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
More filters
TL;DR: ERD2, a gene required for retention, encodes a 26 kd integral membrane protein whose abundance determines the efficiency and capacity of the retention system and possible roles for ERD2 in the secretory pathway are discussed.
527 citations
TL;DR: This novel use of homologous recombination formally proves that chromosomal translocations contribute to malignancy and provides a general strategy to create fusion oncogenes for studying their role in tumorigenesis.
526 citations
TL;DR: It is suggested that the wild-type unc-86 and lin-4 genes act to modify latent reiterative cell lineages, which are revealed when the activity of one of these genes is eliminated.
526 citations
TL;DR: It is demonstrated in the rat optic system that a portion of α-synuclein is carried by the vesicle-moving fast component of axonal transport and that it binds to rat brain vesicles through its amino-terminal repeat region and it is proposed that mutant α- synuclein may accumulate, leading to assembly into Lewy body filaments.
526 citations
TL;DR: Crystal structures of the ribosome bound to elongation factors provide insights into translocation and decoding, and a series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the guanosine triphosphatase center of EF- Tu.
Abstract: The ribosome selects a correct transfer RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA. Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. The signaling pathway that leads to GTP hydrolysis upon codon recognition is critical to accurate decoding. Here we present the crystal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolution. The structure reveals details of the tRNA distortion that allows aminoacyl-tRNA to interact simultaneously with the decoding center of the 30S subunit and EF-Tu at the factor binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the guanosine triphosphatase center of EF-Tu.
525 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 |