X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (5230) 5230
Publication (709) 709
Book Chapter (48) 48
Book Review (38) 38
Conference Proceeding (21) 21
Newsletter (18) 18
Book / eBook (5) 5
Magazine Article (1) 1
Reference (1) 1
Streaming Video (1) 1
Web Resource (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
humans (3168) 3168
animals (2356) 2356
index medicus (1976) 1976
biochemistry & molecular biology (1309) 1309
neurosciences (1241) 1241
alzheimers-disease (1220) 1220
alzheimer's disease (1173) 1173
amyloid - ultrastructure (1130) 1130
mice (1038) 1038
male (1020) 1020
microscopy, electron (995) 995
amyloid - chemistry (896) 896
amyloid - metabolism (884) 884
female (866) 866
alzheimer disease - pathology (823) 823
amyloid beta-peptides - metabolism (810) 810
amyloid (771) 771
alzheimer disease - metabolism (697) 697
rats (649) 649
proteins (647) 647
protein (631) 631
aged (607) 607
amyloid beta-peptides - ultrastructure (599) 599
pathology (585) 585
amyloid beta-peptides - chemistry (582) 582
middle aged (557) 557
amino acid sequence (554) 554
aggregation (533) 533
immunohistochemistry (518) 518
in-vitro (504) 504
amyloid precursor protein (496) 496
microscopy, electron, transmission (495) 495
molecular sequence data (483) 483
brain (473) 473
protein structure, secondary (463) 463
peptide fragments - chemistry (449) 449
protein conformation (445) 445
models, molecular (441) 441
cell biology (437) 437
biophysics (431) 431
brain - pathology (429) 429
mice, transgenic (410) 410
research (409) 409
neurons - ultrastructure (404) 404
disease models, animal (402) 402
disease (399) 399
kinetics (394) 394
peptide fragments - metabolism (384) 384
cells, cultured (374) 374
peptides (372) 372
circular dichroism (366) 366
adult (350) 350
amyloidosis - pathology (349) 349
protein folding (349) 349
peptide fragments - ultrastructure (346) 346
a-beta (344) 344
protein binding (337) 337
analysis (336) 336
article (336) 336
multidisciplinary sciences (336) 336
fibrils (332) 332
neurons - metabolism (329) 329
amyloid - analysis (327) 327
clinical neurology (323) 323
brain - metabolism (318) 318
peptide (318) 318
transgenic mice (317) 317
amyloid beta-protein (316) 316
amyloid beta-protein precursor - metabolism (311) 311
fibril formation (305) 305
amyloid fibrils (304) 304
mutation (301) 301
brain - ultrastructure (296) 296
microscopy, atomic force (294) 294
amyloidosis (292) 292
amyloid beta-protein precursor - genetics (286) 286
alzheimers disease (283) 283
neurons (283) 283
oligomers (279) 279
aged, 80 and over (278) 278
mice, inbred c57bl (271) 271
research article (266) 266
neurodegenerative diseases (264) 264
electron microscopy (261) 261
oxidative stress (259) 259
alzheimer disease - genetics (254) 254
neurons - drug effects (250) 250
alpha-synuclein (240) 240
time factors (232) 232
physiological aspects (229) 229
neurodegeneration (228) 228
amyloidosis - metabolism (227) 227
hydrogen-ion concentration (225) 225
neurons - pathology (220) 220
amyloid-beta (216) 216
precursor protein (215) 215
apoptosis (214) 214
cells (208) 208
microscopy (208) 208
mechanism (204) 204
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (5135) 5135
Japanese (31) 31
German (28) 28
Russian (22) 22
French (19) 19
Chinese (14) 14
Hungarian (7) 7
Spanish (6) 6
Dutch (3) 3
Swedish (2) 2
Bulgarian (1) 1
Czech (1) 1
Danish (1) 1
Polish (1) 1
Portuguese (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2009, Volume 106, Issue 34, pp. 14339 - 14344
We demonstrate that accurate values of mass-per-length (MPL), which serve as strong constraints on molecular structure, can be determined for amyloid fibrils... 
