X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (1724) 1724
furin (1305) 1305
animals (1233) 1233
humans (1106) 1106
biochemistry & molecular biology (683) 683
amino acid sequence (544) 544
molecular sequence data (526) 526
mice (521) 521
furin - metabolism (518) 518
subtilisins - metabolism (448) 448
cell line (404) 404
proprotein convertases (359) 359
expression (318) 318
protein processing, post-translational (305) 305
cell biology (299) 299
proteins (288) 288
rats (267) 267
activation (255) 255
protein precursors - metabolism (246) 246
transfection (234) 234
cleavage (231) 231
cells (218) 218
subtilisins - genetics (206) 206
female (192) 192
cricetinae (188) 188
base sequence (183) 183
furin - genetics (183) 183
mutation (182) 182
male (181) 181
proprotein convertase (178) 178
cells, cultured (170) 170
identification (170) 170
viruses (169) 169
recombinant proteins - metabolism (163) 163
serine endopeptidases - metabolism (161) 161
protein structure, tertiary (160) 160
binding sites (155) 155
substrate specificity (155) 155
virology (152) 152
cho cells (146) 146
research (145) 145
protein (141) 141
cell line, tumor (138) 138
gene expression (135) 135
blotting, western (134) 134
kinetics (134) 134
article (133) 133
multidisciplinary sciences (130) 130
proprotein convertases - metabolism (126) 126
gene (122) 122
tumor cells, cultured (122) 122
biophysics (121) 121
proteases (115) 115
protein binding (114) 114
peptides (112) 112
proteolysis (112) 112
enzymes (107) 107
research article (106) 106
endocrinology & metabolism (105) 105
localization (105) 105
gene-expression (104) 104
precursor (104) 104
analysis (102) 102
mutagenesis, site-directed (101) 101
animal structures (100) 100
recombinant fusion proteins - metabolism (100) 100
cercopithecus aethiops (98) 98
physiological aspects (97) 97
trans-golgi network (96) 96
glycosylation (94) 94
furin - antagonists & inhibitors (92) 92
protein precursors - genetics (92) 92
signal transduction (92) 92
receptor (91) 91
endoprotease (90) 90
sequence homology, amino acid (90) 90
rna, messenger - metabolism (87) 87
abridged index medicus (86) 86
furin - chemistry (86) 86
in-vitro (86) 86
serine endopeptidases - genetics (86) 86
models, molecular (85) 85
oncology (85) 85
sequence (84) 84
hydrogen-ion concentration (83) 83
secretory pathway (83) 83
cell membrane - metabolism (82) 82
enzyme activation (82) 82
immunohistochemistry (82) 82
inhibition (82) 82
cell-surface (81) 81
biochemistry (80) 80
prohormone convertases (79) 79
cloning, molecular (78) 78
cos cells (78) 78
embryonic structures (78) 78
in-vivo (78) 78
membrane proteins - metabolism (78) 78
golgi apparatus - metabolism (77) 77
hek293 cells (74) 74
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (1788) 1788
Chinese (5) 5
Japanese (2) 2
Russian (2) 2
French (1) 1
German (1) 1
Polish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Traffic, ISSN 1398-9219, 07/2009, Volume 10, Issue 7, pp. 883 - 893
The phosphoinositide 5‐kinase (PIKfyve) is a critical enzyme for the synthesis of PtdIns(3,5) P 2 , that has been implicated in various trafficking events... 
PIKfyve | EGF receptor | endocytosis | autophagy | phosphoinositide | Endocytosis | Phosphoinositide | Autophagy | VAC14 | 3-PHOSPHATE | PROTEIN | SACCHAROMYCES-CEREVISIAE | CELL BIOLOGY | PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY | TRANSPORT | RETROMER | RECEPTOR TRAFFICKING | 3,5-BISPHOSPHATE | RNA, Small Interfering - genetics | Membrane Glycoproteins - metabolism | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Autophagy - physiology | Phosphatidylinositol 3-Kinases - metabolism | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Receptor, Epidermal Growth Factor - metabolism | trans-Golgi Network - metabolism | Molecular Structure | Androstadienes - metabolism | Furin - metabolism | Receptor, IGF Type 2 | Shiga Toxin 2 - metabolism | Receptor Protein-Tyrosine Kinases - metabolism | Phosphatidylinositol 3-Kinases - genetics | CD8 Antigens - metabolism | Animals | Recombinant Fusion Proteins - genetics | Vacuoles - metabolism | HeLa Cells | Protein Kinase Inhibitors - metabolism | RNA, Small Interfering - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Phosphatidylinositol | Enzymes | Epidermal growth factor | Oncology, Experimental | Physiological aspects | Research | Cancer | Index Medicus | Original
Journal Article
Journal of Cerebral Blood Flow & Metabolism, ISSN 0271-678X, 04/2007, Volume 27, Issue 4, pp. 697 - 709
Matrix metalloproteinases (MMPs) disrupt the blood—brain barrier (BBB) during reperfusion. Occludin and claudins are recently described tight junction proteins... 
