Imperial College London

ProfessorBernadetteByrne

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Molecular Membrane Biology
 
 
 
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Contact

 

+44 (0)20 7594 3004b.byrne Website

 
 
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Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Publication Type
Year
to

118 results found

Tanabe M, Atkins HS, Harland DN, Elvin SJ, Stagg AJ, Mirza O, Titball RW, Byrne B, Brown KAet al., 2006, The ABC transporter protein OppA provides protection against experimental Yersinia pestis infection, INFECTION AND IMMUNITY, Vol: 74, Pages: 3687-3691, ISSN: 0019-9567

Journal article

Horsefield R, Yankovskaya V, Sexton G, Whittingham W, Shiomi K, Omura S, Byrne B, Cecchini G, Iwata Set al., 2006, Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase) - A mechanism of electron transfer and proton conduction during ubiquinone reduction, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 281, Pages: 7309-7316

Journal article

Byrne B, Jormakka M, 2006, Solubilisation and Purification of Membrane Protein, Structural Genomics on Membrane Proteins, Publisher: Taylor & Francis, Pages: 179-198

Book chapter

Horsefield R, Iwata S, Byrne B, 2004, Complex II from a structural perspective, CURRENT PROTEIN & PEPTIDE SCIENCE, Vol: 5, Pages: 107-118, ISSN: 1389-2037

Journal article

Horsefield R, Yankovskaya V, Byrne B, Cecchini G, Iwata Set al., 2004, The structure of complex II and its quinone-binding site, 13th European Bioenergetics Conference (EBEC 2004), Publisher: ELSEVIER SCIENCE BV, Pages: 165-165, ISSN: 0005-2728

Conference paper

Jormakka M, Richardson D, Byrne B, Iwata Set al., 2004, Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes, STRUCTURE, Vol: 12, Pages: 95-104, ISSN: 0969-2126

Journal article

Jormakka M, Byrne B, Iwata S, 2003, Formate dehydrogenase - a versatile enzyme in changing environments, CURRENT OPINION IN STRUCTURAL BIOLOGY, Vol: 13, Pages: 418-423, ISSN: 0959-440X

Journal article

Jormakka M, Byrne B, Iwata S, 2003, Protonmotive force generation by a redox loop mechanism, FEBS LETTERS, Vol: 545, Pages: 25-30, ISSN: 0014-5793

Journal article

Horsefield R, Yankovskaya V, Tornroth S, Luna-Chavez C, Stambouli E, Barber J, Byrne B, Cecchini G, Iwata Set al., 2003, Using rational screening and electron microscopy to optimize the crystallization of succinate : ubiquinone oxidoreductase from Escherichia coli, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, Vol: 59, Pages: 600-602, ISSN: 0907-4449

Journal article

Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata Set al., 2003, Architecture of succinate dehydrogenase and reactive oxygen species generation, SCIENCE, Vol: 299, Pages: 700-704, ISSN: 0036-8075

Journal article

Iwata M, Abramson J, Byrne B, Iwata Set al., 2003, Structure and function of quinone binding membrane proteins, MEMBRANE PROTEINS, Vol: 63, Pages: 151-176, ISSN: 0065-3233

Journal article

Abramson J, Byrne B, Iwata S, 2003, Crystallization of cytochrome bo3 ubiquinol oxidase from E. coli, Publisher: International University Line, Pages: 227-238

Book chapter

Byrne B, Iwata S, 2003, Generating antibody fragments for structural studies: a guide, Publisher: International University Line, Pages: 89-100

Book chapter

Byrne B, Iwata S, 2002, Membrane protein complexes, CURRENT OPINION IN STRUCTURAL BIOLOGY, Vol: 12, Pages: 239-243, ISSN: 0959-440X

Journal article

Jormakka M, Tornroth S, Byrne B, Iwata Set al., 2002, Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N, SCIENCE, Vol: 295, Pages: 1863-1868, ISSN: 0036-8075

Journal article

Jormakka M, Tornroth S, Abramson J, Byrne B, Iwata Set al., 2002, Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, Vol: 58, Pages: 160-162, ISSN: 0907-4449

