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1. Full Text Metallo‐β‐lactamase structure and function
by Palzkill, Timothy
Annals of the New York Academy of Sciences, ISSN 0077-8923, 01/2013, Volume 1277, Issue 1, pp. 91 - 104
β‐Lactam antibiotics are the most commonly used antibacterial agents and growing resistance to these drugs is a concern. Metallo‐β‐lactamases are a diverse set... 
carbapenem | antibiotic resistance | β‐lactamase | zinc metallo‐enzyme | Carbapenem | Zinc metallo-enzyme | β-lactamase | Antibiotic resistance | ACTIVE-SITE | zinc metallo-enzyme | CRYSTAL-STRUCTURE | ANTIBIOTIC-RESISTANCE | SITE-DIRECTED MUTAGENESIS | BACTEROIDES-FRAGILIS | PSEUDOMONAS-AERUGINOSA | PENICILLIN-BINDING PROTEINS | PHARMACOLOGY & PHARMACY | beta-lactamase | BACILLUS-CEREUS | STANDARD NUMBERING SCHEME | BACTERIAL-CELL WALL | beta-Lactamases - chemistry | Catalytic Domain | beta-Lactamases - classification | Mutagenesis | Metalloendopeptidases - chemistry | Protein Binding | Substrate Specificity | Metalloendopeptidases - metabolism | Catalysis | Metalloendopeptidases - classification | beta-Lactamases - metabolism | Drugs | Enzymes | Inhibitors | Genes | Blocking | Bacteria | Antiinfectives and antibacterials | Zinc
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2. Full Text Peptidoglycan structure and architecture
by Vollmer, Waldemar and Blanot, Didier and De Pedro, Miguel A
FEMS Microbiology Reviews, ISSN 0168-6445, 03/2008, Volume 32, Issue 2, pp. 149 - 167
The peptidoglycan (murein) sacculus is a unique and essential structural element in the cell wall of most bacteria. Made of glycan strands cross‐linked by... 
peptidoglycan | murein | bacterial cell wall | Peptidoglycan | Bacterial cell wall | Murein | STAPHYLOCOCCUS-AUREUS STRAIN | MICROBIOLOGY | INNATE IMMUNE-SYSTEM | PERFORMANCE LIQUID-CHROMATOGRAPHY | GRAM-POSITIVE BACTERIA | D-GLUTAMIC ACID | ATOMIC-FORCE MICROSCOPY | PENICILLIN-BINDING-PROTEINS | BACILLUS-SUBTILIS 168 | ESCHERICHIA-COLI MUREIN | CELL-WALL PEPTIDOGLYCAN | Peptidoglycan - biosynthesis | Bacteria - chemistry | Peptidoglycan - chemistry | Bacteria - cytology | Models, Molecular | Molecular Structure | Cell Wall - chemistry | Escherichia coli - chemistry | Peptidoglycan - classification | Escherichia coli - ultrastructure | Peptidoglycans
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3. Full Text Pectin structure and biosynthesis
by Mohnen, Debra and Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center (BESC)
Current Opinion in Plant Biology, ISSN 1369-5266, 2008, Volume 11, Issue 3, pp. 266 - 277
Pectin is structurally and functionally the most complex polysaccharide in plant cell walls. Pectin has functions in plant growth, morphology, development, and... 
S-ADENOSYLMETHIONINE | HOMOGALACTURONAN | ARABIDOPSIS-THALIANA | GLUCURONOXYLAN BIOSYNTHESIS | PLANTS | XYLOGLUCAN COMPLEX | GOLGI | POLYSACCHARIDE RHAMNOGALACTURONAN-II | ENZYMATIC DEGRADATION | CELL-WALL BIOSYNTHESIS | PLANT SCIENCES | Carbohydrate Sequence | Plants - metabolism | Cell Wall - metabolism | Molecular Sequence Data | Pectins - biosynthesis | Hexuronic Acids - chemistry | Hexuronic Acids - metabolism | Pectins - chemistry | Plants - enzymology | Physiological aspects | Pectin
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4. Full Text Peptidoglycan Structure
by Schumann, Peter
2011, Methods in Microbiology, ISBN 012387730X, Volume 38, 29
Information on the peptidoglycan structure is an indispensable component for the description of new genera of Gram-positive bacteria. In certain genera,... 
bacterial systematics | isolation of peptidoglycan | peptidoglycan structure | chemotaxonomy | Chemotaxonomy | Peptidoglycan structure | Bacterial systematics | Isolation of peptidoglycan | MYCOBACTERIUM-TUBERCULOSIS | ACYL TYPE | GAS-CHROMATOGRAPHY | AMINO ACID SEQUENCE | BACTERIAL-CELL-WALLS | BIOCHEMICAL RESEARCH METHODS | MINIMAL STANDARDS | MICROBIOLOGY | TAXONOMIC SIGNIFICANCE | GLYCOLATE TEST | SIMPLE IDENTIFICATION | COMB. NOV
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5. Fungal cell wall
: structure, synthesis, and assembly
by Ruiz-Herrera, José
2012, 2nd ed., ISBN 9781439848371, cm.