Blood-brain barrier opening | Claudin-5 | Matrix metalloproteinases | Rat | Middle cerebral artery occlusion | Occludin | ACTIVATION | rat | PERMEABILITY | REPERFUSION | PROTEOLYSIS | BLOOD-BRAIN-BARRIER | NEUROSCIENCES | occludin | STRANDS | TYROSINE PHOSPHATASE INHIBITION | ENDOTHELIAL-CELLS | ENDOCRINOLOGY & METABOLISM | MATRIX-METALLOPROTEINASE-9 | HEMATOLOGY | matrix metalloproteinases | blood-brain barrier opening | middle cerebral artery occlusion | claudin-5 | Enzyme Activators - pharmacology | Immunohistochemistry | Cerebral Veins - metabolism | Sucrose | Brain Ischemia - metabolism | Male | Cerebral Arteries - drug effects | Protease Inhibitors - pharmacology | RNA, Messenger - biosynthesis | Gelatinases - metabolism | Membrane Proteins - metabolism | Matrix Metalloproteinases - biosynthesis | Tight Junctions - drug effects | Rats, Inbred SHR | Tight Junctions - metabolism | Astrocytes - drug effects | Furin - biosynthesis | Cerebral Veins - drug effects | Reperfusion Injury - pathology | Endothelial Cells - metabolism | Matrix Metalloproteinase 2 - metabolism | Rats | Infarction, Middle Cerebral Artery - pathology | Reverse Transcriptase Polymerase Chain Reaction | Blood-Brain Barrier - drug effects | Blotting, Western | Nerve Tissue Proteins - metabolism | Animals | Evans Blue | Cerebral Arteries - metabolism | Brain Ischemia - drug therapy | Matrix Metalloproteinase Inhibitors | Matrix Metalloproteinases - physiology | Astrocytes - metabolism | Endothelial Cells - drug effects | Index Medicus
Journal Article
Journal Article
Journal of Clinical Investigation, ISSN 0021-9738, 01/2017, Volume 127, Issue 1, pp. 293 - 305
Prader-Willi syndrome (PWS) is caused by a loss of paternally expressed genes in an imprinted region of chromosome 15q. Among the canonical PWS phenotypes are... 
MEDICINE, RESEARCH & EXPERIMENTAL | PLASMA GHRELIN | BODY-WEIGHT | HORMONE-RELEASING-HORMONE | HYPERPHAGIA | FOOD-INTAKE | PROPROTEIN CONVERTASE-1 | ONSET OBESITY | KNOCKOUT MICE | CIRCULATING GHRELIN LEVELS | CHILDREN | Diabetes Mellitus - pathology | Neurons - pathology | Proinsulin - metabolism | Diabetes Mellitus - genetics | Humans | Male | Obesity - genetics | RNA, Small Nucleolar - metabolism | Basic Helix-Loop-Helix Transcription Factors - metabolism | Hypogonadism - metabolism | Prader-Willi Syndrome - genetics | Female | Neurons - metabolism | Induced Pluripotent Stem Cells - metabolism | Hypogonadism - pathology | Induced Pluripotent Stem Cells - pathology | Basic Helix-Loop-Helix Transcription Factors - genetics | Protein Precursors - genetics | Diabetes Mellitus - metabolism | Proinsulin - genetics | Prader-Willi Syndrome - metabolism | Growth Hormone-Releasing Hormone - genetics | Hyperphagia - metabolism | Proprotein Convertase 1 - deficiency | RNA, Small Nucleolar - genetics | Mice, Knockout | Obesity - metabolism | Obesity - pathology | Protein Precursors - metabolism | Hyperphagia - genetics | Hyperphagia - pathology | Hypogonadism - genetics | Growth Hormone-Releasing Hormone - metabolism | Animals | Prader-Willi Syndrome - pathology | Prader-Willi syndrome | Gene expression | Neurons | Analysis | Risk factors | Proteins | Enzymes | Plasma | Obesity | Rodents | Fibroblasts | Patients | Binding sites | Index Medicus | Abridged Index Medicus
Journal Article
Biochemistry, ISSN 0006-2960, 10/2013, Volume 52, Issue 43, pp. 7551 - 7558
Neuropilin-1 (Nrp1), an essential type I transmembrane receptor, binds two secreted ligand families, vascular endothelial growth factor (VEGF) and class III... 
