Institution
Laboratory of Molecular Biology
Facility•Cambridge, Cambridgeshire, United Kingdom•
About: Laboratory of Molecular Biology is a facility organization based out in Cambridge, Cambridgeshire, United Kingdom. It is known for research contribution in the topics: Gene & RNA. The organization has 19395 authors who have published 24236 publications receiving 2101480 citations.
Topics: Gene, RNA, DNA, Population, Receptor
Papers published on a yearly basis
Papers
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TL;DR: The recently determined atomic structure of the 30S ribosomal subunit is used to determine the structures of its complexes with the antibiotics tetracycline, pactamycin, and hygromycin B to suggest a mechanism for its effects on ribosome function.
848 citations
TL;DR: The structure of the contacts between unlike subunits suggests that the tetramer, rather than the αβ dimer, is the functional unit of haemoglobin.
Abstract: The secondary structure of the haemoglobin chains is similar to that of myoglobin, but some of the helical segments are more irregular and some parts of the non-helical segments have different conformations. The structure of the contacts between unlike subunits suggests that the tetramer, rather than the αβ dimer, is the functional unit of haemoglobin.
847 citations
TL;DR: It is concluded that the binding of Axin to LRP-5 is an important part of the Wnt signal transduction pathway, and the L RP-5 sequences involved in interactions with Axin are required for LEF-1 activation.
846 citations
TL;DR: It is demonstrated that native A68 does not bind to microtubules (MTs), yet dephosphorylated A68 regains the ability to bind to MTs, and phosphorylation of Ser396 may destabilize MTs in AD, resulting in the degeneration of affected cells.
846 citations
TL;DR: The crystal structure of the RNA-binding domain of the small nuclear ribonucleoprotein U1A bound to a 21-nucleotide RNA hairpin has been determined and reveals the stereochemical basis for sequence-specific RNA recognition by the RNP domain.
Abstract: The crystal structure of the RNA-binding domain of the small nuclear ribonucleoprotein U1A bound to a 21-nucleotide RNA hairpin has been determined at 1.92 A resolution. The ten-nucleotide RNA loop binds to the surface of the β-sheet as an open structure, and the AUUGCAC sequence of the loop interacts extensively with the conserved RNP1 and RNP2 motifs and the C-terminal extension of the RNP domain. These interactions include stacking of RNA bases with aromatic side chains of proteins and many direct and water-mediated hydrogen bonds. The structure reveals the stereochemical basis for sequence-specific RNA recognition by the RNP domain.
845 citations
Authors
Showing all 19431 results
| Name | H-index | Papers | Citations |
|---|---|---|---|
| Robert J. Lefkowitz | 214 | 860 | 147995 |
| Ronald M. Evans | 199 | 708 | 166722 |
| Tony Hunter | 175 | 593 | 124726 |
| Marc G. Caron | 173 | 674 | 99802 |
| Mark Gerstein | 168 | 751 | 149578 |
| Timothy A. Springer | 167 | 669 | 122421 |
| Harvey F. Lodish | 165 | 782 | 101124 |
| Ira Pastan | 160 | 1286 | 110069 |
| Bruce N. Ames | 158 | 506 | 129010 |
| Philip Cohen | 154 | 555 | 110856 |
| Gerald M. Rubin | 152 | 382 | 115248 |
| Ashok Kumar | 151 | 5654 | 164086 |
| Kim Nasmyth | 142 | 294 | 59231 |
| Kenneth M. Yamada | 139 | 446 | 72136 |
| Harold E. Varmus | 137 | 496 | 76320 |