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Journal Article
Science, ISSN 0036-8075, 6/2011, Volume 332, Issue 6036, pp. 1401 - 1403
Root hairs are single cells that develop by tip growth and are specialized in the absorption of nutrients. Their cell walls are composed of polysaccharides and... 
Enzymes | Cell growth | Phenotypes | Polysaccharides | Cell walls | RESEARCH ARTICLES | Hair cells | Root hairs | Biochemistry | Plants | Plant cells | MOLECULAR CHARACTERIZATION | MUTANTS | EXTENSIN | CODES | MULTIDISCIPLINARY SCIENCES | GENES | REQUIRES | ARABIDOPSIS | IDENTIFICATION | PROLYL 4-HYDROXYLASE | TOBACCO | Arabidopsis - growth & development | Genes, Plant | Proline - metabolism | Glycoproteins - metabolism | Pentosyltransferases - metabolism | Procollagen-Proline Dioxygenase - metabolism | Arabidopsis Proteins - metabolism | Pentosyltransferases - chemistry | Plant Proteins - chemistry | Arabinose - metabolism | Gene Expression Regulation, Plant | Polysaccharides - chemistry | Plant Proteins - metabolism | Glycosyltransferases - genetics | Glycoproteins - chemistry | Plant Roots - growth & development | Arabidopsis Proteins - genetics | Plant Roots - metabolism | Hydroxylation | Protein Structure, Secondary | Hydroxyproline - metabolism | Glycosylation | Plant Roots - cytology | Arabidopsis - metabolism | Arabidopsis - genetics | Glycosyltransferases - metabolism | Phenotype | Arabidopsis Proteins - chemistry | Procollagen-Proline Dioxygenase - genetics | Models, Biological | Cell Wall - metabolism | Protein Conformation | Protein Processing, Post-Translational | Mutation | Carbohydrate Conformation | Hair | Physiological aspects | Glycoproteins | Genetic aspects | Growth
Journal Article
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
Journal Article
BBA - General Subjects, ISSN 0304-4165, 05/2017, Volume 1861, Issue 5, pp. 1036 - 1045
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