X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
humans (1036) 1036
animals (791) 791
biochemistry & molecular biology (681) 681
amino acid sequence (630) 630
proline-rich protein domains (580) 580
index medicus (579) 579
molecular sequence data (550) 550
proteins (399) 399
proline-rich proteins (367) 367
male (279) 279
cell biology (275) 275
mice (271) 271
protein binding (269) 269
peptides (259) 259
peptides - metabolism (248) 248
peptides - chemistry (246) 246
female (227) 227
proline (226) 226
rats (198) 198
peptides - genetics (194) 194
base sequence (184) 184
biophysics (174) 174
binding (169) 169
proline-rich peptides (169) 169
saliva (163) 163
analysis (162) 162
binding sites (159) 159
models, molecular (156) 156
identification (147) 147
proline-rich protein (147) 147
expression (146) 146
dentistry, oral surgery & medicine (145) 145
src homology domains (144) 144
adult (143) 143
proline-rich (143) 143
sequence homology, amino acid (132) 132
salivary proteins and peptides - metabolism (131) 131
protein (130) 130
protein conformation (127) 127
research (117) 117
ligands (114) 114
protein structure, tertiary (114) 114
immunology (109) 109
salivary proteins and peptides - chemistry (105) 105
signal transduction (104) 104
research article (103) 103
phosphorylation (102) 102
gene expression (101) 101
saliva - chemistry (101) 101
article (97) 97
electrophoresis, polyacrylamide gel (97) 97
sh3 domain (95) 95
salivary proteins and peptides - analysis (94) 94
peptides - analysis (92) 92
proline - chemistry (92) 92
salivary proteins and peptides - genetics (92) 92
peptides - pharmacology (91) 91
proteins - metabolism (91) 91
cell line (90) 90
plant sciences (87) 87
adsorption (86) 86
mass spectrometry (86) 86
cells, cultured (85) 85
middle aged (84) 84
sh3 domains (84) 84
cloning, molecular (83) 83
kinetics (83) 83
microbiology (82) 82
sequence alignment (82) 82
biochemical research methods (81) 81
neurosciences (81) 81
proline-rich region (80) 80
proteins - chemistry (80) 80
molecular weight (78) 78
crystal-structure (77) 77
gene (76) 76
genes (76) 76
genetics & heredity (76) 76
statherin (75) 75
cells (74) 74
circular dichroism (74) 74
life sciences (74) 74
proline - metabolism (74) 74
salivary proteins (73) 73
multidisciplinary sciences (72) 72
physiological aspects (71) 71
biochemistry (70) 70
protein structure, secondary (70) 70
parotid gland - metabolism (69) 69
proline-rich peptide (69) 69
pharmacology & pharmacy (68) 68
biochemistry, general (66) 66
food science & technology (66) 66
mutation (66) 66
proteomics (66) 66
bacteria (65) 65
biology (65) 65
peptides - isolation & purification (64) 64
cattle (63) 63
family (62) 62
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (1996) 1996
Japanese (11) 11
Russian (6) 6
Polish (3) 3
Chinese (1) 1
Czech (1) 1
French (1) 1
Korean (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Applied Microbiology and Biotechnology, ISSN 0175-7598, 7/2014, Volume 98, Issue 13, pp. 5807 - 5822
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 01/2013, Volume 8, Issue 1, pp. e53326 - e53326
Arasin 1 is a 37 amino acid long proline-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. In this work the active region of arasin 1 was... 
PIG INTESTINE | SPIDER CRAB | CECROPIN P1 | CHITIN-BINDING ACTIVITY | HYAS-ARANEUS | MEMBRANE | MULTIDISCIPLINARY SCIENCES | SEQUENCE | SECONDARY STRUCTURE | PR-39 | ANTIBACTERIAL PEPTIDE | Hemolysis - drug effects | Anti-Infective Agents - pharmacology | Escherichia coli - drug effects | Humans | Molecular Sequence Data | Peptide Fragments - pharmacology | Antifungal Agents - chemistry | Structure-Activity Relationship | Microbial Sensitivity Tests | Anti-Bacterial Agents - chemistry | Anti-Infective Agents - chemistry | Chitin - metabolism | Circular Dichroism | Antifungal Agents - pharmacology | Amino Acid Sequence | Microbial Viability - drug effects | Peptides - chemistry | Antimicrobial Cationic Peptides - chemistry | Antimicrobial Cationic Peptides - pharmacology | Peptides - pharmacology | Proline-Rich Protein Domains | Peptide Fragments - chemistry | Cell Membrane Permeability - drug effects | Anti-Bacterial Agents - pharmacology | Kinetics | Peptides | Proline | Membranes | Erythrocytes | Amino acids | Biochemistry | Structure-activity relationships | Drug resistance | Antiinfectives and antibacterials | Fragmentation | Proteins | Crustaceans | Red blood cells | Arginine | Cecropin | Bacteria | Life sciences | Gram-negative bacteria | Killing | Bacterial infections | Cell walls | Crabs | Blood cells | Antimicrobial agents | Chitin | Pharmacology | Mode of action | Antibiotics | Fishery sciences | Minimum inhibitory concentration | Index Medicus | VDP | Basic medical, dental and veterinary science disciplines: 710 | Medical microbiology: 715 | Medical molecular biology: 711 | Medisinske Fag: 700 | Medisinsk molekylærbiologi: 711 | Medisinsk mikrobiologi: 715 | Medical disciplines: 700 | Basale medisinske, odontologiske og veterinærmedisinske fag: 710
Journal Article
Journal Article
Critical Reviews in Biochemistry and Molecular Biology, ISSN 1040-9238, 05/2018, Volume 53, Issue 3, pp. 246 - 263
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 01/2016, Volume 44, Issue 5, pp. 2429 - 2438
Journal Article
Biochemistry, ISSN 0006-2960, 12/2002, Volume 41, Issue 48, pp. 14150 - 14157
The intracellular delivery of most peptides, proteins, and nucleotides to the cytoplasm and nucleus is impeded by the cell membrane. To allow simplified,... 
PIG INTESTINE | CELLS | NUCLEAR-LOCALIZATION SIGNALS | ANTIBACTERIAL PEPTIDES | BOVINE NEUTROPHILS | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | INTRACELLULAR DELIVERY | PENETRATION | PR-39 | Anti-Infective Agents - toxicity | Anti-Infective Agents - metabolism | Peptide Fragments - toxicity | Proline - metabolism | Anti-Infective Agents - pharmacology | Cations - metabolism | Escherichia coli - drug effects | Molecular Sequence Data | Monocytes - metabolism | Peptide Fragments - pharmacology | Peptides, Cyclic - pharmacology | Peptides, Cyclic - toxicity | Peptides, Cyclic - metabolism | Anti-Bacterial Agents | Repetitive Sequences, Amino Acid | Candida albicans - drug effects | Peptides - chemical synthesis | Peptides - metabolism | Peptides - toxicity | Antifungal Agents - pharmacology | Amino Acid Sequence | Cell Line | Cell Survival - drug effects | Peptide Fragments - metabolism | Anti-Infective Agents - chemical synthesis | Peptides - pharmacology | Protein Transport | Monocytes - drug effects | Peptide Fragments - chemical synthesis | Proline-Rich Protein Domains | Animals | Peptides, Cyclic - chemical synthesis | Cell Membrane Permeability - drug effects | Hydrophobic and Hydrophilic Interactions | Mice | Staphylococcus aureus - drug effects | Drug Delivery Systems - methods | Proteins | Peptides | Physiological aspects | Biochemistry | Cell membranes | Research | Nucleotides | Cytoplasm
Journal Article