X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (7747) 7747
Book Review (1369) 1369
Publication (1357) 1357
Book Chapter (126) 126
Conference Proceeding (41) 41
Dissertation (8) 8
Book / eBook (4) 4
Magazine Article (2) 2
Newspaper Article (2) 2
Reference (2) 2
Data Set (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (6658) 6658
animals (4029) 4029
humans (3410) 3410
biochemistry & molecular biology (2523) 2523
proteins (1783) 1783
cell biology (1610) 1610
amino acid sequence (1293) 1293
mice (1180) 1180
molecular sequence data (1171) 1171
models, molecular (1161) 1161
potassium channels (1059) 1059
article (1050) 1050
biophysics (1042) 1042
neurosciences (1004) 1004
physiology (966) 966
protein binding (937) 937
mutation (917) 917
rats (915) 915
domain (893) 893
protein structure, tertiary (877) 877
multidisciplinary sciences (838) 838
analysis (808) 808
physiological aspects (795) 795
binding sites (789) 789
potassium channel (782) 782
research (760) 760
crystal-structure (751) 751
ion channels (744) 744
male (740) 740
expression (705) 705
protein conformation (669) 669
female (633) 633
activation (628) 628
signal transduction (619) 619
biochemistry (600) 600
cells (568) 568
gene expression (561) 561
patch-clamp techniques (543) 543
protein (537) 537
research article (526) 526
cell line (524) 524
potassium (517) 517
kinetics (508) 508
potassium channels, tandem pore domain - metabolism (496) 496
potassium channels - metabolism (487) 487
binding (460) 460
cells, cultured (459) 459
life sciences (447) 447
phosphorylation (440) 440
biology (437) 437
neurons (437) 437
cell membrane - metabolism (421) 421
k+ channel (419) 419
catalytic domain (409) 409
molecular biology (409) 409
potassium channels, tandem pore domain - genetics (409) 409
electrophysiology (408) 408
potassium channels - genetics (402) 402
pharmacology & pharmacy (399) 399
protein structure, secondary (395) 395
genetic aspects (387) 387
domains (385) 385
ion channel gating (382) 382
crystallography, x-ray (380) 380
medicine (373) 373
membrane proteins (368) 368
sequence homology, amino acid (363) 363
enzymes (359) 359
amino acids (358) 358
structure-activity relationship (355) 355
membranes (340) 340
science (340) 340
escherichia-coli (337) 337
xenopus laevis (337) 337
calcium (335) 335
calcium - metabolism (332) 332
ligands (331) 331
hek293 cells (330) 330
identification (312) 312
potassium channels - chemistry (312) 312
apoptosis (311) 311
mechanism (311) 311
models, biological (310) 310
transfection (310) 310
structure (306) 306
ion channel gating - physiology (301) 301
sequence alignment (301) 301
lipids (292) 292
potassium - metabolism (292) 292
hydrogen-ion concentration (291) 291
genes (287) 287
membrane potentials - physiology (283) 283
mutagenesis, site-directed (282) 282
channels (281) 281
mice, inbred c57bl (280) 280
biochemistry, general (278) 278
membrane proteins - metabolism (268) 268
potassium channels - physiology (267) 267
recombinant proteins - metabolism (262) 262
k+ channels (260) 260
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (7791) 7791
Chinese (14) 14
Japanese (6) 6
French (5) 5
German (3) 3
Portuguese (1) 1
Russian (1) 1
Turkish (1) 1
Ukrainian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Journal Article
Cellular and Molecular Life Sciences (CMLS), ISSN 1420-682X, 2015, Volume 17, Issue 19, p. 3677
Potassium channels ubiquitously exist in nearly all kingdoms of life and perform diverse but important functions. Since the first atomic structure of a... 
Biological Sciences | Naturvetenskap | Biokemi och molekylärbiologi | Biologiska vetenskaper | Conductivity | Biochemistry and Molecular Biology | Selectivity | Natural Sciences | Sensor domain | RCK | Gating
Journal Article
Science, ISSN 0036-8075, 05/2015, Volume 348, Issue 6235, pp. 707 - 710
The present palette of opsin-based optogenetic tools lacks a light-gated potassium (K+) channel desirable for silencing of excitable cells. Here, we describe... 
