X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (3578) 3578
Publication (700) 700
Book Review (331) 331
Book Chapter (37) 37
Conference Proceeding (13) 13
Book / eBook (5) 5
Dissertation (2) 2
Data Set (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (3388) 3388
microbiology (1647) 1647
biochemistry & molecular biology (1237) 1237
humans (1090) 1090
molecular sequence data (1085) 1085
amino acid sequence (906) 906
bacteria (862) 862
fimbriae, bacterial - metabolism (843) 843
animals (830) 830
bacterial proteins - genetics (760) 760
fimbriae proteins (740) 740
proteins (730) 730
bacterial proteins - metabolism (651) 651
escherichia-coli (641) 641
fimbriae proteins - metabolism (605) 605
fimbriae proteins - genetics (600) 600
escherichia coli (595) 595
escherichia coli - genetics (591) 591
bacterial adhesion (569) 569
immunology (542) 542
fimbriae, bacterial - genetics (541) 541
fimbriae, bacterial - chemistry (501) 501
fimbriae proteins - chemistry (485) 485
fimbriae, bacterial - physiology (483) 483
fimbriae (482) 482
base sequence (466) 466
virulence (459) 459
mutation (450) 450
research (449) 449
protein (412) 412
pili (409) 409
bacterial proteins - chemistry (402) 402
genes (392) 392
gene expression regulation, bacterial (382) 382
analysis (381) 381
escherichia coli - metabolism (377) 377
expression (370) 370
models, molecular (359) 359
genes, bacterial (357) 357
fimbriae, bacterial - ultrastructure (343) 343
mice (343) 343
bacteriology (341) 341
infectious diseases (340) 340
protein binding (334) 334
genetic aspects (319) 319
physiological aspects (306) 306
gene expression (300) 300
identification (294) 294
pseudomonas-aeruginosa (292) 292
cell biology (290) 290
escherichia coli - pathogenicity (279) 279
adhesion (278) 278
bacterial outer membrane proteins - genetics (273) 273
escherichia coli proteins - genetics (271) 271
gram-negative bacteria (271) 271
escherichia coli proteins (267) 267
e coli (264) 264
escherichia coli proteins - metabolism (261) 261
multidisciplinary sciences (253) 253
binding (251) 251
epithelial-cells (247) 247
research article (238) 238
article (235) 235
fimbriae, bacterial - immunology (233) 233
biofilms (230) 230
biophysics (229) 229
binding sites (228) 228
protein conformation (227) 227
cloning, molecular (226) 226
female (224) 224
type-1 fimbriae (221) 221
bacterial proteins (218) 218
sequence homology, amino acid (216) 216
cells (214) 214
dna, bacterial - genetics (212) 212
adherence (211) 211
protein structure, tertiary (207) 207
gene (206) 206
escherichia coli - physiology (205) 205
uropathogenic escherichia-coli (205) 205
biofilm formation (203) 203
twitching motility (203) 203
escherichia coli proteins - chemistry (200) 200
bacterial adhesion - physiology (197) 197
pathogens (194) 194
dna (191) 191
biochemical phenomena, metabolism, and nutrition (188) 188
biogenesis (187) 187
escherichia coli infections - microbiology (184) 184
plasmids (184) 184
biochemistry (182) 182
biology (180) 180
sequence alignment (178) 178
bacterial outer membrane proteins - metabolism (177) 177
adhesins, bacterial - metabolism (175) 175
crystallography, x-ray (173) 173
nucleotide-sequence (169) 169
microscopy, electron (168) 168
sequence analysis, dna (168) 168
pilin (166) 166
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (3568) 3568
Japanese (6) 6
Russian (6) 6
Chinese (5) 5
French (2) 2
Polish (2) 2
Spanish (1) 1
Turkish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Science, ISSN 0036-8075, 9/2011, Volume 333, Issue 6048, pp. 1445 - 1449
Bacterial chromosomes are confined in submicrometer-sized nucleoids. Chromosome organization is facilitated by nucleoid-associated proteins (NAPs), but the... 
