteins
inferredcites →https://doi.org/10.1016/s0076-6879(96)66017-0openalex-snapshot
[15] Effective protein sequence comparison
inferredcites →https://doi.org/10.1021/bi001295wopenalex-snapshot
Dipeptide Binding to the Extended Active Site of theStreptomycesR61 d -Alanyl- d -alanine-peptidase: The Path to a Specific Substrate†
inferredcites →https://doi.org/10.1021/bi00709a010openalex-snapshot
Effects of donor and acceptor peptides on concomitant hydrolysis and transfer reactions catalyzed by the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R39
inferredcites →https://doi.org/10.1021/bi00731a001openalex-snapshot
Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular DD-carboxypeptidase-transpeptidase for peptide acceptors
inferredcites →https://doi.org/10.1021/bi00757a027openalex-snapshot
Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11
inferredcites →https://doi.org/10.1021/bi00800a001openalex-snapshot
Structure of the peptidoglycan from vegetative cell walls of Bacillus subtilis
inferredcites →https://doi.org/10.1021/bi0350607openalex-snapshot
Neisseria gonorrhoeae Penicillin-Binding Protein 3 Exhibits Exceptionally High Carboxypeptidase and β-Lactam Binding Activities,
inferredcites →https://doi.org/10.1021/bi0473004openalex-snapshot
Crystal Structure ofEscherichia coliPenicillin-Binding Protein 5 Bound to a Tripeptide Boronic Acid Inhibitor: A Role for Ser-110 in Deacylation
inferredcites →https://doi.org/10.1021/bi0505417openalex-snapshot
Transpeptidation Reactions of a Specific Substrate Catalyzed by the Streptomyces R61 dd -Peptidase: The Structural Basis of Acyl Acceptor Specificity
inferredcites →https://doi.org/10.1021/bi050542zopenalex-snapshot
Transpeptidation Reactions of a Specific Substrate Catalyzed by the Streptomyces R61 dd -Peptidase: Characterization of a Chromogenic Substrate and Acyl Acceptor Design
inferredcites →https://doi.org/10.1021/bi051533topenalex-snapshot
Crystal Structure of Penicillin Binding Protein 4 (dacB) from Escherichia coli, both in the Native Form and Covalently Linked to Various Antibiotics
inferredcites →https://doi.org/10.1021/bi061804fopenalex-snapshot
Reactivity of Penicillin-Binding Proteins with Peptidoglycan-Mimetic β-Lactams: What's Wrong with These Enzymes?
inferredcites →https://doi.org/10.1021/bi100757copenalex-snapshot
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
inferredcites →https://doi.org/10.1021/bi101760popenalex-snapshot
Kinetics of Reactions of the Actinomadura R39 dd -Peptidase with Specific Substrates
inferredcites →https://doi.org/10.1021/bi9003099openalex-snapshot
Neisseria gonorrhoeae Penicillin-Binding Protein 3 Demonstrates a Pronounced Preference for Nε-Acylated Substrates
inferredcites →https://doi.org/10.1021/cb7001347openalex-snapshot
Reactions of Peptidoglycan-Mimetic β-Lactams with Penicillin-Binding Proteins in Vivo and in Membranes
inferredcites →https://doi.org/10.1021/ja0434376openalex-snapshot
Activation for Catalysis of Penicillin-Binding Protein 2a from Methicillin-Resistant Staphylococcus aureus by Bacterial Cell Wall
inferredcites →https://doi.org/10.1021/ja2040656openalex-snapshot
Transpeptidase-Mediated Incorporation of d -Amino Acids into Bacterial Peptidoglycan
inferredcites →https://doi.org/10.1021/ja903773fopenalex-snapshot
Crystal Structures of Penicillin-Binding Protein 6 from Escherichia coli
inferredcites →https://doi.org/10.1021/jo035397eopenalex-snapshot
Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 of Gram-Negative Bacteria
