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Institution

Randall Division of Cell and Molecular Biophysics

About: Randall Division of Cell and Molecular Biophysics is a based out in . It is known for research contribution in the topics: Actin cytoskeleton & Skeletal muscle. The organization has 576 authors who have published 1229 publications receiving 78279 citations.


Papers
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Journal ArticleDOI
TL;DR: The cell membrane is a highly complex designed material with remarkable physicochemical properties; comprised mainly of lipid moieties, it is capable of self-assembling, changing morphology, housing a range of distinct proteins, and withstanding electrical, chemical and mechanical perturbations.

16 citations

Journal ArticleDOI
TL;DR: The current knowledge of the molecular aspects of mammalian iron metabolism and NTBI are presented and the mechanisms of iron uptake, storage and metabolic regulation are clarified.
Abstract: Iron (Fe) is an essential, but potentially noxious, metal for almost all organisms Its precise cellular regulation is necessary to ensure synthesis of numerous iron-containing proteins required for metabolic processes yet at the same time avoiding the build-up of potentially toxic levels of iron In humans, iron-deficiency results in anemia, while excess iron can lead to organ damage as a result of a build-up of non-transferrin-bound iron (NTBI) In recent years, the cloning of novel proteins has clarified the mechanisms of iron uptake, storage and metabolic regulation Our current knowledge of the molecular aspects of mammalian iron metabolism and NTBI are presented in this review

16 citations

Journal ArticleDOI
20 Sep 2011-PLOS ONE
TL;DR: High resolution analysis of nucleosomes of the IgE switch region prior to the initiation of class switch recombination in primary human B cells and the human CL-01 B cell line suggests that acetylation and K4 tri-methylation of histone H3 may represent marks of recombinationally active chromatin and further implicates splicing in the regulation of AID action.
Abstract: Antibodies are assembled by a highly orchestrated series of recombination events during B cell development. One of these events, class switch recombination, is required to produce the IgG, IgE and IgA antibody isotypes characteristic of a secondary immune response. The action of the enzyme activation induced cytidine deaminase is now known to be essential for the initiation of this recombination event. Previous studies have demonstrated that the immunoglobulin switch regions acquire distinct histone modifications prior to recombination. We now present a high resolution analysis of these histone modifications across the IgE switch region prior to the initiation of class switch recombination in primary human B cells and the human CL-01 B cell line. These data show that upon stimulation with IL-4 and an anti-CD40 antibody that mimics T cell help, the nucleosomes of the switch regions are highly modified on histone H3, accumulating acetylation marks and tri-methylation of lysine 4. Distinct peaks of modified histones are found across the switch region, most notably at the 5' splice donor site of the germline (I) exon, which also accumulates AID. These data suggest that acetylation and K4 tri-methylation of histone H3 may represent marks of recombinationally active chromatin and further implicates splicing in the regulation of AID action.

16 citations

Journal ArticleDOI
TL;DR: There is a greater treatment effect if formulation and homework are involved in therapy, and high correlation between components means that these may be indicators of overall treatment fidelity.
Abstract: This is an author-produced electronic version of an article accepted for publication in the British Journal of Psychiatry. The definitive publisher-authenticated version is available online at http://bjp.rcpsych.org

16 citations

Journal ArticleDOI
TL;DR: The high-resolution crystal structure of the ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer determined at cryo-temperature is reported and the residues that are responsible for RNA binding are identified and a model is built to illustrate how L 30e binds to an RNA kink turn motif.
Abstract: We report here the high-resolution crystal structure of the ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer determined at cryo-temperature When it is compared with its mesophilic homologue, L30e from yeast, a number of structural features that can enhance thermostability are revealed Disordered residues corresponding to a large RNA-binding loop in yeast L30e are well structured in the T celer protein The overall charge of T celer L30e is near neutral, whereas that of the yeast homologue is highly positive This is the result of an increase in the number of acidic residues at the expense of polar residues, Asn, Ser, and Thr Extensive ion pair networks are found on the molecular surface Exposed nonpolar surface areas are reduced in the T celer protein Its side chain atoms preferably form hydrogen bonds with main chain atoms Taken together, these factors contribute to high protein stability The roles of well-conserved L30e residues are studied and found to be important in defining a very compact overall structure and in maintaining the structure of the RNA binding site By comparing it with the yeast homologue, we also identified the residues that are responsible for RNA binding and built a model to illustrate how L30e binds to an RNA kink turn motif

16 citations


Authors

Showing all 576 results

NameH-indexPapersCitations
Janet M. Thornton130539105144
Graham Dunn10148437152
Anne J. Ridley9625647563
Luigi Cavallo7954625262
Erik Sahai6914324753
Christopher Corrigan6927722451
Mathias Gautel6915916377
Hannah J. Gould6020711436
Enrico Girardi5936812712
Paul Brown5925113251
John G. Parnavelas5816411046
Heinz Jungbluth5721113707
Gareth E. Jones551619816
Linda J. Richards5415410093
Elisabeth Ehler541328503
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
202115
202026
201926
201848
201788
2016113