Proteins | Molecules | DNA | Genes | Imaging | REPORTS | Cell lines | Genetic loci | Gene expression regulation | Genomes | Chromosomes | CELLS | STRUCTURING PROTEIN | CAULOBACTER-CRESCENTUS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | GENE-EXPRESSION | OPTICAL RECONSTRUCTION MICROSCOPY | H-NS PROTEIN | BINDING | GENOME | Molecular Chaperones - metabolism | DNA, Bacterial - metabolism | Factor For Inversion Stimulation Protein - metabolism | Fimbriae Proteins - metabolism | Protein Multimerization | DNA, Bacterial - chemistry | Genetic Loci | Recombinant Fusion Proteins - metabolism | Escherichia coli K12 - ultrastructure | DNA-Binding Proteins - metabolism | Integration Host Factors - metabolism | Chromosomes, Bacterial - metabolism | Escherichia coli K12 - metabolism | Cell Division | Nucleic Acid Conformation | Binding Sites | Repressor Proteins - metabolism | Protein Structure, Tertiary | Genome, Bacterial | Repressor Proteins - chemistry | Operon | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Chromosomes, Bacterial - ultrastructure | Fimbriae Proteins - genetics | Escherichia coli Proteins - genetics | Fimbriae Proteins - chemistry | Escherichia coli K12 - genetics | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Cellular proteins | Research | Properties | Bacterial genetics | E coli | Microbiology | Bacterial proteins | Index Medicus
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6946 - 6957
Type IV pili (T4P) are ubiquitous bacterial cell surface structures, involved in processes such as twitching motility, biofilm formation, bacteriophage... 
CYTOPLASMIC DOMAIN | ATPase | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NEISSERIA-MENINGITIDIS | VIBRIO-CHOLERAE | BIOGENESIS PROTEIN | cell motility | secretion | TWITCHING MOTILITY | Myxococcus xanthus | PSEUDOMONAS-AERUGINOSA | N-TERMINAL DOMAIN | membrane transport | membrane reconstitution | II SECRETION SYSTEM | THERMUS-THERMOPHILUS | type IV pili | Virulence Factors - genetics | Fimbriae Proteins - metabolism | Protein Multimerization | Virulence | Fimbriae, Bacterial - genetics | Molecular Motor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Nucleotides - chemistry | Pseudomonas aeruginosa - metabolism | Adenosine Triphosphate - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Molecular Motor Proteins - metabolism | Gene Expression | Myxococcus xanthus - genetics | Adenosine Triphosphatases - metabolism | Fimbriae, Bacterial - chemistry | Myxococcus xanthus - pathogenicity | Virulence Factors - chemistry | Myxococcus xanthus - metabolism | Recombinant Fusion Proteins - chemistry | Molecular Motor Proteins - chemistry | Nucleotides - metabolism | Bacterial Adhesion | Liposomes - chemistry | Fimbriae Proteins - genetics | Pseudomonas aeruginosa - genetics | Escherichia coli - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Adenosine Triphosphatases - chemistry | Fimbriae Proteins - chemistry | Liposomes - metabolism | Virulence Factors - metabolism | Adenosine Triphosphatases - genetics | Kinetics | Adenosine Triphosphate - chemistry | Fimbriae, Bacterial - metabolism | Index Medicus | Membrane Biology
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 2758 - 11
Uropathogenic Escherichia coil attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed by the domains of the... 
UROPATHOGENIC ESCHERICHIA-COLI | DISULFIDE BOND FORMATION | ATOMIC-FORCE MICROSCOPY | SINGLE PROTEIN | CHAPERONE-USHER PATHWAY | STABILITY | MULTIDISCIPLINARY SCIENCES | FIMD USHER | CATCH BONDS | DONOR-STRAND EXCHANGE | DSBA | Disulfides - metabolism | Molecular Chaperones - metabolism | Fimbriae Proteins - metabolism | Protein Disulfide-Isomerases - metabolism | Molecular Chaperones - chemistry | Fimbriae, Bacterial - genetics | Adhesins, Escherichia coli - chemistry | Adhesins, Escherichia coli - genetics | Uropathogenic Escherichia coli - metabolism | Uropathogenic Escherichia coli - ultrastructure | Disulfides - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Microscopy, Atomic Force | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Adhesins, Escherichia coli - metabolism | Genetic Vectors - chemistry | Molecular Chaperones - genetics | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Fimbriae, Bacterial - ultrastructure | Recombinant Proteins - genetics | Uropathogenic Escherichia coli - genetics | Molecular Dynamics Simulation | Protein Folding | Protein Disulfide-Isomerases - genetics | Fimbriae Proteins - genetics | Protein Conformation, beta-Strand | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Fimbriae Proteins - chemistry | Protein Disulfide-Isomerases - chemistry | Escherichia coli Proteins - chemistry | Fimbriae, Bacterial - metabolism | Pathogens | Spectroscopy | Disulfide bonds | Stability | Pili | Oxidoreductase | Escherichia coli | Folding | Molecular chains | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2015, Volume 290, Issue 1, pp. 601 - 611
Journal Article
PLoS Pathogens, ISSN 1553-7366, 01/2012, Volume 8, Issue 1, pp. e1002373 - e1002373
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2016, Volume 113, Issue 26, pp. 7130 - 7135
Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of , as well as many other enteric bacteria, and... 