inferredcites →https://doi.org/10.1021/jo048885aopenalex-snapshot
Synthesis and Evaluation of New Substrate Analogues of Streptomyces R61 dd -Peptidase: Dissection of a Specific Ligand
inferredcites →https://doi.org/10.1038/nsb858openalex-snapshot
Structural basis for the β lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus
inferredcites →https://doi.org/10.1042/0264-6021:3380153openalex-snapshot
Hydrogen bonding and protein perturbation in β-lactam acyl-enzymes of Streptococcus pneumoniae penicillin-binding protein PBP2x
inferredcites →https://doi.org/10.1042/bj20030217openalex-snapshot
On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides
inferredcites →https://doi.org/10.1042/bj2700525openalex-snapshot
Chromogenic depsipeptide substrates for β-lactamases and penicillin-sensitive dd -peptidases
inferredcites →https://doi.org/10.1042/bj3270377openalex-snapshot
Site-directed mutagenesis of the Actinomadura R39 DD-peptidase
inferredcites →https://doi.org/10.1046/j.1365-2958.1999.01612.xopenalex-snapshot
The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan‐polymerizing penicillin‐binding protein 1b of Escherichia coli
inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03886.xopenalex-snapshot
Overexpression and enzymatic characterization of Neisseria gonorrhoeae penicillin‐binding protein 4
inferredcites →https://doi.org/10.1073/pnas.0407186102openalex-snapshot
Active site restructuring regulates ligand recognition in class A penicillin-binding proteins
inferredcites →https://doi.org/10.1073/pnas.191260798openalex-snapshot
An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci
inferredcites →https://doi.org/10.1073/pnas.64.2.528openalex-snapshot
STRUCTURE OF THE PEPTIDOGLYCAN OF BACTERIAL SPORES: OCCURRENCE OF THE LACTAM OF MURAMIC ACID
inferredcites →https://doi.org/10.1074/jbc.m310177200openalex-snapshot
Crystal Structure of Wild-type Penicillin-binding Protein 5 from Escherichia coli
inferredcites →https://doi.org/10.1074/jbc.m403589200openalex-snapshot
The Basis for Resistance to β-Lactam Antibiotics by Penicillin-binding Protein 2a of Methicillin-resistant Staphylococcus aureus
inferredcites →https://doi.org/10.1074/jbc.m408446200openalex-snapshot
Crystal Structure of a Peptidoglycan Synthesis Regulatory Factor (PBP3) from Streptococcus pneumoniae
inferredcites →https://doi.org/10.1074/jbc.m503271200openalex-snapshot
Crystal Structure of the Actinomadura R39 DD-peptidase Reveals New Domains in Penicillin-binding Proteins
inferredcites →https://doi.org/10.1080/10408410902733979openalex-snapshot
Beta-lactams and Beta-lactamase-inhibitors in current- or potential-clinical practice: A comprehensive update
inferredcites →https://doi.org/10.1110/ps.051641005openalex-snapshot
Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D‐Ala‐D‐Ala peptidase
inferredcites →https://doi.org/10.1110/ps.062112106openalex-snapshot
Structural analysis of an “open” form of PBP1B from Streptococcus pneumoniae
inferredcites →https://doi.org/10.1111/j.1365-2958.2010.07205.xopenalex-snapshot
Septal and lateral wall localization of PBP5, the major D,D‐carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.00597.xopenalex-snapshot
Penicillin‐binding Protein 7/8 of Escherichia coli is a dd ‐endopeptidase
inferredcites →https://doi.org/10.1111/j.1469-0691.2009.02724.xopenalex-snapshot
The antimicrobial resistance profile of Streptococcus pneumoniae
inferredcites →https://doi.org/10.1111/j.1574-6968.2009.01761.xopenalex-snapshot
