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Showing 1 to 11 of 11 entries
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Drosophila Syncrip binds the gurken mRNA localisation signal and regulates localised transcripts during axis specification.

Biology open

McDermott SM, Meignin C, Rappsilber J, Davis I.
PMID: 23213441
Biol Open. 2012 May 15;1(5):488-97. doi: 10.1242/bio.2012885. Epub 2012 Apr 11.

In the Drosophila oocyte, mRNA transport and localised translation play a fundamental role in axis determination and germline formation of the future embryo. gurken mRNA encodes a secreted TGF-α signal that specifies dorsal structures, and is localised to the...

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McDermott SM, Meignin C, Rappsilber J, et al. Drosophila Syncrip binds the gurken mRNA localisation signal and regulates localised transcripts during axis specification. Biol Open. 2012;1(5):488-97doi: 10.1242/bio.2012885.
McDermott, S. M., Meignin, C., Rappsilber, J., & Davis, I. (2012). Drosophila Syncrip binds the gurken mRNA localisation signal and regulates localised transcripts during axis specification. Biology open, 1(5), 488-97. https://doi.org/10.1242/bio.2012885
McDermott, Suzanne M, et al. "Drosophila Syncrip binds the gurken mRNA localisation signal and regulates localised transcripts during axis specification." Biology open vol. 1,5 (2012): 488-97. doi: https://doi.org/10.1242/bio.2012885
McDermott SM, Meignin C, Rappsilber J, Davis I. Drosophila Syncrip binds the gurken mRNA localisation signal and regulates localised transcripts during axis specification. Biol Open. 2012 May 15;1(5):488-97. doi: 10.1242/bio.2012885. Epub 2012 Apr 11. PMID: 23213441; PMCID: PMC3507208.
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Quantitative cross-linking/mass spectrometry reveals subtle protein conformational changes.

Wellcome open research

Chen Z, Fischer L, Tahir S, Bukowski-Wills JC, Barlow P, Rappsilber J.
PMID: 27976756
Wellcome Open Res. 2016 Nov 15;1:5. doi: 10.12688/wellcomeopenres.9896.1. eCollection 2016.

Quantitative cross-linking/mass spectrometry (QCLMS) probes protein structural dynamics in solution by quantitatively comparing the yields of cross-links between different conformational statuses. We have used QCLMS to understand the final maturation step of the proteasome lid and also to elucidate...

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Chen Z, Fischer L, Tahir S, et al. Quantitative cross-linking/mass spectrometry reveals subtle protein conformational changes. Wellcome Open Res. 2016;1:5doi: 10.12688/wellcomeopenres.9896.1.
Chen, Z., Fischer, L., Tahir, S., Bukowski-Wills, J. C., Barlow, P., & Rappsilber, J. (2016). Quantitative cross-linking/mass spectrometry reveals subtle protein conformational changes. Wellcome open research, 15. https://doi.org/10.12688/wellcomeopenres.9896.1
Chen, Zhuo, et al. "Quantitative cross-linking/mass spectrometry reveals subtle protein conformational changes." Wellcome open research vol. 1 (2016): 5. doi: https://doi.org/10.12688/wellcomeopenres.9896.1
Chen Z, Fischer L, Tahir S, Bukowski-Wills JC, Barlow P, Rappsilber J. Quantitative cross-linking/mass spectrometry reveals subtle protein conformational changes. Wellcome Open Res. 2016 Nov 15;1:5. doi: 10.12688/wellcomeopenres.9896.1. eCollection 2016. PMID: 27976756; PMCID: PMC5140025.
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Efficient and versatile CRISPR engineering of human neurons in culture to model neurological disorders.

Wellcome open research

Shah RR, Cholewa-Waclaw J, Davies FCJ, Paton KM, Chaligne R, Heard E, Abbott CM, Bird AP.
PMID: 27976757
Wellcome Open Res. 2016 Nov 15;1:13. doi: 10.12688/wellcomeopenres.10011.1.

The recent identification of multiple new genetic causes of neurological disorders highlights the need for model systems that give experimental access to the underlying biology. In particular, the ability to couple disease-causing mutations with human neuronal differentiation systems would...

