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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, Transcription (biology)


Papers
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Journal ArticleDOI
TL;DR: The unique features of the early-appearing GABA signalling systems might help to explain how GABA acts as a developmental signal in the immature brain.
Abstract: In the mature brain, GABA (gamma-aminobutyric acid) functions primarily as an inhibitory neurotransmitter. But it can also act as a trophic factor during nervous system development to influence events such as proliferation, migration, differentiation, synapse maturation and cell death. GABA mediates these processes by the activation of traditional ionotropic and metabotropic receptors, and probably by both synaptic and non-synaptic mechanisms. However, the functional properties of GABA receptor signalling in the immature brain are significantly different from, and in some ways opposite to, those found in the adult brain. The unique features of the early-appearing GABA signalling systems might help to explain how GABA acts as a developmental signal.

1,095 citations

Journal ArticleDOI
06 Jun 2013-Cell
TL;DR: It is concluded that cell-type-specific chromatin organization occurs at the submegabase scale and that architectural proteins shape the genome in hierarchical length scales.

1,092 citations

Journal ArticleDOI
TL;DR: This work shows how the concept of time-averaged forces can be used to simplify conformafional energy calculations on globular proteins and shows that the simplifications work well in representing the stable native conformation of this globular protein.

1,089 citations

Journal ArticleDOI
TL;DR: Different functional properties of HBGF-1 may be dissociated at the structural level, as observed in transfection studies and Mitogenic assays.
Abstract: The fibroblast or heparin-binding growth factors (HBGFs) are thought to be modulators of cell growth and migration, angiogenesis, wound repair, neurite extension, and mesoderm induction. A better understanding of the structural basis for the different activities of these proteins should facilitate the development of agonists and antagonists of specific HBGF activities and identification of the signal transduction pathways involved in the mechanisms of action of these growth factors. Chemical modification studies of Harper and Lobb (Harper, J. W., and R. R. Lobb. 1988. Biochemistry. 27:671-678) implicated lysine 132 in HBGF-1 (acidic fibroblast growth factor) as being important to the heparin-binding, receptor-binding, and mitogenic activities of the protein. We changed lysine 132 to a glutamic acid residue by site-directed mutagenesis of the human cDNA and expressed the mutant protein in Escherichia coli to obtain sufficient quantities for functional studies. Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type). Mitogenic assays established two points: (a) human recombinant HBGF-1 is highly dependent on the presence of heparin for optimal mitogenic activity, and (b) the change of lysine 132 to glutamic acid drastically reduces the specific mitogenic activity of HBGF-1. The poor mitogenic activity of the mutant protein does not appear to be due to a reduced affinity for the HBGF receptor. Similarly, the mutant HBGF-1 can stimulate tyrosine kinase activity and induce protooncogene expression. Differences in the biological properties of the wild-type and mutant proteins were observed in transfection studies. Mutant HBGF-1 expression in transfected NIH 3T3 cells did not induce the same transformed phenotype characteristic of cells expressing wild-type HBGF-1. Together these data indicate that different functional properties of HBGF-1 may be dissociated at the structural level.

1,088 citations

Journal ArticleDOI
TL;DR: Domain Antibels (dAbs) as discussed by the authors are the smallest known antigen-binding fragments of antibodies, ranging from 11 kDa to 15 kDa, and they are the robust variable regions of the heavy and light chains of immunoglobulins (VH and VL respectively).

1,078 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