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Insights into Key Interactions between Vancomycin and Bacterial Cell Wall Structures
37/37 checkable references clean · checked 2026-07-23
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
1 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 37 checked references that resolve
resolves10.1021/ar00022a006
D-Alanyl-D-alanine ligases and the molecular mechanism of vancomycin resistance
resolves10.1126/science.284.5413.482
Dissecting and Exploiting Intermodular Communication in Polyketide Synthases
resolves10.7164/antibiotics.46.1181
Structure-activity relationships of vancomycin-type glycopeptide antibiotics.
resolves10.1146/annurev.mi.38.100184.002011
THE STRUCTURE AND MODE OF ACTION OF GLYCOPEPTIDE ANTIBIOTICS OF THE VANCOMYCIN GROUP
resolves10.1128/aac.36.4.867
Evidence for in vivo incorporation of D-lactate into peptidoglycan precursors of vancomycin-resistant enterococci
resolves10.1021/bi00107a007
Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA
resolves10.1002/chem.201102195
Molecular Interactions between Glycopeptide Vancomycin and Bacterial Cell Wall Peptide Analogues
resolves10.1002/1521-3773(20010504)40:9<1693::aid-anie16930>3.0.co;2-8
The Biosynthesis of Vancomycin-Type Glycopeptide Antibiotics—New Insights into the Cyclization Steps
resolves10.1021/ja963566p
Simultaneous Recognition of a Carboxylate-Containing Ligand and an Intramolecular Surrogate Ligand in the Crystal Structure of an Asymmetric Vancomycin Dimer
resolves10.1016/s0969-2126(94)00075-1
The structure of an asymmetric dimer relevant to the mode of action of the glycopeptide antibiotics
resolves10.7164/antibiotics.48.805
Cooperativity between Non-polar and Ionic Forces in the Binding of Bacterial Cell Wall Analogues by Vancomycin in Aqueous Solution.
resolves10.1021/bi0121407
Rotational-Echo Double Resonance Characterization of Vancomycin Binding Sites in <i>Staphylococcus aureus</i>
resolves10.1021/bi052660s
Structures of <i>Staphylococcus aureus</i> Cell-Wall Complexes with Vancomycin, Eremomycin, and Chloroeremomycin Derivatives by <sup>13</sup>C{<sup>19</sup>F} and <sup>15</sup>N{<sup>19</sup>F} Rotational-Echo Double Resonance
resolves10.1016/j.jmb.2008.01.031
Oritavancin Exhibits Dual Mode of Action to Inhibit Cell-Wall Biosynthesis in Staphylococcus aureus
resolves10.1021/bi702232a
Vancomycin Derivative with Damaged <scp>d</scp>-Ala-<scp>d</scp>-Ala Binding Cleft Binds to Cross-linked Peptidoglycan in the Cell Wall of Staphylococcus aureus
resolves10.1021/bi800838c
Hydrophobic Side-Chain Length Determines Activity and Conformational Heterogeneity of a Vancomycin Derivative Bound to the Cell Wall of <i>Staphylococcus aureus</i>
resolves10.1016/j.jmb.2009.06.033
Oritavancin Binds to Isolated Protoplast Membranes but not Intact Protoplasts of Staphylococcus aureus
resolves10.1021/bi400054p
Locations of the Hydrophobic Side Chains of Lipoglycopeptides Bound to the Peptidoglycan of <i>Staphylococcus aureus</i>
resolves10.1021/acs.biochem.6b01125
Desleucyl-Oritavancin with a Damaged <scp>d</scp>-Ala-<scp>d</scp>-Ala Binding Site Inhibits the Transpeptidation Step of Cell-Wall Biosynthesis in Whole Cells of <i>Staphylococcus aureus</i>
resolves10.1021/acs.biochem.6b00188
The Carboxyl Terminus of Eremomycin Facilitates Binding to the Non-<scp>d</scp>-Ala-<scp>d</scp>-Ala Segment of the Peptidoglycan Pentapeptide Stem
resolves10.1039/p19890002335
Preparation and conformational analysis of vancomycin hexapeptide and aglucovancomycin hexapeptide
resolves10.1128/aac.46.8.2344-2348.2002
Hexapeptide Derivatives of Glycopeptide Antibiotics: Tools for Mechanism of Action Studies
resolves10.1021/bi048357t
Synchronized Conformational Fluctuations and Binding Site Desolvation during Molecular Recognition
resolves10.1002/jcc.21367
CHARMM general force field: A force field for drug‐like molecules compatible with the CHARMM all‐atom additive biological force fields
resolves10.1002/jcc.540040211
<scp>CHARMM</scp>: A program for macromolecular energy, minimization, and dynamics calculations
resolves10.1016/j.bbamem.2014.05.025
REDOR constraints on the peptidoglycan lattice architecture of Staphylococcus aureus and its FemA mutant
resolves10.1016/j.bbamem.2014.05.031
Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR
resolves10.1021/ja00046a032
The representation of van der Waals (vdW) interactions in molecular mechanics force fields: potential form, combination rules, and vdW parameters
resolves10.1002/bip.360230610
Quasi‐harmonic method for studying very low frequency modes in proteins
The 1 reference without a DOI — listed, not checked
no DOI — not checkedFrisch, M.; Trucks, G.; Schlegel, H. B.; Scuseria, G.; Robb, M.; Cheeseman, J.; Scalmani, G.; Barone, V.; Mennucci, B.; Petersson, G.Gaussian 09, revision a. 02,Gaussian. Inc.:Wallingford, CT, 2009, 200.
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