Histograms | Yeasts | Electron beams | Transmission electron microscopy | Prions | Elastic scattering | Electron microscopes | Amyloids | Solar fibrils | Electrons | Molecular structure | Alzheimer's disease | Solid state NMR | PROTEIN | SOLID-STATE NMR | MULTIDISCIPLINARY SCIENCES | NUCLEAR-MAGNETIC-RESONANCE | SACCHAROMYCES-CEREVISIAE | molecular structure | YEAST | IN-VITRO | WEIGHT DETERMINATION | HET-S PRION | BETA-SHEET STRUCTURE | solid state NMR | prions | PIN+ PRION | Fungal Proteins - chemistry | Peptide Fragments - ultrastructure | Saccharomyces cerevisiae Proteins - ultrastructure | Green Fluorescent Proteins - metabolism | Prions - ultrastructure | Molecular Weight | Peptide Termination Factors - genetics | Microscopy, Electron, Transmission - methods | Humans | Green Fluorescent Proteins - genetics | Green Fluorescent Proteins - ultrastructure | Prions - chemistry | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Fungal Proteins - ultrastructure | Peptide Fragments - chemistry | Peptide Termination Factors - ultrastructure | Recombinant Fusion Proteins - ultrastructure | Amyloid beta-Peptides - ultrastructure | Recombinant Fusion Proteins - genetics | Peptide Termination Factors - chemistry | Amyloid beta-Peptides - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Measurement | Physiological aspects | Glycoproteins | Research | Electron microscopy | Biological Sciences
Journal Article
ACTA NEUROPATHOLOGICA, ISSN 0001-6322, 01/2012, Volume 123, Issue 1, pp. 53 - 70
Journal Article
Diabetes, Obesity and Metabolism, ISSN 1462-8902, 09/2018, Volume 20, Issue S2, pp. 137 - 144
While a number of structural and cellular abnormalities occur in the islet of Langerhans in diabetes, and in particular in type 2 diabetes, the focus has been... 
somatostatin producing δ‐cells | electron microscopy insulin producing β‐cells | type 2 diabetes mellitus | IAPP | pancreatic islet of Langerhans structure | ultrastructure | amyloid deposition | glucagon producing α‐cells | somatostatin producing δ-cells | electron microscopy insulin producing β-cells | glucagon producing α-cells | AMYLOID POLYPEPTIDE | BETA-CELL APOPTOSIS | glucagon producing alpha-cells | somatostatin producing delta-cells | DEDIFFERENTIATION | INSULIN | EUROPEAN SUBJECTS | SOMATOSTATIN | MASS | ENDOCRINOLOGY & METABOLISM | MICE | SECRETORY GRANULES | electron microscopy insulin producing beta-cells | GLUCAGON | Glucagon-Secreting Cells - ultrastructure | Humans | Rats | Haplorhini | Papio | Animals | Amyloid - metabolism | Islets of Langerhans - cytology | Models, Animal | Islets of Langerhans - ultrastructure | Mice | Diabetes Mellitus, Type 2 - pathology | Somatostatin-Secreting Cells - ultrastructure | Blood Glucose - metabolism | Pancreatic Polypeptide-Secreting Cells - ultrastructure | Type 2 diabetes | Insulin resistance | Glucose | Glucagon | Dextrose | Secretion | Diabetes mellitus | Insulin | Glucose tolerance | Hyperglycemia | Ultrastructure | Somatostatin | Diabetes | Islets of Langerhans | Pancreas | Diabetes mellitus (non-insulin dependent) | Structure-function relationships
Journal Article
Journal Article
Journal of Comparative Neurology, ISSN 0021-9967, 07/2008, Volume 509, Issue 3, pp. 259 - 270
Journal Article
Oncotarget, ISSN 1949-2553, 2017, Volume 8, Issue 25, pp. 40006 - 40018
Journal Article
Journal of Alzheimer's Disease, ISSN 1387-2877, 2016, Volume 53, Issue 3, pp. 787 - 800
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2010, Volume 395, Issue 3, pp. 627 - 642
Journal Article