Aggregation | CsgG | Intrinsically disordered protein | Protein-protein interaction | Biofilm formation | intrinsically disordered protein | CURLI BIOSYNTHESIS | ENTERICA SEROVAR TYPHIMURIUM | MULTIDISCIPLINARY SCIENCES | biofilm formation | aggregation | BACTERIAL BIOFILMS | SALMONELLA-ENTERITIDIS | THIN AGGREGATIVE FIMBRIAE | SURFACE ORGANELLES | ESCHERICHIA-COLI K-12 | protein-protein interaction | NEGATIVE DETERMINANTS | AUTOMATED NOE ASSIGNMENT | Molecular Chaperones - metabolism | Lipoproteins - genetics | Bacterial Proteins - chemistry | Amyloid - chemistry | Molecular Chaperones - chemistry | Amyloid - metabolism | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | Lipoproteins - metabolism | Membrane Transport Proteins - metabolism | Amyloid - genetics | Magnetic Resonance Spectroscopy | Bacterial Proteins - genetics | Molecular Chaperones - genetics | Escherichia coli Proteins - metabolism | Lipoproteins - chemistry | Escherichia coli - chemistry | Membrane Transport Proteins - chemistry | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Bacterial Proteins - metabolism | Protein Conformation | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Magnetic resonance imaging | Bacterial proteins | Physiological aspects | Glycoproteins | Structure | Health aspects | Methods | Proteins | Nuclear magnetic resonance--NMR | Biofilms | Microscopy | Binding sites | Electrons | Index Medicus | protein–protein interaction | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2016, Volume 113, Issue 37, pp. 10352 - 10357
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2014, Volume 289, Issue 49, pp. 34349 - 34365
Background: Bacterial fimbriae mediate binding to host tissue through specific interactions. Results: ECP interacts with arabinosyl residues in pectin and... 
UNITED-STATES | Ligand-binding Protein | Glycan Array | BIOCHEMISTRY & MOLECULAR BIOLOGY | Escherichia coli (E | coli | COLONIZATION | ARABINOGALACTAN-PROTEINS | VIBRIO-CHOLERAE | E. COLI | Bacterial Adhesion | Arabinose | Glycobiology | O157-H7 | Plant Cell Wall | Organelle | Adhesin | MONOCLONAL-ANTIBODIES | OUTBREAK | CONSUMPTION | Host-Pathogen Interaction | BIOFILM FORMATION | Cell Wall - microbiology | Antibody Specificity | Molecular Chaperones - metabolism | Plant Cells - microbiology | Adhesins, Bacterial - chemistry | Fimbriae Proteins - metabolism | Adhesins, Bacterial - genetics | Spinacia oleracea - metabolism | Molecular Chaperones - chemistry | Fimbriae, Bacterial - genetics | Adhesins, Bacterial - metabolism | Arabinose - metabolism | Polysaccharides - chemistry | Plant Cells - chemistry | Antibodies, Monoclonal - chemistry | Recombinant Proteins - metabolism | Arabinose - chemistry | Plant Cells - metabolism | Escherichia coli O157 - genetics | Escherichia coli O157 - metabolism | Molecular Chaperones - genetics | Fimbriae, Bacterial - chemistry | Recombinant Proteins - chemistry | Spinacia oleracea - microbiology | Escherichia coli Proteins - metabolism | Recombinant Proteins - genetics | Cell Wall - chemistry | Escherichia coli O157 - chemistry | Polysaccharides - metabolism | Host-Pathogen Interactions | Fimbriae Proteins - genetics | Cell Wall - metabolism | Escherichia coli Proteins - genetics | Protein Binding | Spinacia oleracea - chemistry | Fimbriae Proteins - chemistry | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Fimbriae, Bacterial - metabolism | Index Medicus | Microbiology | Escherichia coli (E. coli)
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2011, Volume 108, Issue 25, pp. 10278 - 10283
Structural vaccinology is an emerging strategy for the rational design of vaccine candidates. We successfully applied structural vaccinology to design a fully... 