Journal article

Jormakka M, Toernroth S, Byrne B, Iwata Set al., 2002, STRUCTURAL STUDIES ON FORMATE DEHYDROGENASE-N FROM E. COLI, Publisher: INT UNION CRYSTALLOGRAPHY, Pages: C207-C207, ISSN: 2053-2733

Conference paper

Abramson J, Svensson-Ek M, Byrne B, Iwata Set al., 2001, Structure of cytochrome c oxidase: a comparison of the bacterial and mitochondrial enzymes, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, Vol: 1544, Pages: 1-9, ISSN: 0167-4838

Journal article

Byrne B, Abramson J, Jansson M, Holmgren E, Iwata Set al., 2000, Fusion protein approach to improve the crystal quality of cytochrome bo(3) ubiquinol oxidase from Escherichia coli, BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1459, Pages: 449-455, ISSN: 0005-2728

Journal article

Abramson J, Larsson G, Byrne B, Puustinen A, Garcia-Horsman A, Iwata Set al., 2000, Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo(3) ubiquinol oxidase from Escherichia coli, ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, Vol: 56, Pages: 1076-1078, ISSN: 2059-7983

Journal article

Byrne B, Jormakka M, Abramson J, Iwata Set al., 2000, A novel, fusion protein strategy for membrane protein crystallisation., Publisher: INT UNION CRYSTALLOGRAPHY, Pages: S58-S58, ISSN: 2053-2733

Conference paper

Byrne B, McGregor A, Taylor PL, Sellar R, Rodger FE, Fraser HM, Eidne KAet al., 1999, Isolation and characterisation of the marmoset gonadotrophin releasing hormone receptor: Ser(140) of the DRS motif is substituted by Phe, JOURNAL OF ENDOCRINOLOGY, Vol: 163, Pages: 447-456, ISSN: 0022-0795

Journal article

Byrne B, Klahn S, Taylor PL, Eidne KAet al., 1998, Functional analysis of GnRH receptor ligand binding using biotinylated GnRH derivatives, MOLECULAR AND CELLULAR ENDOCRINOLOGY, Vol: 144, Pages: 11-19, ISSN: 0303-7207

Journal article

Byrne B, Fowler PA, Templeton AA, 1996, Gonadotrophin surge attenuating factor suppresses progesterone augmentation of GnRH priming, Journal of Clinical Endocrinology & Metabolism, Vol: 81, Pages: 1454-1459

We investigated the effects of gonadotropin surge-attenuating factor (GnSAF), inhibin, and follistatin on GnRH self-priming and its augmentation by progesterone. Two GnRH challenges, 60 min apart, were administered to rat pituitary monolayers after 90-min exposure to medium alone (control), progesterone, GnSAF, inhibin, or follistatin. Inhibin-stripped follicular fluid from superovulated women was used as a source of GnSAF bioactivity. Under control conditions, the greater response to the second GnRH challenge (peak 2, 9.2 +/- 2.1; peak 1, 4.4 +/- 0.9 ng LH/mL; P < 0.01) demonstrated GnRH self-priming. None of the treatments significantly altered the first LH peak. Progesterone markedly increased GnRH self-priming (peak 2, 12.6 +/- 2.5 ng LH/mL; P < 0.01). However, GnSAF and RU486 significantly reduced GnRH self-priming (peak 2, 4.6 +/- 0.9 and 5.6 +/- 1.6 ng LH/mL, respectively; P < 0.01). The augmentation of self-priming induced by progesterone was completely abolished by coincubation with either GnSAF or RU486 (peak 2, 7.5 +/- 1.6 and 4.3 +/- 0.9 ng LH/mL, respectively; P < 0.01). Neither inhibin nor follistatin had any effect on GnRH self-priming or its augmentation by progesterone. The actions of RU486 in the presence and absence of progesterone demonstrate a nonprogestagenic effect of RU486 on the gonadotropes. In conclusion, the suppression of GnRH self-priming, with or without progesterone augmentation, supports the hypothesis that GnSAF acts by maintaining the pituitary in an unprimed state of reduced responsiveness to GnRH.

