---
_id: '8482'
abstract:
- lang: eng
  text: The SOFAST-HMQC experiment [P. Schanda, B. Brutscher, Very fast two-dimensional
    NMR spectroscopy for real-time investigation of dynamic events in proteins on
    the time scale of seconds, J. Am. Chem. Soc. 127 (2005) 8014–8015] allows recording
    two-dimensional correlation spectra of macromolecules such as proteins in only
    a few seconds acquisition time. To achieve the highest possible sensitivity, SOFAST-HMQC
    experiments are preferably performed on high-field NMR spectrometers equipped
    with cryogenically cooled probes. The duty cycle of over 80% in fast-pulsing SOFAST-HMQC
    experiments, however, may cause problems when using a cryogenic probe. Here we
    introduce SE-IPAP-SOFAST-HMQC, a new pulse sequence that provides comparable sensitivity
    to standard SOFAST-HMQC, while avoiding heteronuclear decoupling during 1H detection,
    and thus significantly reducing the radiofrequency load of the probe during the
    experiment. The experiment is also attractive for fast and sensitive measurement
    of heteronuclear one-bond spin coupling constants.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Thomas
  full_name: Kern, Thomas
  last_name: Kern
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Kern T, Schanda P, Brutscher B. Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing
    2D NMR with reduced radiofrequency load. <i>Journal of Magnetic Resonance</i>.
    2008;190(2):333-338. doi:<a href="https://doi.org/10.1016/j.jmr.2007.11.015">10.1016/j.jmr.2007.11.015</a>
  apa: Kern, T., Schanda, P., &#38; Brutscher, B. (2008). Sensitivity-enhanced IPAP-SOFAST-HMQC
    for fast-pulsing 2D NMR with reduced radiofrequency load. <i>Journal of Magnetic
    Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2007.11.015">https://doi.org/10.1016/j.jmr.2007.11.015</a>
  chicago: Kern, Thomas, Paul Schanda, and Bernhard Brutscher. “Sensitivity-Enhanced
    IPAP-SOFAST-HMQC for Fast-Pulsing 2D NMR with Reduced Radiofrequency Load.” <i>Journal
    of Magnetic Resonance</i>. Elsevier, 2008. <a href="https://doi.org/10.1016/j.jmr.2007.11.015">https://doi.org/10.1016/j.jmr.2007.11.015</a>.
  ieee: T. Kern, P. Schanda, and B. Brutscher, “Sensitivity-enhanced IPAP-SOFAST-HMQC
    for fast-pulsing 2D NMR with reduced radiofrequency load,” <i>Journal of Magnetic
    Resonance</i>, vol. 190, no. 2. Elsevier, pp. 333–338, 2008.
  ista: Kern T, Schanda P, Brutscher B. 2008. Sensitivity-enhanced IPAP-SOFAST-HMQC
    for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic
    Resonance. 190(2), 333–338.
  mla: Kern, Thomas, et al. “Sensitivity-Enhanced IPAP-SOFAST-HMQC for Fast-Pulsing
    2D NMR with Reduced Radiofrequency Load.” <i>Journal of Magnetic Resonance</i>,
    vol. 190, no. 2, Elsevier, 2008, pp. 333–38, doi:<a href="https://doi.org/10.1016/j.jmr.2007.11.015">10.1016/j.jmr.2007.11.015</a>.
  short: T. Kern, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 190 (2008)
    333–338.
date_created: 2020-09-18T10:12:46Z
date_published: 2008-02-01T00:00:00Z
date_updated: 2021-01-12T08:19:35Z
day: '01'
doi: 10.1016/j.jmr.2007.11.015
extern: '1'
intvolume: '       190'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '02'
oa_version: None
page: 333-338
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced
  radiofrequency load
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 190
year: '2008'
...