Book
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6. Full Text Lignin Biosynthesis and Structure
by Ruben Vanholme and Brecht Demedts and Kris Morreel and John Ralph and Wout Boerjan and Great Lakes Bioenergy Research Center (GLBRC)
Plant Physiology, ISSN 0032-0889, 7/2010, Volume 153, Issue 3, pp. 895 - 905
Lignin | Transcription factors | Cell walls | Genes | Biosynthesis | Update on Lignin Biosynthesis and Structure | Plants | Polymers | Monomers | Alcohols | Plant cells | DOMAIN TRANSCRIPTION FACTOR | ARABIDOPSIS-THALIANA | SECONDARY METABOLISM | O-METHYLTRANSFERASE ACTIVITY | CINNAMYL-ALCOHOL-DEHYDROGENASE | PHENYLPROPANOID METABOLISM | CELL-WALL FORMATION | DOWN-REGULATION | FERULATE 5-HYDROXYLASE | CAD-DEFICIENT | PLANT SCIENCES | Lignin - chemistry | Lignin - biosynthesis | Biological Transport | Metabolic Networks and Pathways | Gene Expression Regulation, Plant | Evolution, Molecular | Research | Properties | Phytochemistry
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7. Full Text Esau's Plant anatomy
: meristems, cells, and tissues of the plant body : their structure, function, and development
by Evert, Ray Franklin and Esau, Katherine, 1898
2006, 3rd ed., ISBN 9780471738435, 623
This revision of the now classic Plant Anatomy offers a completely updated review of the structure, function, and development of meristems, cells, and tissues... 
Plant morphology | Plant anatomy
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8. Full Text Modular structure of the receptor binding proteins of Lactococcus lactis phages: The RBP structure of the temperate phage TP901-1
by Spinelli, Silvia and Campanacci, Valérie and Blangy, Stéphanie and Moineau, Sylvain and Tegoni, Mariella and Cambillau, Christian
Journal of Biological Chemistry, ISSN 0021-9258, 05/2006, Volume 281, Issue 20, pp. 14256 - 14262
Lactococcus lactis is a Gram-positive bacterium widely used by the dairy industry. Several industrial L. lactis strains are sensitive to various distinct... 
BACTERIOPHAGES | ATTACHMENT | CELL-WALL | EVOLUTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACID BACTERIA | BETA-HELIX | IDENTIFICATION | CHEESE | ADENOVIRUS FIBER | Protein Structure, Tertiary | Amino Acid Sequence | Bacteriophages - chemistry | Protein Structure, Secondary | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Lactococcus lactis - virology | Microscopy, Electron | Cell Wall - metabolism | Protein Binding | Carrier Proteins - chemistry | Protein Conformation | Glycerol - chemistry
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9. Full Text Downregulation of Cinnamoyl-Coenzyme A Reductase in Poplar: Multiple-Level Phenotyping Reveals Effects on Cell Wall Polymer Metabolism and Structure
by Jean-Charles Leplé and Rebecca Dauwe and Kris Morreel and Véronique Storme and Catherine Lapierre and Brigitte Pollet and Annette Naumann and Kyu-Young Kang and Hoon Kim and Katia Ruel and Andrée Lefèbvre and Jean-Paul Joseleau and Jacqueline Grima-Pettenati and Riet De Rycke and Sara Andersson-Gunnerås and Alexander Erban and Ines Fehrle and Michel Petit-Conil and Joachim Kopka and Andrea Polle and Eric Messens and Björn Sundberg and Shawn D. Mansfield and John Ralph and Gilles Pilate and Wout Boerjan and Sveriges lantbruksuniversitet
The Plant Cell, ISSN 1040-4651, 11/2007, Volume 19, Issue 11, pp. 3669 - 3691
Cinnamoyl-CoA reductase (CCR) catalyzes the penultimate step in monolignol biosynthesis. We show that downregulation of CCR in transgenic poplar (Populus... 
