X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (3310) 3310
Publication (593) 593
Book Chapter (32) 32
Book Review (26) 26
Conference Proceeding (15) 15
Dissertation (5) 5
Data Set (3) 3
Government Document (2) 2
Book / eBook (1) 1
Magazine Article (1) 1
Paper (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
animals (2608) 2608
mice (1460) 1460
humans (1369) 1369
prpsc proteins - metabolism (1316) 1316
index medicus (1042) 1042
scrapie (1001) 1001
creutzfeldt-jakob-disease (814) 814
prion protein (776) 776
nervous system diseases (775) 775
prions (768) 768
animal diseases (726) 726
biochemistry & molecular biology (677) 677
sheep (666) 666
prpsc proteins - chemistry (629) 629
prpsc proteins - genetics (620) 620
brain - metabolism (611) 611
prions - metabolism (562) 562
brain - pathology (558) 558
cricetinae (523) 523
cattle (520) 520
prp (514) 514
prion (512) 512
creutzfeldt-jakob disease (511) 511
prions - genetics (510) 510
prpsc (490) 490
female (485) 485
prion diseases - metabolism (459) 459
bovine spongiform encephalopathy (445) 445
protein (442) 442
proteins (438) 438
scrapie - metabolism (415) 415
prion diseases (402) 402
virology (399) 399
neurosciences (398) 398
prpc proteins - metabolism (396) 396
brain (391) 391
prpsc proteins (390) 390
bse (389) 389
prions - chemistry (353) 353
immunohistochemistry (348) 348
prpsc proteins - analysis (347) 347
male (343) 343
protein folding (343) 343
mice, transgenic (337) 337
protein conformation (322) 322
blotting, western (320) 320
pathology (305) 305
scrapie - pathology (296) 296
disease (290) 290
transmission (286) 286
prpc proteins - chemistry (285) 285
transgenic mice (277) 277
research (272) 272
prpsc proteins - pathogenicity (271) 271
research article (269) 269
prion diseases - pathology (263) 263
molecular sequence data (258) 258
veterinary sciences (258) 258
multidisciplinary sciences (252) 252
mice, inbred c57bl (244) 244
amino acid sequence (239) 239
cell biology (237) 237
biology (236) 236
mutation (229) 229
agent (224) 224
prpc proteins - genetics (224) 224
disease models, animal (219) 219
transmissible spongiform encephalopathy (216) 216
clinical neurology (214) 214
prion diseases - genetics (214) 214
brain chemistry (213) 213
creutzfeldt-jakob syndrome - pathology (213) 213
prpsc proteins - immunology (212) 212
infectivity (211) 211
infectious diseases (208) 208
mesocricetus (206) 206
natural scrapie (206) 206
conversion (205) 205
genotype (204) 204
scrapie - genetics (203) 203
spongiform encephalopathy (200) 200
prpsc proteins - isolation & purification (198) 198
time factors (197) 197
creutzfeldt-jakob syndrome - metabolism (195) 195
biotechnology & applied microbiology (191) 191
cell line (190) 190
creutzfeldt-jakob syndrome - genetics (188) 188
diagnosis (187) 187
analysis (183) 183
prion diseases - transmission (180) 180
middle aged (177) 177
species specificity (177) 177
biophysics (172) 172
scrapie - transmission (171) 171
pathogenesis (170) 170
prions - pathogenicity (169) 169
medicine (166) 166
neurodegeneration (163) 163
microbiology (162) 162
identification (160) 160
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (3225) 3225
Japanese (28) 28
Chinese (18) 18
French (15) 15
German (10) 10
Spanish (9) 9
Russian (6) 6
Czech (4) 4
Italian (2) 2
Korean (2) 2
Polish (2) 2
Portuguese (2) 2
Dutch (1) 1
Icelandic (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


PLoS ONE, ISSN 1932-6203, 09/2017, Volume 12, Issue 9, p. e0180905
Proteins associated with neurodegenerative diseases are highly pleiomorphic and may adopt an all-a-helical fold in one environment, assemble into... 