---
_id: '11116'
abstract:
- lang: eng
  text: The metazoan nuclear envelope (NE) breaks down and re-forms during each cell
    cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport
    during interphase, assemble into the re-forming NE at the end of mitosis. Using
    in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal
    effect lethal), a recently discovered NE component in Caenorhabditis elegans,
    functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107–160 complex
    (Nup for nucleoporin), an important building block of the NPC, and is essential
    for the recruitment of the Nup107–160 complex to chromatin. We suggest that MEL-28
    acts as a seeding point for NPC assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Cerstin
  full_name: Franz, Cerstin
  last_name: Franz
- first_name: Rudolf
  full_name: Walczak, Rudolf
  last_name: Walczak
- first_name: Sevil
  full_name: Yavuz, Sevil
  last_name: Yavuz
- first_name: Rachel
  full_name: Santarella, Rachel
  last_name: Santarella
- first_name: Marc
  full_name: Gentzel, Marc
  last_name: Gentzel
- first_name: Peter
  full_name: Askjaer, Peter
  last_name: Askjaer
- first_name: Vincent
  full_name: Galy, Vincent
  last_name: Galy
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
- first_name: Iain W
  full_name: Mattaj, Iain W
  last_name: Mattaj
- first_name: Wolfram
  full_name: Antonin, Wolfram
  last_name: Antonin
citation:
  ama: Franz C, Walczak R, Yavuz S, et al. MEL‐28/ELYS is required for the recruitment
    of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO
    reports</i>. 2007;8(2):165-172. doi:<a href="https://doi.org/10.1038/sj.embor.7400889">10.1038/sj.embor.7400889</a>
  apa: Franz, C., Walczak, R., Yavuz, S., Santarella, R., Gentzel, M., Askjaer, P.,
    … Antonin, W. (2007). MEL‐28/ELYS is required for the recruitment of nucleoporins
    to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO Reports</i>.
    EMBO. <a href="https://doi.org/10.1038/sj.embor.7400889">https://doi.org/10.1038/sj.embor.7400889</a>
  chicago: Franz, Cerstin, Rudolf Walczak, Sevil Yavuz, Rachel Santarella, Marc Gentzel,
    Peter Askjaer, Vincent Galy, Martin Hetzer, Iain W Mattaj, and Wolfram Antonin.
    “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and
    Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>. EMBO, 2007. <a
    href="https://doi.org/10.1038/sj.embor.7400889">https://doi.org/10.1038/sj.embor.7400889</a>.
  ieee: C. Franz <i>et al.</i>, “MEL‐28/ELYS is required for the recruitment of nucleoporins
    to chromatin and postmitotic nuclear pore complex assembly,” <i>EMBO reports</i>,
    vol. 8, no. 2. EMBO, pp. 165–172, 2007.
  ista: Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, Galy V, Hetzer
    M, Mattaj IW, Antonin W. 2007. MEL‐28/ELYS is required for the recruitment of
    nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO
    reports. 8(2), 165–172.
  mla: Franz, Cerstin, et al. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins
    to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>,
    vol. 8, no. 2, EMBO, 2007, pp. 165–72, doi:<a href="https://doi.org/10.1038/sj.embor.7400889">10.1038/sj.embor.7400889</a>.
  short: C. Franz, R. Walczak, S. Yavuz, R. Santarella, M. Gentzel, P. Askjaer, V.
    Galy, M. Hetzer, I.W. Mattaj, W. Antonin, EMBO Reports 8 (2007) 165–172.
date_created: 2022-04-07T07:56:13Z
date_published: 2007-01-19T00:00:00Z
date_updated: 2022-07-18T08:56:40Z
day: '19'
doi: 10.1038/sj.embor.7400889
extern: '1'
external_id:
  pmid:
  - '17235358'
intvolume: '         8'
issue: '2'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/sj.embor.7400889
month: '01'
oa: 1
oa_version: Published Version
page: 165-172
pmid: 1
publication: EMBO reports
publication_identifier:
  eissn:
  - 1469-3178
  issn:
  - 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
scopus_import: '1'
status: public
title: MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and
  postmitotic nuclear pore complex assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 8
year: '2007'
...