Characterization of the proteins encoded by theBacillus subtilis yoxA-dacC operon
inferredcites →https://doi.org/10.1111/j.1574-6968.2009.01863.xopenalex-snapshot
A weak dd-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape inEscherichia coli
inferredcites →https://doi.org/10.1126/science.8153626openalex-snapshot
Resistance to Antibiotics Mediated by Target Alterations
inferredcites →https://doi.org/10.1128/aac.01604-06openalex-snapshot
Neisseria gonorrhoeae Isolates with Reduced Susceptibility to Cefixime and Ceftriaxone: Association with Genetic Polymorphisms in penA , mtrR , porB1b , and ponA
inferredcites →https://doi.org/10.1128/aac.38.9.1980openalex-snapshot
Overproduction of a low-affinity penicillin-binding protein and high-level ampicillin resistance in Enterococcus faecium
inferredcites →https://doi.org/10.1128/jb.174.23.7572-7578.1992openalex-snapshot
Possible role of Escherichia coli penicillin-binding protein 6 in stabilization of stationary-phase peptidoglycan
inferredcites →https://doi.org/10.1128/jb.178.1.168-174.1996openalex-snapshot
Naturally occurring peptidoglycan variants of Streptococcus pneumoniae
inferredcites →https://doi.org/10.1128/jb.180.18.4967-4973.1998openalex-snapshot
Characterization of dacC , Which Encodes a New Low-Molecular-Weight Penicillin-Binding Protein in Bacillus subtilis
inferredcites →https://doi.org/10.1128/jb.181.13.3956-3966.1999openalex-snapshot
Analysis of Peptidoglycan Structure from Vegetative Cells of Bacillus subtilis 168 and Role of PBP 5 in Peptidoglycan Maturation
inferredcites →https://doi.org/10.1128/jb.183.5.1595-1599.2001openalex-snapshot
Purification and Characterization of PBP4a, a New Low-Molecular-Weight Penicillin-Binding Protein from Bacillus subtilis
inferredcites →https://doi.org/10.1128/jb.184.13.3630-3639.2002openalex-snapshot
Contribution of Membrane-Binding and Enzymatic Domains of Penicillin Binding Protein 5 to Maintenance of Uniform Cellular Morphology of Escherichia coli
inferredcites →https://doi.org/10.1128/microbiolspec.gpp3-0018-2018openalex-snapshot
The Cell Wall of Streptococcus pneumoniae
inferredcites →https://doi.org/10.1128/mmbr.62.1.181-203.1998openalex-snapshot
Growth of the Stress-Bearing and Shape-Maintaining Murein Sacculus of Escherichia coli
inferredcites →https://doi.org/10.1146/annurev.bi.48.070179.000445openalex-snapshot
Use of Model Enzymes in the Determination of the Mode of Action of Penicillins and Delta3-Cephalosporins
inferredcites →https://doi.org/10.1146/annurev.mi.45.100191.000345openalex-snapshot
SERINE β-LACTAMASES AND PENICILLIN-BINDING PROTEINS
inferredcites →https://doi.org/10.1186/1472-6807-3-7openalex-snapshot
Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site
inferredcites →https://doi.org/10.2142/biophys.45.s124_1openalex-snapshot
2P017 Crystal structure of penicillin binding protein 4 from Escherichia coli, both in the native form and covalently linked to antibiotics
inferredcites →https://doi.org/10.3109/10408418409105906openalex-snapshot
Penicillin-Sensitive Enzymes in Peptidoglycan Biosynthesis
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4087303openalex-extracted
Small Molecules as Modulators of Active Forms of MMPs
inferred← citeshttps://doi.org/10.1002/cbic.202200693openalex-snapshot
Mechanistic Insights into the Activities of Major Families of Enzymes in Bacterial Peptidoglycan Assembly and Breakdown
inferred← citeshttps://doi.org/10.1002/chem.202004831openalex-snapshot