DOMAIN | LOV | MULTIDISCIPLINARY SCIENCES | CHLORIDE CHANNEL | ION CHANNELS | K+ CHANNEL | CHANNELRHODOPSIN | Potassium channels | Physiological aspects | Identification and classification | Protein-protein interactions | Signal transduction | Photobiology | Neurons | Potassium | Luminous intensity | Membranes | Construction | Modules | Zebrafish | Channels
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3411 - 3422
Journal Article
eLife, ISSN 2050-084X, 2014, Volume 3, pp. e03255 - e03255
Temperature-sensitive transient receptor potential (TRP) ion channels are members of the large tetrameric cation channels superfamily but are considered to be... 
gating | TRP channel | allosteric coupling | potassium channel | conformational changes | temperature sensing | Potassium - metabolism | Large-Conductance Calcium-Activated Potassium Channels - metabolism | Allosteric Regulation | Humans | Shaker Superfamily of Potassium Channels - metabolism | Large-Conductance Calcium-Activated Potassium Channels - chemistry | TRPV Cation Channels - metabolism | Shal Potassium Channels - genetics | Shaker Superfamily of Potassium Channels - chemistry | HEK293 Cells | Large-Conductance Calcium-Activated Potassium Channels - genetics | Shal Potassium Channels - chemistry | Ion Transport | Transgenes | Protein Structure, Tertiary | Shab Potassium Channels - genetics | Gene Expression | Shaker Superfamily of Potassium Channels - genetics | Shab Potassium Channels - chemistry | TRPV Cation Channels - chemistry | Hot Temperature | Membrane Potentials - physiology | TRPV Cation Channels - genetics | Patch-Clamp Techniques | Shab Potassium Channels - metabolism | Shal Potassium Channels - metabolism | Animals | Mice | Ion Channel Gating | GATING CHARGE | DEPENDENT POTASSIUM | ACTIVATION | TRP channels | CAPSAICIN RECEPTOR | TRPV1 ION-CHANNEL | potassium channels | BIOLOGY | CLOSED-STATE INACTIVATION | SHAKER | K+ CHANNEL | PORE DOMAIN | KV4.2 CHANNELS | Data analysis | Pain perception | Channel gating | Capsaicin receptors | Equilibrium | Thermal energy | Transient receptor potential proteins | Heat | Allosteric properties | Temperature effects | Nociceptors | Physiology | Potassium channels (voltage-gated) | Ion channels | Sensors | Potassium | Index Medicus
Journal Article
Journal of General Physiology, ISSN 0022-1295, 04/2018, Volume 150, Issue 4, pp. 625 - 635
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3569 - 3580
Changes in voltage-dependent potassium channels (Kv channels) associate to proliferation in many cell types, including transfected HEK293 cells. In this system... 