---
_id: '8485'
abstract:
- lang: eng
  text: High signal to noise is a necessity for the quantification of NMR spectral
    parameters to be translated into accurate and precise restraints on protein structure
    and dynamics. An important source of long-range structural information is obtained
    from 1H–1H residual dipolar couplings (RDCs) measured for weakly aligned molecules.
    For sensitivity reasons, such measurements are generally performed on highly deuterated
    protein samples. Here we show that high sensitivity is also obtained for protonated
    protein samples if the pulse schemes are optimized in terms of longitudinal relaxation
    efficiency and J-mismatch compensated coherence transfer. The new sensitivity-optimized
    quantitative J-correlation experiment yields important signal gains reaching factors
    of 1.5 to 8 for individual correlation peaks when compared to previously proposed
    pulse schemes.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Ewen
  full_name: Lescop, Ewen
  last_name: Lescop
- first_name: Mirjam
  full_name: Falge, Mirjam
  last_name: Falge
- first_name: Rémy
  full_name: Sounier, Rémy
  last_name: Sounier
- first_name: Jérôme
  full_name: Boisbouvier, Jérôme
  last_name: Boisbouvier
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. Sensitivity-optimized
    experiment for the measurement of residual dipolar couplings between amide protons.
    <i>Journal of Biomolecular NMR</i>. 2007;38:47-55. doi:<a href="https://doi.org/10.1007/s10858-006-9138-2">10.1007/s10858-006-9138-2</a>
  apa: Schanda, P., Lescop, E., Falge, M., Sounier, R., Boisbouvier, J., &#38; Brutscher,
    B. (2007). Sensitivity-optimized experiment for the measurement of residual dipolar
    couplings between amide protons. <i>Journal of Biomolecular NMR</i>. Springer
    Nature. <a href="https://doi.org/10.1007/s10858-006-9138-2">https://doi.org/10.1007/s10858-006-9138-2</a>
  chicago: Schanda, Paul, Ewen Lescop, Mirjam Falge, Rémy Sounier, Jérôme Boisbouvier,
    and Bernhard Brutscher. “Sensitivity-Optimized Experiment for the Measurement
    of Residual Dipolar Couplings between Amide Protons.” <i>Journal of Biomolecular
    NMR</i>. Springer Nature, 2007. <a href="https://doi.org/10.1007/s10858-006-9138-2">https://doi.org/10.1007/s10858-006-9138-2</a>.
  ieee: P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, and B. Brutscher,
    “Sensitivity-optimized experiment for the measurement of residual dipolar couplings
    between amide protons,” <i>Journal of Biomolecular NMR</i>, vol. 38. Springer
    Nature, pp. 47–55, 2007.
  ista: Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. 2007.
    Sensitivity-optimized experiment for the measurement of residual dipolar couplings
    between amide protons. Journal of Biomolecular NMR. 38, 47–55.
  mla: Schanda, Paul, et al. “Sensitivity-Optimized Experiment for the Measurement
    of Residual Dipolar Couplings between Amide Protons.” <i>Journal of Biomolecular
    NMR</i>, vol. 38, Springer Nature, 2007, pp. 47–55, doi:<a href="https://doi.org/10.1007/s10858-006-9138-2">10.1007/s10858-006-9138-2</a>.
  short: P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, B. Brutscher,
    Journal of Biomolecular NMR 38 (2007) 47–55.
date_created: 2020-09-18T10:13:12Z
date_published: 2007-03-08T00:00:00Z
date_updated: 2021-01-12T08:19:36Z
day: '08'
doi: 10.1007/s10858-006-9138-2
extern: '1'
intvolume: '        38'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '03'
oa_version: None
page: 47-55
publication: Journal of Biomolecular NMR
publication_identifier:
  issn:
  - 0925-2738
  - 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Sensitivity-optimized experiment for the measurement of residual dipolar couplings
  between amide protons
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 38
year: '2007'
...