Lignin | Xylem | Colors | Cell walls | Genes | Biosynthesis | Plants | Down regulation | Transgenic plants | Plant cells | SERINE-CARBOXYPEPTIDASE | ARABIDOPSIS-THALIANA | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHENYLPROPANOID METABOLISM | O-METHYLTRANSFERASE | MONOLIGNOL BIOSYNTHESIS | ARABINOGALACTAN-PROTEIN | PLANT SCIENCES | CELL BIOLOGY | ALCOHOL-DEHYDROGENASE | COA-REDUCTASE | CHROMATOGRAPHY-MASS SPECTROMETRY | LIGNIN BIOSYNTHESIS | Immunohistochemistry | Carbohydrates | Solubility | Fluorescence | Lignin - chemistry | Gene Expression Profiling | Populus - genetics | Aldehyde Oxidoreductases - genetics | Cell Wall - chemistry | Chromatography, High Pressure Liquid | Spectroscopy, Fourier Transform Infrared | Down-Regulation - genetics | Phenols - analysis | Phenotype | Populus - enzymology | Xylem - cytology | Lignin - metabolism | Plants, Genetically Modified | Gene Expression Regulation, Plant | Populus - cytology | Xylem - growth & development | Populus - ultrastructure | Cell Wall - ultrastructure | Xylem - ultrastructure | Physiological aspects | Poplar | Coenzymes | Chemical properties | Skogsvetenskap | Forest Science
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10. Full Text Anchor structure of staphylococcal surface proteins: V. Anchor structure of the sortase B substrate IsdC
by Marraffini, Luciano A and Schneewind, Olaf
Journal of Biological Chemistry, ISSN 0021-9258, 04/2005, Volume 280, Issue 16, pp. 16263 - 16271
Staphylococcus aureus sortase A cleaves surface protein precursors bearing C-terminal LPXTG motif sorting signals between the threonine and glycine residues.... 
GRAM-POSITIVE BACTERIA | CELL-WALL | PEPTIDOGLYCAN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SENSITIVE ENZYMATIC REACTIONS | SORTING REACTION | CROSS-LINKING | AUREUS STRAIN COPENHAGEN | D-ALANINE CARBOXYPEPTIDASE | LPXTG MOTIF | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Cysteine Endopeptidases | Staphylococcus aureus - enzymology | Carrier Proteins - metabolism | Endopeptidase K - metabolism | Aminoacyltransferases - metabolism | Carrier Proteins - chemistry | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Bacterial Proteins | Staphylococcus aureus - metabolism
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11. Full Text The penicillin‐binding proteins: structure and role in peptidoglycan biosynthesis
by Sauvage, Eric and Kerff, Frédéric and Terrak, Mohammed and Ayala, Juan A and Charlier, Paulette
FEMS Microbiology Reviews, ISSN 0168-6445, 03/2008, Volume 32, Issue 2, pp. 234 - 258
Penicillin‐binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long‐term... 
3D structure | transpeptidase | penicillin‐binding | transglycosylase | peptidoglycan synthesis | Peptidoglycan synthesis | Transglycosylase | Penicillin-binding | Transpeptidase | BETA-LACTAM RESISTANCE | ACYL-ENZYME COMPLEX | ESCHERICHIA-COLI | penicillin-binding | ALA-PEPTIDASE REVEALS | MICROBIOLOGY | PREDICTED SECONDARY STRUCTURES | ENTEROCOCCUS-FAECIUM BM4339 | STREPTOCOCCUS-PNEUMONIAE | BACILLUS-SUBTILIS | ALANINE CARBOXYPEPTIDASE IA | CELL-WALL PEPTIDOGLYCAN | Protein Structure, Tertiary | Bacteria - metabolism | Peptidyl Transferases - metabolism | Bacteria - chemistry | Multienzyme Complexes - classification | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Glycosyltransferases - chemistry | Penicillin-Binding Proteins - classification | Peptidyl Transferases - chemistry | Bacterial Proteins - chemistry | Multienzyme Complexes - metabolism | Penicillin-Binding Proteins - metabolism | Peptide Hydrolases - chemistry | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Glycosyltransferases - metabolism | beta-Lactams - pharmacology | Penicillin-Binding Proteins - chemistry | Bacterial Proteins - metabolism | Bacterial Proteins - classification | beta-Lactamases - metabolism | Peptide Hydrolases - metabolism | Physiological aspects | Peptidoglycans
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