ALPHA-SYNUCLEIN OLIGOMERS | ATOMIC-FORCE MICROSCOPY | SOLID-STATE NMR | SODIUM DODECYL-SULFATE | MULTIDISCIPLINARY SCIENCES | PARTIALLY FOLDED STRUCTURE | PAIRED HELICAL FILAMENTS | AMYLOID-BETA-PROTEIN | C-TERMINAL THREONINE | INDUCED CONFORMATIONAL-CHANGES | HUMAN PRION PROTEIN | Protein Aggregates | Protein Structure, Secondary | Humans | Protein Multimerization | Models, Molecular | tau Proteins - metabolism | PrPSc Proteins - chemistry | Protein Folding | tau Proteins - chemistry | PrPSc Proteins - genetics | alpha-Synuclein - chemistry | PrPSc Proteins - metabolism | Animals | tau Proteins - genetics | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - metabolism | Protein Domains | alpha-Synuclein - genetics | Amyloid beta-Peptides - chemistry | Protein Stability | alpha-Synuclein - metabolism | Electrons | Hydrogen-Ion Concentration | Protein folding | Physiological aspects | Nervous system | Development and progression | Degeneration | Genetic aspects | Research | Coils | Amyloidogenesis | Backbone | Rate constants | Agglomeration | Synuclein | pH effects | Neuromodulation | Modulators | Proteins | Oligomers | Fibrillogenesis | Pathways | Chirality | Chemical bonds | Catalysis | Prion protein | Dimerization | Folding | Linkages | Polypeptides | Incubation | Neurodegenerative diseases | Tertiary structure | Polymerization | Shielding | Secondary structure | Density distribution | Neurological diseases | Chemistry | Tensors | Propagation (polymerization) | Aggregates | Tau protein | Prions | Morphology | β-Amyloid | Dimers | Mutation | Protein structure
Journal Article
Nature, ISSN 0028-0836, 05/2012, Volume 485, Issue 7399, pp. 507 - 511
The mechanisms leading to neuronal death in neurodegenerative disease are poorly understood. Many of these disorders, including Alzheimer's, Parkinson's and... 
UNFOLDED PROTEIN RESPONSE | TOXICITY IN-VIVO | ALZHEIMERS-DISEASE | ER STRESS | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | MICE | ENDOPLASMIC-RETICULUM STRESS | DYSFUNCTION | PRP | PROTEOSTASIS | Neurons - pathology | Neuroprotective Agents | Phosphorylation | Prions - genetics | Eukaryotic Initiation Factor-2 - chemistry | Neurodegenerative Diseases - etiology | PrPSc Proteins - analysis | Synapses - pathology | Thiourea - pharmacology | Phosphoproteins - metabolism | Repressor Proteins - analysis | PrPSc Proteins - metabolism | Synapses - metabolism | Phosphoproteins - analysis | Protein Folding - drug effects | Protein Phosphatase 1 - genetics | Eukaryotic Initiation Factor-2 - metabolism | Synaptic Transmission - drug effects | Cell Death - drug effects | PrPSc Proteins - toxicity | Neurons - drug effects | Repressor Proteins - metabolism | Prions - metabolism | Synapses - drug effects | Repressor Proteins - chemistry | Neurodegenerative Diseases - pathology | Mice, Inbred C57BL | Kaplan-Meier Estimate | Hippocampus - pathology | Prion Diseases - pathology | Neurodegenerative Diseases - metabolism | Hippocampus - cytology | Cinnamates - pharmacology | Eukaryotic Initiation Factor-2 - analysis | Hippocampus - metabolism | Protein Phosphatase 1 - metabolism | Animals | Prions - biosynthesis | Protein Biosynthesis - drug effects | Mice | Unfolded Protein Response - physiology | Thiourea - analogs & derivatives
Journal Article
Journal Article
Journal Article