---
_id: '8486'
abstract:
- lang: eng
  text: A technique is described that allows reducing acquisition times of multidimensional
    NMR experiments by extensive spectral folding. The method is simple and has many
    interesting applications for NMR studies of molecular structure, dynamics, and
    kinetics.
article_processing_charge: No
article_type: original
author:
- first_name: Ewen
  full_name: Lescop, Ewen
  last_name: Lescop
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Rodolfo
  full_name: Rasia, Rodolfo
  last_name: Rasia
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Lescop E, Schanda P, Rasia R, Brutscher B. Automated spectral compression for
    fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy.
    <i>Journal of the American Chemical Society</i>. 2007;129(10):2756-2757. doi:<a
    href="https://doi.org/10.1021/ja068949u">10.1021/ja068949u</a>
  apa: Lescop, E., Schanda, P., Rasia, R., &#38; Brutscher, B. (2007). Automated spectral
    compression for fast multidimensional NMR and increased time resolution in real-time
    NMR spectroscopy. <i>Journal of the American Chemical Society</i>. American Chemical
    Society. <a href="https://doi.org/10.1021/ja068949u">https://doi.org/10.1021/ja068949u</a>
  chicago: Lescop, Ewen, Paul Schanda, Rodolfo Rasia, and Bernhard Brutscher. “Automated
    Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution
    in Real-Time NMR Spectroscopy.” <i>Journal of the American Chemical Society</i>.
    American Chemical Society, 2007. <a href="https://doi.org/10.1021/ja068949u">https://doi.org/10.1021/ja068949u</a>.
  ieee: E. Lescop, P. Schanda, R. Rasia, and B. Brutscher, “Automated spectral compression
    for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy,”
    <i>Journal of the American Chemical Society</i>, vol. 129, no. 10. American Chemical
    Society, pp. 2756–2757, 2007.
  ista: Lescop E, Schanda P, Rasia R, Brutscher B. 2007. Automated spectral compression
    for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy.
    Journal of the American Chemical Society. 129(10), 2756–2757.
  mla: Lescop, Ewen, et al. “Automated Spectral Compression for Fast Multidimensional
    NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.” <i>Journal of
    the American Chemical Society</i>, vol. 129, no. 10, American Chemical Society,
    2007, pp. 2756–57, doi:<a href="https://doi.org/10.1021/ja068949u">10.1021/ja068949u</a>.
  short: E. Lescop, P. Schanda, R. Rasia, B. Brutscher, Journal of the American Chemical
    Society 129 (2007) 2756–2757.
date_created: 2020-09-18T10:13:21Z
date_published: 2007-02-17T00:00:00Z
date_updated: 2021-01-12T08:19:36Z
day: '17'
doi: 10.1021/ja068949u
extern: '1'
intvolume: '       129'
issue: '10'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '02'
oa_version: None
page: 2756-2757
publication: Journal of the American Chemical Society
publication_identifier:
  issn:
  - 0002-7863
  - 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Automated spectral compression for fast multidimensional NMR and increased
  time resolution in real-time NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 129
year: '2007'
...
---
_id: '8487'
abstract:
- lang: eng
  text: Following unidirectional biophysical events such as the folding of proteins
    or the equilibration of binding interactions, requires experimental methods that
    yield information at both atomic-level resolution and at high repetition rates.
    Toward this end a number of different approaches enabling the rapid acquisition
    of 2D NMR spectra have been recently introduced, including spatially encoded “ultrafast”
    2D NMR spectroscopy and SOFAST HMQC NMR. Whereas the former accelerates acquisitions
    by reducing the number of scans that are necessary for completing arbitrary 2D
    NMR experiments, the latter operates by reducing the delay between consecutive
    scans while preserving sensitivity. Given the complementarities between these
    two approaches it seems natural to combine them into a single tool, enabling the
    acquisition of full 2D protein NMR spectra at high repetition rates. We demonstrate
    here this capability with the introduction of “ultraSOFAST” HMQC NMR, a spatially
    encoded and relaxation-optimized approach that can provide 2D protein correlation
    spectra at ∼1 s repetition rates for samples in the ∼2 mM concentration range.