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Shah RR, Cholewa-Waclaw J, Davies FCJ, et al. Efficient and versatile CRISPR engineering of human neurons in culture to model neurological disorders. Wellcome Open Res. 2016;1:13doi: 10.12688/wellcomeopenres.10011.1.
Shah, R. R., Cholewa-Waclaw, J., Davies, F. C. J., Paton, K. M., Chaligne, R., Heard, E., Abbott, C. M., & Bird, A. P. (2016). Efficient and versatile CRISPR engineering of human neurons in culture to model neurological disorders. Wellcome open research, 113. https://doi.org/10.12688/wellcomeopenres.10011.1
Shah, Ruth R, et al. "Efficient and versatile CRISPR engineering of human neurons in culture to model neurological disorders." Wellcome open research vol. 1 (2016): 13. doi: https://doi.org/10.12688/wellcomeopenres.10011.1
Shah RR, Cholewa-Waclaw J, Davies FCJ, Paton KM, Chaligne R, Heard E, Abbott CM, Bird AP. Efficient and versatile CRISPR engineering of human neurons in culture to model neurological disorders. Wellcome Open Res. 2016 Nov 15;1:13. doi: 10.12688/wellcomeopenres.10011.1. PMID: 27976757; PMCID: PMC5146642.
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Quirks of Error Estimation in Cross-Linking/Mass Spectrometry.

Analytical chemistry

Fischer L, Rappsilber J.
PMID: 28267312
Anal Chem. 2017 Apr 04;89(7):3829-3833. doi: 10.1021/acs.analchem.6b03745. Epub 2017 Mar 24.

Cross-linking/mass spectrometry is an increasingly popular approach to obtain structural information on proteins and their complexes in solution. However, methods for error assessment are under current development. We note that false-discovery rates can be estimated at different points during...

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Fischer L, Rappsilber J. Quirks of Error Estimation in Cross-Linking/Mass Spectrometry. Anal Chem. 2017;89(7):3829-3833doi: 10.1021/acs.analchem.6b03745.
Fischer, L., & Rappsilber, J. (2017). Quirks of Error Estimation in Cross-Linking/Mass Spectrometry. Analytical chemistry, 89(7), 3829-3833. https://doi.org/10.1021/acs.analchem.6b03745
Fischer, Lutz, and Rappsilber, Juri. "Quirks of Error Estimation in Cross-Linking/Mass Spectrometry." Analytical chemistry vol. 89,7 (2017): 3829-3833. doi: https://doi.org/10.1021/acs.analchem.6b03745
Fischer L, Rappsilber J. Quirks of Error Estimation in Cross-Linking/Mass Spectrometry. Anal Chem. 2017 Apr 04;89(7):3829-3833. doi: 10.1021/acs.analchem.6b03745. Epub 2017 Mar 24. PMID: 28267312; PMCID: PMC5423704.
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Blind testing cross-linking/mass spectrometry under the auspices of the 11.

Wellcome open research

Belsom A, Schneider M, Fischer L, Mabrouk M, Stahl K, Brock O, Rappsilber J.
PMID: 28317030
Wellcome Open Res. 2016 Dec 09;1:24. doi: 10.12688/wellcomeopenres.10046.1.

Determining the structure of a protein by any method requires various contributions from experimental and computational sides. In a recent study, high-density cross-linking/mass spectrometry (HD-CLMS) data in combination with

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Belsom A, Schneider M, Fischer L, et al. Blind testing cross-linking/mass spectrometry under the auspices of the 11. Wellcome Open Res. 2016;1:24doi: 10.12688/wellcomeopenres.10046.1.
Belsom, A., Schneider, M., Fischer, L., Mabrouk, M., Stahl, K., Brock, O., & Rappsilber, J. (2016). Blind testing cross-linking/mass spectrometry under the auspices of the 11. Wellcome open research, 124. https://doi.org/10.12688/wellcomeopenres.10046.1
Belsom, Adam, et al. "Blind testing cross-linking/mass spectrometry under the auspices of the 11." Wellcome open research vol. 1 (2016): 24. doi: https://doi.org/10.12688/wellcomeopenres.10046.1
Belsom A, Schneider M, Fischer L, Mabrouk M, Stahl K, Brock O, Rappsilber J. Blind testing cross-linking/mass spectrometry under the auspices of the 11. Wellcome Open Res. 2016 Dec 09;1:24. doi: 10.12688/wellcomeopenres.10046.1. PMID: 28317030; PMCID: PMC5354267.
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Cdc14 phosphatase directs centrosome re-duplication at the meiosis I to meiosis II transition in budding yeast.

Wellcome open research

Fox C, Zou J, Rappsilber J, Marston AL.
PMID: 28133632
Wellcome Open Res. 2017 Jan 05;2:2. doi: 10.12688/wellcomeopenres.10507.2.

No abstract available.

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Fox C, Zou J, Rappsilber J, et al. Cdc14 phosphatase directs centrosome re-duplication at the meiosis I to meiosis II transition in budding yeast. Wellcome Open Res. 2017;2:2doi: 10.12688/wellcomeopenres.10507.2.
Fox, C., Zou, J., Rappsilber, J., & Marston, A. L. (2017). Cdc14 phosphatase directs centrosome re-duplication at the meiosis I to meiosis II transition in budding yeast. Wellcome open research, 22. https://doi.org/10.12688/wellcomeopenres.10507.2
Fox, Colette, et al. "Cdc14 phosphatase directs centrosome re-duplication at the meiosis I to meiosis II transition in budding yeast." Wellcome open research vol. 2 (2017): 2. doi: https://doi.org/10.12688/wellcomeopenres.10507.2
Fox C, Zou J, Rappsilber J, Marston AL. Cdc14 phosphatase directs centrosome re-duplication at the meiosis I to meiosis II transition in budding yeast. Wellcome Open Res. 2017 Jan 05;2:2. doi: 10.12688/wellcomeopenres.10507.2. PMID: 28133632; PMCID: PMC5266553.
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Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-tubulin ring complex to the mitotic spindle.