Journal article

Byrne B, Fowler PA, Templeton AA, 1996, The effects of steroidal and non-steroidal ovarian factors on the pituitary responsiveness to gonadotrophin surge attenuating factor., Journal of Endocrinology, Vol: 150, Pages: 413-422

Primary pituitary cultures from adult female rats were used to investigate the effects of steroidal (oestradiol and progesterone) and non-steroidal (inhibin, follistatin) ovarian hormones on the suppressive actions of the ovarian factor gonadotrophin surge-attenuating factor (GnSAF) in the control of gonadotrophin secretion. The source of GnSAF was a chromatographic preparation from follicular fluid containing four distinct protein bands as resolved on SDS-PAGE. Oestradiol and progesterone added alone had no effect on gonadotrophin secretion but had a wide range of effects on the suppression of both LH and FSH secretion caused by the non-steroidal factors. Oestradiol, progesterone and oestradiol+progesterone enhanced the suppressive actions of GnSAF on GnRH-induced LH secretion (causing 19.3 +/- 5.2% (P < 0.05), 41.9 +/- 3.4% (P < 0.001) and 32.2 +/- 5.3% (P < 0.001) greater suppression than GnSAF alone). Progesterone and oestradiol+progesterone completely abolished the suppression of basal FSH secretion caused by inhibin (causing 157.1 +/- 22.2%, P < 0.001, and 160.9 +/- 11.3%, P < 0.001, stimulation compared with inhibin alone). Separately the steroids had no effect on the suppression of gonadotrophin secretion caused by follistatin. However, in combination, oestradiol+progesterone potentiated the suppressive actions of follistatin on GnRH-induced LH secretion causing 29.9 +/- 5.3% (P < 0.05) greater suppression than follistatin alone. In combination, high-dose follistatin and GnSAF caused 31.1 +/- 6.5% (P < 0.01) greater suppression than GnSAF alone. Thus in combination high-dose follistatin and GnSAF have additive effects on the suppression of GnRH-induced LH secretion. Recombinant human inhibin and GnSAF added in combination had little further effect compared with either alone suggesting that they may have a similar mechanism of action at the pituitary level. These results demonstrate that while FSH secretion in vitro is mainly controlled b

Journal article

Byrne B, Fowler PA, Fraser M, Culler M, Templeton Aet al., 1995, GnSAF bioactivity present in serum from superovulated women is not blocked by inhibin antibody., Biology of Reproduction, Vol: 52, Pages: 88-95

Primary pituitary cultures from adult female rats were used to investigate gonadotropin surge attenuating factor (GnSAF) bioactivity. Serum from superovulated women was charcoal-treated and incubated with either an inhibin antibody (MC4), normal sheep serum (NSS), or serum-free defined medium (SFDM) before addition to cell culture. The reduction in GnRH-induced LH secretion (GnSAF bioactivity) produced by the serum (30.1 +/- 6.5%, p < 0.001, of control) was not altered by prior incubation with either MC4 or NSS (24.9 +/- 3.6 and 23.2 +/- 2.7%, p < 0.001, of control, respectively). This indicates that GnSAF bioactivity present in serum from superovulated women is not entirely attributable to inhibin. Recombinant human inhibin reduced basal FSH secretion to 24.6 +/- 4.7% (p < 0.001) of the control value. However, this was totally abolished by prior incubation with MC4, but not NSS. We have also shown that ovarian steroids are not responsible for GnSAF bioactivity in vitro. In conclusion, in contrast to findings in superovulated rats, inhibin antibody did not block GnSAF bioactivity in serum from superovulated women.

Journal article

Fowler PA, Cunningham P, Fraser M, MacGregor F, Byrne B, Pappas A, Messinis IE, Templeton Aet al., 1994, Ciruclating gonadotrphin surge attenuating factor from superovulated women suppresses in vitro gonadotrophin-releasing hormone self-priming, Journal of Endocrinology, Vol: 143, Pages: 45-54