    The principles, relative advantages, and current limitations of this new approach
    are discussed, and its application is exemplified with a study of the fast hydrogen−deuterium
    exchange characterizing amide sites in Ubiquitin.
article_processing_charge: No
article_type: original
author:
- first_name: Maayan
  full_name: Gal, Maayan
  last_name: Gal
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
- first_name: Lucio
  full_name: Frydman, Lucio
  last_name: Frydman
citation:
  ama: Gal M, Schanda P, Brutscher B, Frydman L. UltraSOFAST HMQC NMR and the repetitive
    acquisition of 2D protein spectra at Hz rates. <i>Journal of the American Chemical
    Society</i>. 2007;129(5):1372-1377. doi:<a href="https://doi.org/10.1021/ja066915g">10.1021/ja066915g</a>
  apa: Gal, M., Schanda, P., Brutscher, B., &#38; Frydman, L. (2007). UltraSOFAST
    HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. <i>Journal
    of the American Chemical Society</i>. American Chemical Society. <a href="https://doi.org/10.1021/ja066915g">https://doi.org/10.1021/ja066915g</a>
  chicago: Gal, Maayan, Paul Schanda, Bernhard Brutscher, and Lucio Frydman. “UltraSOFAST
    HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.” <i>Journal
    of the American Chemical Society</i>. American Chemical Society, 2007. <a href="https://doi.org/10.1021/ja066915g">https://doi.org/10.1021/ja066915g</a>.
  ieee: M. Gal, P. Schanda, B. Brutscher, and L. Frydman, “UltraSOFAST HMQC NMR and
    the repetitive acquisition of 2D protein spectra at Hz rates,” <i>Journal of the
    American Chemical Society</i>, vol. 129, no. 5. American Chemical Society, pp.
    1372–1377, 2007.
  ista: Gal M, Schanda P, Brutscher B, Frydman L. 2007. UltraSOFAST HMQC NMR and the
    repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American
    Chemical Society. 129(5), 1372–1377.
  mla: Gal, Maayan, et al. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of
    2D Protein Spectra at Hz Rates.” <i>Journal of the American Chemical Society</i>,
    vol. 129, no. 5, American Chemical Society, 2007, pp. 1372–77, doi:<a href="https://doi.org/10.1021/ja066915g">10.1021/ja066915g</a>.
  short: M. Gal, P. Schanda, B. Brutscher, L. Frydman, Journal of the American Chemical
    Society 129 (2007) 1372–1377.
date_created: 2020-09-18T10:13:27Z
date_published: 2007-01-10T00:00:00Z
date_updated: 2021-01-12T08:19:37Z
day: '10'
doi: 10.1021/ja066915g
extern: '1'
intvolume: '       129'
issue: '5'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '01'
oa_version: None
page: 1372-1377
publication: Journal of the American Chemical Society
publication_identifier:
  issn:
  - 0002-7863
  - 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at
  Hz rates
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 129
year: '2007'
...
---
_id: '8488'
abstract:
- lang: eng
  text: We demonstrate for different protein samples that three-dimensional HNCO and
    HNCA correlation spectra may be recorded in a few minutes acquisition time using
    the band-selective excitation short-transient sequences presented here. This opens
    new perspectives for the NMR structural investigation of unstable protein samples
    and real-time site-resolved studies of protein kinetics.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Hélène
  full_name: Van Melckebeke, Hélène
  last_name: Van Melckebeke
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Schanda P, Van Melckebeke H, Brutscher B. Speeding up three-dimensional protein
    NMR experiments to a few minutes. <i>Journal of the American Chemical Society</i>.