LUNG-CANCER | NEUROPILIN-1 | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SECRETED SEMAPHORINS | TUMOR ANGIOGENESIS | VEGF-A | RECEPTORS | BINDING | CELL | ENDOTHELIAL GROWTH-FACTOR | Neuropilin-1 - genetics | Phosphorylation | Human Umbilical Vein Endothelial Cells - metabolism | Neuropilin-1 - metabolism | Humans | Vascular Endothelial Growth Factor A - metabolism | Recombinant Fusion Proteins - metabolism | Vascular Endothelial Growth Factor Receptor-2 - genetics | Vascular Endothelial Growth Factor Receptor-2 - antagonists & inhibitors | Nerve Tissue Proteins - chemistry | Proteolysis | Vascular Endothelial Growth Factor Receptor-2 - agonists | Membrane Proteins - metabolism | Peptide Fragments - genetics | Furin - metabolism | Binding, Competitive | Recombinant Proteins - metabolism | Angiogenesis Inhibitors - genetics | Peptide Fragments - metabolism | Neuropilin-1 - biosynthesis | Signal Transduction | Membrane Proteins - genetics | Cells, Cultured | Recombinant Proteins - chemistry | Vascular Endothelial Growth Factor Receptor-2 - metabolism | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Peptide Fragments - chemical synthesis | Peptide Fragments - chemistry | Angiogenesis Inhibitors - metabolism | Animals | Membrane Proteins - chemistry | Endothelium, Vascular - metabolism | Mutant Proteins - chemistry | Protein Processing, Post-Translational | Sus scrofa | Neovascularization, Physiologic | Angiogenesis Inhibitors - chemistry | Physiological aspects | Semaphorins | Research | Index Medicus
Journal Article
Blood, ISSN 0006-4971, 01/2008, Volume 111, Issue 2, pp. 924 - 931
Journal Article
The EMBO Journal, ISSN 0261-4189, 10/2008, Volume 27, Issue 19, pp. 2580 - 2591
The glycosylphosphatidylinositol (GPI)‐anchored proteoglycan Cripto binds Nodal and its type I receptor Alk4 to activate Smad2,3 transcription factors, but a... 
EGF‐CFC | TGFβ | trafficking | unconventional exocytosis | EGF-CFC | Trafficking | Unconventional exocytosis | TGF-BETA | VERTEBRATE DEVELOPMENT | ENDOCYTIC PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-SURFACE | PLASMA-MEMBRANE | CELL BIOLOGY | ENDOSOMES | PROPROTEIN CONVERTASES | EARLY MOUSE EMBRYO | SIGNALING PATHWAY | TGF beta | GPI-ANCHORED PROTEINS | Membrane Glycoproteins - metabolism | Membrane Microdomains - metabolism | Humans | Cercopithecus aethiops | Molecular Sequence Data | Protein Transport - physiology | Neoplasm Proteins - metabolism | Exocytosis - physiology | Proprotein Convertases - genetics | Endosomes - metabolism | trans-Golgi Network - metabolism | Furin - genetics | Serine Endopeptidases - genetics | Membrane Proteins - metabolism | Neoplasm Proteins - genetics | Furin - metabolism | Amino Acid Sequence | Epidermal Growth Factor - genetics | Membrane Proteins - genetics | Proprotein Convertases - metabolism | Epidermal Growth Factor - metabolism | Membrane Glycoproteins - genetics | Protein Precursors - metabolism | Sequence Alignment | Animals | Transforming Growth Factor beta - genetics | Glycosylphosphatidylinositols - metabolism | Signal Transduction - physiology | Mice | Serine Endopeptidases - metabolism | COS Cells | Transforming Growth Factor beta - metabolism | Nodal Protein | Signal transduction | Membranes | Cellular biology | Molecular biology | Binding sites | Index Medicus
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2008, Volume 283, Issue 4, pp. 2373 - 2384
Journal Article