Biology open

Chen JWC, Chen ZA, Rogala KB, Metz J, Deane CM, Rappsilber J, Wakefield JG.
PMID: 28351835
Biol Open. 2017 May 15;6(5):654-663. doi: 10.1242/bio.022905.

The hetero-octameric protein complex, Augmin, recruits γ-Tubulin ring complex (γ-TuRC) to pre-existing microtubules (MTs) to generate branched MTs during mitosis, facilitating robust spindle assembly. However, despite a recent partial reconstitution of the human Augmin complex

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Chen JWC, Chen ZA, Rogala KB, et al. Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-tubulin ring complex to the mitotic spindle. Biol Open. 2017;6(5):654-663doi: 10.1242/bio.022905.
Chen, J. W. C., Chen, Z. A., Rogala, K. B., Metz, J., Deane, C. M., Rappsilber, J., & Wakefield, J. G. (2017). Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-tubulin ring complex to the mitotic spindle. Biology open, 6(5), 654-663. https://doi.org/10.1242/bio.022905
Chen, Jack W C, et al. "Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-tubulin ring complex to the mitotic spindle." Biology open vol. 6,5 (2017): 654-663. doi: https://doi.org/10.1242/bio.022905
Chen JWC, Chen ZA, Rogala KB, Metz J, Deane CM, Rappsilber J, Wakefield JG. Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-tubulin ring complex to the mitotic spindle. Biol Open. 2017 May 15;6(5):654-663. doi: 10.1242/bio.022905. PMID: 28351835; PMCID: PMC5450317.
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Microinjection of Antibodies Targeting the Lamin A/C Histone-Binding Site Blocks Mitotic Entry and Reveals Separate Chromatin Interactions with HP1, CenpB and PML.

Cells

Dixon CR, Platani M, Makarov AA, Schirmer EC.
PMID: 28346356
Cells. 2017 Mar 25;6(2). doi: 10.3390/cells6020009.

Lamins form a scaffold lining the nucleus that binds chromatin and contributes to spatial genome organization; however, due to the many other functions of lamins, studies knocking out or altering the lamin polymer cannot clearly distinguish between direct and...

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Dixon CR, Platani M, Makarov AA, et al. Microinjection of Antibodies Targeting the Lamin A/C Histone-Binding Site Blocks Mitotic Entry and Reveals Separate Chromatin Interactions with HP1, CenpB and PML. Cells. 2017;6(2)doi: 10.3390/cells6020009.
Dixon, C. R., Platani, M., Makarov, A. A., & Schirmer, E. C. (2017). Microinjection of Antibodies Targeting the Lamin A/C Histone-Binding Site Blocks Mitotic Entry and Reveals Separate Chromatin Interactions with HP1, CenpB and PML. Cells, 6(2), . https://doi.org/10.3390/cells6020009
Dixon, Charles R, et al. "Microinjection of Antibodies Targeting the Lamin A/C Histone-Binding Site Blocks Mitotic Entry and Reveals Separate Chromatin Interactions with HP1, CenpB and PML." Cells vol. 6,2 (2017). doi: https://doi.org/10.3390/cells6020009
Dixon CR, Platani M, Makarov AA, Schirmer EC. Microinjection of Antibodies Targeting the Lamin A/C Histone-Binding Site Blocks Mitotic Entry and Reveals Separate Chromatin Interactions with HP1, CenpB and PML. Cells. 2017 Mar 25;6(2). doi: 10.3390/cells6020009. PMID: 28346356; PMCID: PMC5492013.
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Dgp71WD is required for the assembly of the acentrosomal Meiosis I spindle, and is not a general targeting factor for the γ-TuRC.

Biology open

Reschen RF, Colombie N, Wheatley L, Dobbelaere J, St Johnston D, Ohkura H, Raff JW.
PMID: 23213433
Biol Open. 2012 May 15;1(5):422-9. doi: 10.1242/bio.2012596. Epub 2012 Mar 06.

Dgp71WD/Nedd1 proteins are essential for mitotic spindle formation. In human cells, Nedd1 targets γ-tubulin to both centrosomes and spindles, but in other organisms the function of Dgp71WD/Nedd1 is less clear. In Drosophila cells, Dgp71WD plays a major part in...