cell proliferation | C-TERMINUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | Kv1 | structure-function | SURFACE EXPRESSION | SUBUNITS | mutagenesis | IMMUNOMODULATION | electrophysiology | membrane potential | potassium channel | TARGETS | SMOOTH-MUSCLE-CELLS | SWITCH | tyrosine phosphorylation | ION CHANNELS | voltage-dependent conformation | K+ CHANNELS | LYMPHOCYTES | Kv1.5 Potassium Channel - chemistry | Phosphorylation | Cell Proliferation | Kv1.3 Potassium Channel - agonists | Humans | Kv1.3 Potassium Channel - genetics | Recombinant Fusion Proteins - metabolism | MAP Kinase Signaling System | Kv1.3 Potassium Channel - chemistry | MAP Kinase Kinase 1 - genetics | RNA Interference | HEK293 Cells | Kv1.5 Potassium Channel - genetics | Kv1.3 Potassium Channel - metabolism | Protein Interaction Domains and Motifs | MAP Kinase Kinase 2 - genetics | Peptide Fragments - genetics | Recombinant Proteins - metabolism | MAP Kinase Kinase 1 - antagonists & inhibitors | Peptide Fragments - metabolism | Recombinant Proteins - chemistry | MAP Kinase Kinase 1 - metabolism | MAP Kinase Kinase 2 - metabolism | Recombinant Fusion Proteins - chemistry | Kv1.5 Potassium Channel - agonists | Protein Transport | Point Mutation | Peptide Fragments - chemistry | Tyrosine - metabolism | MAP Kinase Kinase 2 - antagonists & inhibitors | Peptide Fragments - antagonists & inhibitors | Kv1.5 Potassium Channel - metabolism | Luminescent Proteins - genetics | Protein Conformation | Mutagenesis, Insertional | Protein Processing, Post-Translational | Amino Acid Substitution | Luminescent Proteins - metabolism | Index Medicus | Membrane Biology | Kv1.3
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 7097 - 7106
The structural similarity between defensins and scorpion neurotoxins suggests that they might have evolved from a common ancestor. However, there is no direct... 
VENOM | PORE REGION | bacteria | TOXIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | structure-function | KV1.3 CHANNEL | STRUCTURAL BASIS | FUNGAL DEFENSIN | defensin | INSECT DEFENSINS | neurotoxin | potassium channel | MESOBUTHUS-MARTENSII | PROTEOMIC ANALYSIS | K+ CHANNELS | Kv1.2 Potassium Channel - antagonists & inhibitors | Humans | Micrococcus luteus - growth & development | Potassium Channel Blockers - metabolism | Bacillus subtilis - growth & development | Defensins - pharmacology | Kv1.3 Potassium Channel - metabolism | Potassium Channel Blockers - pharmacology | Kv1.1 Potassium Channel - genetics | Amino Acid Sequence | Gene Expression | Methicillin-Resistant Staphylococcus aureus - drug effects | Models, Molecular | Recombinant Proteins - chemistry | Methicillin-Resistant Staphylococcus aureus - growth & development | Scorpion Venoms - chemistry | Kv1.2 Potassium Channel - metabolism | Neurotoxins - metabolism | Anti-Bacterial Agents - pharmacology | Mice | Scorpion Venoms - biosynthesis | Potassium Channel Blockers - chemistry | Defensins - metabolism | Defensins - genetics | Kv1.1 Potassium Channel - metabolism | Molecular Sequence Data | Neurotoxins - genetics | Structure-Activity Relationship | Defensins - chemistry | Kv1.3 Potassium Channel - genetics | Micrococcus luteus - drug effects | Scorpions - physiology | Anti-Bacterial Agents - chemistry | Protein Interaction Domains and Motifs | Recombinant Proteins - metabolism | Neurotoxins - chemistry | Protein Structure, Secondary | Kv1.1 Potassium Channel - antagonists & inhibitors | Anti-Bacterial Agents - metabolism | Scorpions - chemistry | Recombinant Proteins - genetics | Kv1.3 Potassium Channel - antagonists & inhibitors | Recombinant Proteins - pharmacology | Neurotoxins - pharmacology | Kv1.2 Potassium Channel - genetics | Sequence Alignment | Animals | Structural Homology, Protein | Staphylococcus aureus - drug effects | Staphylococcus aureus - growth & development | Bacillus subtilis - drug effects | Index Medicus | Cell Biology
Journal Article
Nature, ISSN 0028-0836, 08/2002, Volume 418, Issue 6900, pp. 880 - 884
Journal Article
American Journal of Physiology - Renal Physiology, ISSN 0363-6127, 2000, Volume 279, Issue 5, pp. F793 - F801
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2013, Volume 8, Issue 3, pp. e59265 - e59265
Journal Article
BBA - Biomembranes, ISSN 0005-2736, 2011, Volume 1808, Issue 8, pp. 2036 - 2044
Journal Article
Nature Neuroscience, ISSN 1097-6256, 07/2008, Volume 11, Issue 7, pp. 772 - 779
Journal Article