    2006;128(28):9042-9043. doi:<a href="https://doi.org/10.1021/ja062025p">10.1021/ja062025p</a>
  apa: Schanda, P., Van Melckebeke, H., &#38; Brutscher, B. (2006). Speeding up three-dimensional
    protein NMR experiments to a few minutes. <i>Journal of the American Chemical
    Society</i>. American Chemical Society. <a href="https://doi.org/10.1021/ja062025p">https://doi.org/10.1021/ja062025p</a>
  chicago: Schanda, Paul, Hélène Van Melckebeke, and Bernhard Brutscher. “Speeding
    up Three-Dimensional Protein NMR Experiments to a Few Minutes.” <i>Journal of
    the American Chemical Society</i>. American Chemical Society, 2006. <a href="https://doi.org/10.1021/ja062025p">https://doi.org/10.1021/ja062025p</a>.
  ieee: P. Schanda, H. Van Melckebeke, and B. Brutscher, “Speeding up three-dimensional
    protein NMR experiments to a few minutes,” <i>Journal of the American Chemical
    Society</i>, vol. 128, no. 28. American Chemical Society, pp. 9042–9043, 2006.
  ista: Schanda P, Van Melckebeke H, Brutscher B. 2006. Speeding up three-dimensional
    protein NMR experiments to a few minutes. Journal of the American Chemical Society.
    128(28), 9042–9043.
  mla: Schanda, Paul, et al. “Speeding up Three-Dimensional Protein NMR Experiments
    to a Few Minutes.” <i>Journal of the American Chemical Society</i>, vol. 128,
    no. 28, American Chemical Society, 2006, pp. 9042–43, doi:<a href="https://doi.org/10.1021/ja062025p">10.1021/ja062025p</a>.
  short: P. Schanda, H. Van Melckebeke, B. Brutscher, Journal of the American Chemical
    Society 128 (2006) 9042–9043.
date_created: 2020-09-18T10:13:36Z
date_published: 2006-06-21T00:00:00Z
date_updated: 2021-01-12T08:19:37Z
day: '21'
doi: 10.1021/ja062025p
extern: '1'
intvolume: '       128'
issue: '28'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '06'
oa_version: None
page: 9042-9043
publication: Journal of the American Chemical Society
publication_identifier:
  issn:
  - 0002-7863
  - 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Speeding up three-dimensional protein NMR experiments to a few minutes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 128
year: '2006'
...
---
_id: '8490'
abstract:
- lang: eng
  text: We demonstrate the feasibility of recording 1H–15N correlation spectra of
    proteins in only one second of acquisition time. The experiment combines recently
    proposed SOFAST-HMQC with Hadamard-type 15N frequency encoding. This allows site-resolved
    real-time NMR studies of kinetic processes in proteins with an increased time
    resolution. The sensitivity of the experiment is sufficient to be applicable to
    a wide range of molecular systems available at millimolar concentration on a high
    magnetic field spectrometer.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Schanda P, Brutscher B. Hadamard frequency-encoded SOFAST-HMQC for ultrafast
    two-dimensional protein NMR. <i>Journal of Magnetic Resonance</i>. 2006;178(2):334-339.
    doi:<a href="https://doi.org/10.1016/j.jmr.2005.10.007">10.1016/j.jmr.2005.10.007</a>
  apa: Schanda, P., &#38; Brutscher, B. (2006). Hadamard frequency-encoded SOFAST-HMQC
    for ultrafast two-dimensional protein NMR. <i>Journal of Magnetic Resonance</i>.
    Elsevier. <a href="https://doi.org/10.1016/j.jmr.2005.10.007">https://doi.org/10.1016/j.jmr.2005.10.007</a>
  chicago: Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC
    for Ultrafast Two-Dimensional Protein NMR.” <i>Journal of Magnetic Resonance</i>.
    Elsevier, 2006. <a href="https://doi.org/10.1016/j.jmr.2005.10.007">https://doi.org/10.1016/j.jmr.2005.10.007</a>.
  ieee: P. Schanda and B. Brutscher, “Hadamard frequency-encoded SOFAST-HMQC for ultrafast
    two-dimensional protein NMR,” <i>Journal of Magnetic Resonance</i>, vol. 178,
    no. 2. Elsevier, pp. 334–339, 2006.
  ista: Schanda P, Brutscher B. 2006. Hadamard frequency-encoded SOFAST-HMQC for ultrafast
    two-dimensional protein NMR. Journal of Magnetic Resonance. 178(2), 334–339.