Proteins | Antigens | Immunization | Streptococcus | Vaccination | Crystallization | Antibodies | Mice | Epitopes | Crystal structure | Backbone protein | Isopeptide bonds | Homology modeling | isopeptide bonds | MULTIDISCIPLINARY SCIENCES | INVOLVEMENT | COLONIZATION | EXTENSION | IDENTIFICATION | homology modeling | PILI | STABILIZING ISOPEPTIDE | BONDS | backbone protein | SURFACE | BACILLI | Recombinant Fusion Proteins - immunology | Bacterial Vaccines - chemical synthesis | Streptococcus agalactiae - immunology | Protein Subunits - immunology | Recombinant Fusion Proteins - therapeutic use | Fimbriae, Bacterial - chemistry | Models, Molecular | Crystallography, X-Ray | Recombinant Fusion Proteins - chemical synthesis | Recombinant Fusion Proteins - chemistry | Streptococcal Infections - prevention & control | Animals | Bacterial Vaccines - immunology | Bacterial Vaccines - therapeutic use | Bacterial Vaccines - chemistry | Protein Engineering | Female | Fimbriae Proteins - chemistry | Protein Conformation | Fimbriae, Bacterial - immunology | Protein Subunits - chemistry | Streptococcal Infections - immunology | Fimbriae Proteins - immunology | Prevention | Physiological aspects | Genetic aspects | Streptococcal infections | Vaccines | Health aspects | Peptides | Streptococcus infections | Index Medicus | Infection | Pathogens | Pili | pilin | Lymphocytes B | Virulence | protective antigen | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2009, Volume 106, Issue 40, pp. 16967 - 16971
Cell-surface pili are important virulence factors that enable bacterial pathogens to adhere to specific host tissues and modulate host immune response.... 
Proteins | Molecules | Hydrogen bonds | Disulfides | Fimbriae proteins | Adhesive bonding | Chemical bonding | Polymers | Corynebacterium diphtheriae | Crystal structure | Polymerization | Pilin motif | Mass spectrometry | Bacterial pilus | polymerization | DOMAIN | pilin motif | COLLAGEN | PROTEIN | MULTIDISCIPLINARY SCIENCES | GRAM-POSITIVE BACTERIA | bacterial pilus | MSCRAMM | crystal structure | PILUS | SURFACE | HUG MODEL | mas spectromrtry | STAPHYLOCOCCUS-AUREUS | BINDING | Disulfides - metabolism | Threonine - chemistry | Fimbriae Proteins - metabolism | Bacterial Proteins - chemistry | Molecular Sequence Data | Corynebacterium diphtheriae - metabolism | Crystallography, X-Ray | Threonine - metabolism | Immunoglobulins - metabolism | Disulfides - chemistry | Corynebacterium diphtheriae - genetics | Mass Spectrometry | Lysine - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Bacterial Proteins - genetics | Models, Molecular | Protein Folding | Sequence Homology, Amino Acid | Immunoglobulins - chemistry | Fimbriae Proteins - genetics | Asparagine - metabolism | Bacterial Proteins - metabolism | Fimbriae Proteins - chemistry | Lysine - chemistry | Asparagine - chemistry | Corynebacteria | Evaluation | Crosslinked polymers | Bacterial proteins | Crystals | Physiological aspects | Properties | Observations | Structure | Methods | Pathogens | Disulfide bonds | Adhesins | Immune response | pilin | Calcium | Tertiary structure | Mass spectroscopy | Monomers | virulence factors | Pili | Protein structure | Index Medicus | Biological Sciences | mass spectrometry
Journal Article