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Reschen RF, Colombie N, Wheatley L, et al. Dgp71WD is required for the assembly of the acentrosomal Meiosis I spindle, and is not a general targeting factor for the γ-TuRC. Biol Open. 2012;1(5):422-9doi: 10.1242/bio.2012596.
Reschen, R. F., Colombie, N., Wheatley, L., Dobbelaere, J., St Johnston, D., Ohkura, H., & Raff, J. W. (2012). Dgp71WD is required for the assembly of the acentrosomal Meiosis I spindle, and is not a general targeting factor for the γ-TuRC. Biology open, 1(5), 422-9. https://doi.org/10.1242/bio.2012596
Reschen, Richard F, et al. "Dgp71WD is required for the assembly of the acentrosomal Meiosis I spindle, and is not a general targeting factor for the γ-TuRC." Biology open vol. 1,5 (2012): 422-9. doi: https://doi.org/10.1242/bio.2012596
Reschen RF, Colombie N, Wheatley L, Dobbelaere J, St Johnston D, Ohkura H, Raff JW. Dgp71WD is required for the assembly of the acentrosomal Meiosis I spindle, and is not a general targeting factor for the γ-TuRC. Biol Open. 2012 May 15;1(5):422-9. doi: 10.1242/bio.2012596. Epub 2012 Mar 06. PMID: 23213433; PMCID: PMC3507215.
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Optimizing the Parameters Governing the Fragmentation of Cross-Linked Peptides in a Tribrid Mass Spectrometer.

Analytical chemistry

Kolbowski L, Mendes ML, Rappsilber J.
PMID: 28402676
Anal Chem. 2017 May 16;89(10):5311-5318. doi: 10.1021/acs.analchem.6b04935. Epub 2017 Apr 26.

We compared the five different ways of fragmentation available on a tribrid mass spectrometer and optimized their collision energies with regard to optimal sequence coverage of cross-linked peptides. We created a library of bis(sulfosuccinimidyl)suberate (BS3/DSS) cross-linked precursors, derived from...

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Kolbowski L, Mendes ML, Rappsilber J. Optimizing the Parameters Governing the Fragmentation of Cross-Linked Peptides in a Tribrid Mass Spectrometer. Anal Chem. 2017;89(10):5311-5318doi: 10.1021/acs.analchem.6b04935.
Kolbowski, L., Mendes, M. L., & Rappsilber, J. (2017). Optimizing the Parameters Governing the Fragmentation of Cross-Linked Peptides in a Tribrid Mass Spectrometer. Analytical chemistry, 89(10), 5311-5318. https://doi.org/10.1021/acs.analchem.6b04935
Kolbowski, Lars, et al. "Optimizing the Parameters Governing the Fragmentation of Cross-Linked Peptides in a Tribrid Mass Spectrometer." Analytical chemistry vol. 89,10 (2017): 5311-5318. doi: https://doi.org/10.1021/acs.analchem.6b04935
Kolbowski L, Mendes ML, Rappsilber J. Optimizing the Parameters Governing the Fragmentation of Cross-Linked Peptides in a Tribrid Mass Spectrometer. Anal Chem. 2017 May 16;89(10):5311-5318. doi: 10.1021/acs.analchem.6b04935. Epub 2017 Apr 26. PMID: 28402676; PMCID: PMC5436099.
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Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry.

Analytical chemistry

Belsom A, Mudd G, Giese S, Auer M, Rappsilber J.
PMID: 28430416
Anal Chem. 2017 May 16;89(10):5319-5324. doi: 10.1021/acs.analchem.6b04938. Epub 2017 May 04.

Use of a heterobifunctional photoactivatable cross-linker, sulfo-SDA (diazirine), has yielded high-density data that facilitated structure modeling of individual proteins. We expand the photoactivatable chemistry toolbox here with a second reagent, sulfo-SBP (benzophenone). This further increases the density of photo-cross-linking...

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Belsom A, Mudd G, Giese S, et al. Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry. Anal Chem. 2017;89(10):5319-5324doi: 10.1021/acs.analchem.6b04938.
Belsom, A., Mudd, G., Giese, S., Auer, M., & Rappsilber, J. (2017). Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry. Analytical chemistry, 89(10), 5319-5324. https://doi.org/10.1021/acs.analchem.6b04938
Belsom, Adam, et al. "Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry." Analytical chemistry vol. 89,10 (2017): 5319-5324. doi: https://doi.org/10.1021/acs.analchem.6b04938
Belsom A, Mudd G, Giese S, Auer M, Rappsilber J. Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry. Anal Chem. 2017 May 16;89(10):5319-5324. doi: 10.1021/acs.analchem.6b04938. Epub 2017 May 04. PMID: 28430416; PMCID: PMC5441754.
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Showing 1 to 11 of 11 entries