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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
03 Aug 2006-Nature
TL;DR: P2X receptors have a molecular architecture distinct from other ion channel protein families, and have several unique functional properties, and in autocrine loops of endothelial and epithelial cells.
Abstract: P2X receptors are membrane ion channels activated by the binding of extracellular adenosine triphosphate (ATP). For years their functional significance was consigned to distant regions of the autonomic nervous system, but recent work indicates several further key roles, such as afferent signalling, chronic pain, and in autocrine loops of endothelial and epithelial cells. P2X receptors have a molecular architecture distinct from other ion channel protein families, and have several unique functional properties.

814 citations

Journal ArticleDOI
TL;DR: Despite the general organisational similarity of networks across the phylogenetic spectrum, there are interesting qualitative differences among the network components, such as the transcription factors.

811 citations

Journal ArticleDOI
01 Mar 1997-Nature
TL;DR: In this paper, the structure of the core protein of the hepatitis B virus was solved to 7.4 A resolution using electron cryomicroscopy, revealing the complete fold of the polypeptide chain, which is unlike previously solved viral capsid proteins and is largely α-helical.
Abstract: Hepatitis B virus, a major human pathogen with an estimated 300 million carriers worldwide, can lead to cirrhosis and liver cancer in cases of chronic infection. The virus consists of an inner nucleocapsid or core, surrounded by a lipid envelope containing virally encoded surface proteins. The core protein, when expressed in bacteria, assembles into core shell particles, closely resembling the native core of the virus. Here we use electron cryomicroscopy to solve the structure of the core protein to 7.4 A resolution. Images of about 6,400 individual particles from 34 micrographs at different levels of defocus were combined, imposing icosahedral symmetry. The three-dimensional map reveals the complete fold of the polypeptide chain, which is quite unlike previously solved viral capsid proteins and is largely α-helical. The dimer clustering of subunits produces spikes on the surface of the shell, which consist of radial bundles of four long α-helices. Our model implies that the sequence corresponding to the immunodominant region of the core protein lies at the tip of the spike and also explains other properties of the core protein.

810 citations

Journal ArticleDOI
06 Aug 1966-Nature
TL;DR: Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups and their use in the determination of amide groups are studied.
Abstract: Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups

810 citations

Journal ArticleDOI
17 Aug 2020-Nature
TL;DR: Cryo-electron microscopy and tomography is applied to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface and providing a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.
Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2–6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9–12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. Cryo-electron microscopy and tomography studies reveal the structures, conformations and distributions of spike protein trimers on intact severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions and provide a basis for understanding the interactions of the spike protein with neutralizing antibodies.

808 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