Synthesis of Carbapenems Containing Peptidoglycan Mimetics and Inhibition of the Cross‐Linking Activity of a Transpeptidase of l,d Specificity
inferred← citeshttps://doi.org/10.1007/978-3-642-39968-8_4openalex-snapshot
The β-Lactam Antibiotics: Their Future in the Face of Resistance
inferred← citeshttps://doi.org/10.1007/s10930-018-9765-yopenalex-snapshot
Substitution of Alanine at Position 184 with Glutamic Acid in Escherichia coli PBP5 Ω-Like Loop Introduces a Moderate Cephalosporinase Activity
inferred← citeshttps://doi.org/10.1016/j.biochi.2023.10.021openalex-snapshot
Small molecular exogenous modulators of active forms of MMPs
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.151221openalex-snapshot
The OTA-degrading phenotype in the Lysobacter and Stenotrophomonas genera is conferred by the hydrolytic activity of subtype I amidohydrolases
inferred← citeshttps://doi.org/10.1021/acs.biochem.6b00576openalex-snapshot
Synthesis and Kinetic Analysis of Two Conformationally Restricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.1c00717openalex-snapshot
High-Throughput Crystallography Reveals Boron-Containing Inhibitors of a Penicillin-Binding Protein with Di- and Tricovalent Binding Modes
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.6b00448openalex-snapshot
β-Lactamases: Why and How
inferred← citeshttps://doi.org/10.1021/bi300148vopenalex-snapshot
Inhibition of Bacterial DD-Peptidases (Penicillin-Binding Proteins) in Membranes and in Vivo by Peptidoglycan-Mimetic Boronic Acids
inferred← citeshttps://doi.org/10.1021/bi400048sopenalex-snapshot
Inhibition of dd -Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 dd -Peptidase
inferred← citeshttps://doi.org/10.1021/bi400211qopenalex-snapshot
Dual Substrate Specificity of Bacillus subtilis PBP4a
inferred← citeshttps://doi.org/10.1021/bi500970fopenalex-snapshot
Interactions of “Bora-Penicilloates” with Serine β-Lactamases and DD-Peptidases
inferred← citeshttps://doi.org/10.1021/ja508147sopenalex-snapshot
Detection of Lipid-Linked Peptidoglycan Precursors by Exploiting an Unexpected Transpeptidase Reaction
inferred← citeshttps://doi.org/10.1021/ml3001006openalex-snapshot
4-Quinolones as Noncovalent Inhibitors of High Molecular Mass Penicillin-Binding Proteins
inferred← citeshttps://doi.org/10.1089/mdr.2016.0084openalex-snapshot
Promoter Identification and Transcription Analysis of Penicillin-Binding Protein Genes in Streptococcus pneumoniae R6
inferred← citeshttps://doi.org/10.1099/mic.0.000074openalex-snapshot
A putative low-molecular-mass penicillin-binding protein (PBP) of Mycobacterium smegmatis exhibits prominent physiological characteristics of dd-carboxypeptidase and beta-lactamase
inferred← citeshttps://doi.org/10.1111/1462-2920.12189openalex-snapshot
From models to pathogens: how much have we learned about S treptococcus pneumoniae cell division?
inferred← citeshttps://doi.org/10.1201/b17871-17openalex-snapshot
Bacterial Cell Wall: Morphology and Biochemistry
inferred← citeshttps://doi.org/10.14418/wes01.3.27openalex-snapshot
Design of Hydroxamic Acid-Based Inhibitors for Serine β-Lactamases
inferred← citeshttps://doi.org/10.33263/briac112.89969006openalex-snapshot
An In Silico Study for the Identification of Novel Putative Compounds Against the Wild and Mutant Type Penicillin Binding Protein 2 of Neisseria Gonorrhoeae
inferred← citeshttps://doi.org/10.3390/ph18091325openalex-snapshot
Boronate-Based Inhibitors of Penicillin-Binding Proteins: An Underestimated Avenue for Antibiotic Discovery?
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.