  mla: Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC
    for Ultrafast Two-Dimensional Protein NMR.” <i>Journal of Magnetic Resonance</i>,
    vol. 178, no. 2, Elsevier, 2006, pp. 334–39, doi:<a href="https://doi.org/10.1016/j.jmr.2005.10.007">10.1016/j.jmr.2005.10.007</a>.
  short: P. Schanda, B. Brutscher, Journal of Magnetic Resonance 178 (2006) 334–339.
date_created: 2020-09-18T10:13:51Z
date_published: 2006-02-01T00:00:00Z
date_updated: 2021-01-12T08:19:38Z
day: '01'
doi: 10.1016/j.jmr.2005.10.007
extern: '1'
intvolume: '       178'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '02'
oa_version: None
page: 334-339
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
status: public
title: Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein
  NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 178
year: '2006'
...
---
_id: '13428'
abstract:
- lang: eng
  text: Mixtures of oppositely charged nanoparticles of various sizes and charge ratios
    precipitate only at the point of electroneutrality. This phenomenonspecific to
    the nanoscale and reminiscent of threshold precipitation of ionsis a consequence
    of the formation of core-and-shell nanoparticle aggregates, in which the shells
    are composed of like-charged particles and are stabilized by efficient electrostatic
    screening.
article_processing_charge: No
article_type: original
author:
- first_name: Alexander M.
  full_name: Kalsin, Alexander M.
  last_name: Kalsin
- first_name: Bartlomiej
  full_name: Kowalczyk, Bartlomiej
  last_name: Kowalczyk
- first_name: Stoyan K.
  full_name: Smoukov, Stoyan K.
  last_name: Smoukov
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
- first_name: Bartosz A.
  full_name: Grzybowski, Bartosz A.
  last_name: Grzybowski
citation:
  ama: Kalsin AM, Kowalczyk B, Smoukov SK, Klajn R, Grzybowski BA. Ionic-like behavior
    of oppositely charged nanoparticles. <i>Journal of the American Chemical Society</i>.
    2006;128(47):15046-15047. doi:<a href="https://doi.org/10.1021/ja0642966">10.1021/ja0642966</a>
  apa: Kalsin, A. M., Kowalczyk, B., Smoukov, S. K., Klajn, R., &#38; Grzybowski,
    B. A. (2006). Ionic-like behavior of oppositely charged nanoparticles. <i>Journal
    of the American Chemical Society</i>. American Chemical Society. <a href="https://doi.org/10.1021/ja0642966">https://doi.org/10.1021/ja0642966</a>
  chicago: Kalsin, Alexander M., Bartlomiej Kowalczyk, Stoyan K. Smoukov, Rafal Klajn,
    and Bartosz A. Grzybowski. “Ionic-like Behavior of Oppositely Charged Nanoparticles.”
    <i>Journal of the American Chemical Society</i>. American Chemical Society, 2006.
    <a href="https://doi.org/10.1021/ja0642966">https://doi.org/10.1021/ja0642966</a>.
  ieee: A. M. Kalsin, B. Kowalczyk, S. K. Smoukov, R. Klajn, and B. A. Grzybowski,
    “Ionic-like behavior of oppositely charged nanoparticles,” <i>Journal of the American
    Chemical Society</i>, vol. 128, no. 47. American Chemical Society, pp. 15046–15047,
    2006.
  ista: Kalsin AM, Kowalczyk B, Smoukov SK, Klajn R, Grzybowski BA. 2006. Ionic-like
    behavior of oppositely charged nanoparticles. Journal of the American Chemical
    Society. 128(47), 15046–15047.
  mla: Kalsin, Alexander M., et al. “Ionic-like Behavior of Oppositely Charged Nanoparticles.”
