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Institution

Laboratory of Molecular Biology

FacilityCambridge, 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
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Journal ArticleDOI
TL;DR: A role for miRNAs is uncovered in regulating m( 6)A formation of mRNAs and provide a foundation for future functional studies of m(6)A modification in cell reprogramming.

450 citations

Journal ArticleDOI
TL;DR: This work focuses on interphase cargoes of dynein, which include membrane-bound organelles, RNAs, protein complexes and viruses, and indicates how adaptor proteins play an important role in this process.
Abstract: Cytoplasmic dynein 1 is an important microtubule-based motor in many eukaryotic cells. Dynein has critical roles both in interphase and during cell division. Here, we focus on interphase cargoes of dynein, which include membrane-bound organelles, RNAs, protein complexes and viruses. A central challenge in the field is to understand how a single motor can transport such a diverse array of cargoes and how this process is regulated. The molecular basis by which each cargo is linked to dynein and its cofactor dynactin has started to emerge. Of particular importance for this process is a set of coiled-coil proteins - activating adaptors - that both recruit dynein-dynactin to their cargoes and activate dynein motility.

450 citations

Journal ArticleDOI
TL;DR: This Meeting Review describes the proceedings and conclusions from the inaugural meeting of the Electron Microscopy Validation Validation Task Force organized by the Unified Data Resource for 3DEM and aims to increase the impact of 3DEM in biology and medicine.

449 citations

Journal ArticleDOI
TL;DR: A fluorogenic reaction between bicyclo[6.1.0]non-4-yn-9-ylmethanol (BCN) and tetrazines that is 3–7 orders of magnitude faster than many bioorthogonal reactions is reported.
Abstract: Rapid, site-specific labeling of proteins with diverse probes remains an outstanding challenge for chemical biologists. Enzyme-mediated labeling approaches may be rapid but use protein or peptide fusions that introduce perturbations into the protein under study and may limit the sites that can be labeled, while many “bioorthogonal” reactions for which a component can be genetically encoded are too slow to effect quantitative site-specific labeling of proteins on a time scale that is useful for studying many biological processes. We report a fluorogenic reaction between bicyclo[6.1.0]non-4-yn-9-ylmethanol (BCN) and tetrazines that is 3–7 orders of magnitude faster than many bioorthogonal reactions. Unlike the reactions of strained alkenes, including trans-cyclooctenes and norbornenes, with tetrazines, the BCN–tetrazine reaction gives a single product of defined stereochemistry. We have discovered aminoacyl-tRNA synthetase/tRNA pairs for the efficient site-specific incorporation of a BCN-containing amino ac...

448 citations

Journal ArticleDOI
05 Feb 1999-Cell
TL;DR: Crystal structures suggest that the seven Sm proteins could form a closed ring and the snRNAs may be bound in the positively charged central hole.

448 citations


Authors

Showing all 19431 results

NameH-indexPapersCitations
Robert J. Lefkowitz214860147995
Ronald M. Evans199708166722
Tony Hunter175593124726
Marc G. Caron17367499802
Mark Gerstein168751149578
Timothy A. Springer167669122421
Harvey F. Lodish165782101124
Ira Pastan1601286110069
Bruce N. Ames158506129010
Philip Cohen154555110856
Gerald M. Rubin152382115248
Ashok Kumar1515654164086
Kim Nasmyth14229459231
Kenneth M. Yamada13944672136
Harold E. Varmus13749676320
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20239
202265
20211,222
20201,165
20191,082
2018945