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, Transcription (biology)
Papers published on a yearly basis
Papers
More filters
TL;DR: The main target of Gctf is to maximize the cross-correlation of a simulated CTF with the logarithmic amplitude spectra of observed micrographs after background subtraction to improve CTF parameters of all particles for subsequent image processing.
2,919 citations
TL;DR: An approach to DNA sequencing using chain-terminating inhibitors (Sanger et al., 1977) combined with cloning of small fragments of DNA in a single-stranded DNA bacteriophage is described, determining the 2771-nucleotide sequence of the largest MboI restriction enzyme fragment from human mitochondrial DNA.
2,902 citations
TL;DR: The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
Abstract: In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.
2,878 citations
TL;DR: A complete atomic model for bacteriorhodopsin between amino acid residues 8 and 225 has been built and suggests that pK changes in the Schiff base must act as the means by which light energy is converted into proton pumping pressure in the channel.
2,772 citations
[...]
TL;DR: The structure, assembly, and function of the posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells.
Abstract: The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds. Reminiscent of a code, the various ubiquitin modifications adopt distinct conformations and lead to different outcomes in cells. Here, we discuss the structure, assembly, and function of this ubiquitin code.
2,762 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 |