X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (26) 26
humans (14) 14
biochemistry & molecular biology (12) 12
models, molecular (11) 11
article (10) 10
biophysics (8) 8
cell biology (8) 8
protein conformation (8) 8
proteins (8) 8
analysis (7) 7
molecular biology (7) 7
research (7) 7
amino acid sequence (6) 6
autism (6) 6
crystal-structure (6) 6
animals (5) 5
intervention (5) 5
mechanism (5) 5
molecular sequence data (5) 5
phosphorylation (5) 5
saccharomyces-cerevisiae (5) 5
aquaporins - chemistry (4) 4
calmodulin (4) 4
complex (4) 4
conserved sequence (4) 4
cryoelectron microscopy (4) 4
electron microscopy (4) 4
methods (4) 4
mutation (4) 4
physiological aspects (4) 4
protein structure, tertiary (4) 4
sequence homology, amino acid (4) 4
adult (3) 3
aquaporins - metabolism (3) 3
archaeal proteins - chemistry (3) 3
binding sites (3) 3
biology (3) 3
calmodulin - metabolism (3) 3
chemical properties (3) 3
child (3) 3
crystal structure (3) 3
dyskeratosis-congenita (3) 3
electron-microscopy (3) 3
eye proteins - chemistry (3) 3
eye proteins - metabolism (3) 3
family (3) 3
microscopy (3) 3
multidisciplinary sciences (3) 3
neurosciences (3) 3
nuclear proteins - chemistry (3) 3
permeability (3) 3
protein (3) 3
research article (3) 3
rna-binding proteins - chemistry (3) 3
saccharomyces cerevisiae proteins - chemistry (3) 3
sheep (3) 3
specificity (3) 3
structure (3) 3
studies (3) 3
t cells (3) 3
2-dimensional crystals (2) 2
adoptive t-cell therapy (2) 2
animal structures (2) 2
aquaporin (2) 2
aquaporins (2) 2
archaeal proteins - metabolism (2) 2
autism spectrum disorders (2) 2
bacteriorhodopsin (2) 2
behavior (2) 2
behavioral disciplines and activities (2) 2
bias (2) 2
calmodulin - chemistry (2) 2
cancer (2) 2
care and treatment (2) 2
child and school psychology (2) 2
child development disorders, pervasive - psychology (2) 2
child development disorders, pervasive - therapy (2) 2
child, preschool (2) 2
children (2) 2
children & youth (2) 2
cholera toxin (2) 2
crystallization (2) 2
crystallography - methods (2) 2
crystallography, x-ray - methods (2) 2
cyclic amp-dependent protein kinases - metabolism (2) 2
diagnosis (2) 2
dsm-5 (2) 2
electron cryomicroscopy (2) 2
environmental molecular sciences laboratory (2) 2
enzyme activation (2) 2
escherichia-coli (2) 2
families & family life (2) 2
female (2) 2
gap-junction channels (2) 2
genes (2) 2
gspd (2) 2
her2 (2) 2
image processing, computer-assisted (2) 2
immunology (2) 2
immunotherapy (2) 2
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Nature Structural & Molecular Biology, ISSN 1545-9993, 10/2010, Volume 17, Issue 10, pp. 1226 - 1232
Journal Article
NATURE STRUCTURAL & MOLECULAR BIOLOGY, ISSN 1545-9993, 09/2013, Volume 20, Issue 9, pp. 1085 - 1085
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 10/2010, Volume 17, Issue 10, pp. 1195 - 1201
Phosphorylation of the C-terminal domain (CTD) of RNA polymerase II controls the co-transcriptional assembly of RNA processing and transcription factors.... 
COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | CTD FUNCTION | SACCHAROMYCES-CEREVISIAE | PROCESSING FACTORS | PRE-MESSENGER-RNA | CELL BIOLOGY | YEAST | BIOPHYSICS | IICTD | GENE-EXPRESSION | CAPPING ENZYME | DIFFERENT PHOSPHORYLATED FORMS | Phosphorylation | Transcription Factors - chemistry | mRNA Cleavage and Polyadenylation Factors - metabolism | Humans | mRNA Cleavage and Polyadenylation Factors - chemistry | Molecular Sequence Data | RNA Polymerase II - metabolism | Conserved Sequence | Transcription, Genetic | RNA Polymerase II - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Peptide Fragments - metabolism | RNA-Binding Proteins - chemistry | Models, Molecular | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Protein Interaction Mapping | Sequence Homology, Amino Acid | Transcription Factors - metabolism | Point Mutation | Peptide Fragments - chemistry | Sequence Alignment | Saccharomyces cerevisiae Proteins - metabolism | Serine-Arginine Splicing Factors | Protein Conformation | Protein Processing, Post-Translational | Phosphoserine - chemistry | RNA-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Physiological aspects | Transcription factors | Research | RNA polymerases | Binding sites (Biochemistry) | Proteins | RNA polymerase | Mutation | Molecular structure | Molecular biology | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 12/2018, Volume 564, Issue 7736, pp. 372 - 377
Journal Article
eLife, ISSN 2050-084X, 05/2018, Volume 7
The transcription factor ASCIZ (ATMIN, ZNF822) has an unusually high number of recognition motifs for the product of its main target gene, the hub protein LC8... 
LC8 | DNA-BINDING | COMPLEX | DYNEIN LIGHT-CHAIN | BIOLOGY | BINDING PROTEIN CBP | MULTISITE PHOSPHORYLATION | ASCIZ | UNSTRUCTURED REGION | C-TERMINAL DOMAIN | DYNLL1 | Physiological aspects | Transcription factors | Index Medicus
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 03/2007, Volume 366, Issue 4, pp. 1209 - 1221
Journal Article