A perifusion system based on ovine pituitary tissue explants was used to investigate the effects of follicular fluid (hFF) and serum from superovulated women on pituitary responsiveness to gonadotrophin-releasing hormone (GnRH). The specific aims of the study were to determine both if gonadotrophin surge-attenuating factor (GnSAF) bioactivity is present in the peripheral circulation as well as in the follicles of superovulated women and if GnSAF suppresses GnRH self-priming in vitro. Two pulses of GnRH, 1 h apart, produced marked peaks in LH secreted from control chambers, with GnRH self-priming evident in the significant difference between the first (134.4 +/- 1.7 - 232.1 +/- 24.0% of basal secretion) and second (183.9 +/- 15.8 - 313.9 +/- 14.0% of basal secretion) LH peaks. Both follicular fluid and serum pooled from two different groups of women produced marked suppression of the first (unprimed) and second (primed) LH peaks. The hFF reduced the first LH peak to 69.6 +/- 7.8 and 60.2 +/- 9.7% and the second LH peak to 57.4 +/- 6.7 and 42.6 +/- 6.5% of control LH secretion. Overall, the serum reduced the first and second LH peaks to 76.8 +/- 4.2 and 62.9 +/- 3.6% of control respectively. These results demonstrated that GnSAF bioactivity suppresses GnRH self-priming, and is present in both the peripheral circulation and hFF. The same material administered to dispersed ovine pituitary monolayers produced similar marked suppression of GnRH-induced LH secretion, with approximately 50-fold less GnSAF bioactivity in serum compared with hFF. Combined doses of oestradiol and progesterone, or hFF from large follicles containing little GnSAF, produced stimulation of GnRH-induced LH secretion and GnRH self-priming (second peaks 78.1 +/- 38.9 and 27.4 +/- 15.7% respectively higher than first peaks). Thus, in conclusion, GnSAF in hFF and serum markedly attenuated both unprimed and primed pituitary response to GnRH, virtually abolishing the GnRH self-priming effect.

Journal article

Fowler PA, Fraser M, Cunningham P, Knight PG, Byrne B, McLaughlin EA, Wardle PG, Hull MG, Templeton Aet al., 1994, Higher gonadotrophin surge-attenuating factor bioactivity is found in small follicles from superovulated women, Journal of Endocrinology, Vol: 143, Pages: 33-44

Ovine and rat pituitary bioassays for gonadotrophin surge-attenuating factor (GnSAF) were utilized to determine whether the level of GnSAF bioactivity in pooled human follicular fluid (hFF) from superovulated women varied according to follicle diameter (< or = 11 mm, 12-15 mm and 16-21 mm follicles examined using the ovine bioassay, or < or = 10 mm, 11-13 mm, 14-17 mm, 18-20 mm, 21-24 mm and > or = 25 mm follicles examined using the rat bioassay). When tested using dispersed ovine pituitary cells, GnSAF bioactivity, expressed in terms of the reduction in gonadotrophin-releasing hormone (GnRH)-induced LH secretion, was inversely related to follicle diameter (P < 0.01). In response to 5 microliters hFF/well from follicles of < or = 11, 12-15 and 16-21 mm diameter, GnRH-induced LH secretion was reduced to 40.5 +/- 6.9%, 65.2 +/- 6.6% and 83.7 +/- 7.9% of control respectively. A similar inverse relationship was observed when a second batch of hFF samples from different sized follicles was tested using rat pituitary cell monolayers. Expressing GnSAF bioactivity in terms of the dose required to suppress GnRH-induced LH secretion by rat pituitary cells to 50% of the maximal suppression observed (ED50), the three smallest follicle size pools contained the most GnSAF (ED50 values of 0.13, 2.79 and 5.36 microliters hFF/well from follicles of < or = 10, 11-13 and 14-17 mm respectively). The ED50 values for follicles of 18-20, 21-24 and > or = 25 mm were 8.81, 27.1 and 60.0 microliters hFF/well respectively. Thus hFF from follicles < or = 11 mm was over 450 times more potent than hFF from follicles > or = 25 mm in suppressing GnRH-induced LH release. The ED50 values for inhibin bioactivity (measured as the suppression of basal FSH secretion from rat pituitary monolayers) were much less variable than those for GnSAF bioactivity (between 0.85 and 0.13 microliters hFF/well). Inhibin immunoreactivity, measured by a two-site immunoradiometric assay, follow

Journal article

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