    <i>Journal of the American Chemical Society</i>, vol. 128, no. 47, American Chemical
    Society, 2006, pp. 15046–47, doi:<a href="https://doi.org/10.1021/ja0642966">10.1021/ja0642966</a>.
  short: A.M. Kalsin, B. Kowalczyk, S.K. Smoukov, R. Klajn, B.A. Grzybowski, Journal
    of the American Chemical Society 128 (2006) 15046–15047.
date_created: 2023-08-01T10:36:27Z
date_published: 2006-11-29T00:00:00Z
date_updated: 2023-08-08T11:30:06Z
day: '29'
doi: 10.1021/ja0642966
extern: '1'
external_id:
  pmid:
  - '17117829'
intvolume: '       128'
issue: '47'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '11'
oa_version: None
page: 15046-15047
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
  eissn:
  - 1520-5126
  issn:
  - 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Ionic-like behavior of oppositely charged nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 128
year: '2006'
...
---
_id: '8491'
abstract:
- lang: eng
  text: Fast multidimensional NMR with a time resolution of a few seconds provides
    a new tool for high throughput screening and site-resolved real-time studies of
    kinetic molecular processes by NMR. Recently we have demonstrated the feasibility
    to record protein 1H–15N correlation spectra in a few seconds of acquisition time
    using a new SOFAST-HMQC experiment (Schanda and Brutscher (2005) J. Am. Chem.
    Soc. 127, 8014). Here, we investigate in detail the performance of SOFAST-HMQC
    to record 1H–15N and 1H−13C correlation spectra of proteins of different size
    and at different magnetic field strengths. Compared to standard 1H–15N correlation
    experiments SOFAST-HMQC provides a significant gain in sensitivity, especially
    for fast repetition rates. Guidelines are provided on how to set up SOFAST-HMQC
    experiments for a given protein sample. In addition, an alternative pulse scheme,
    IPAP-SOFAST-HMQC is presented that allows application on NMR spectrometers equipped
    with cryogenic probes, and fast measurement of one-bond 1H–13C and 1H–15N scalar
    and residual dipolar coupling constants.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Ēriks
  full_name: Kupče, Ēriks
  last_name: Kupče
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Schanda P, Kupče Ē, Brutscher B. SOFAST-HMQC experiments for recording two-dimensional
    deteronuclear correlation spectra of proteins within a few seconds. <i>Journal
    of Biomolecular NMR</i>. 2005;33(4):199-211. doi:<a href="https://doi.org/10.1007/s10858-005-4425-x">10.1007/s10858-005-4425-x</a>
  apa: Schanda, P., Kupče, Ē., &#38; Brutscher, B. (2005). SOFAST-HMQC experiments
    for recording two-dimensional deteronuclear correlation spectra of proteins within
    a few seconds. <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href="https://doi.org/10.1007/s10858-005-4425-x">https://doi.org/10.1007/s10858-005-4425-x</a>
  chicago: Schanda, Paul, Ēriks Kupče, and Bernhard Brutscher. “SOFAST-HMQC Experiments
    for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within
    a Few Seconds.” <i>Journal of Biomolecular NMR</i>. Springer Nature, 2005. <a
    href="https://doi.org/10.1007/s10858-005-4425-x">https://doi.org/10.1007/s10858-005-4425-x</a>.
  ieee: P. Schanda, Ē. Kupče, and B. Brutscher, “SOFAST-HMQC experiments for recording
    two-dimensional deteronuclear correlation spectra of proteins within a few seconds,”
    <i>Journal of Biomolecular NMR</i>, vol. 33, no. 4. Springer Nature, pp. 199–211,
    2005.
  ista: Schanda P, Kupče Ē, Brutscher B. 2005. SOFAST-HMQC experiments for recording
    two-dimensional deteronuclear correlation spectra of proteins within a few seconds.
    Journal of Biomolecular NMR. 33(4), 199–211.
  mla: Schanda, Paul, et al. “SOFAST-HMQC Experiments for Recording Two-Dimensional
    Deteronuclear Correlation Spectra of Proteins within a Few Seconds.” <i>Journal
    of Biomolecular NMR</i>, vol. 33, no. 4, Springer Nature, 2005, pp. 199–211, doi:<a
    href="https://doi.org/10.1007/s10858-005-4425-x">10.1007/s10858-005-4425-x</a>.
  short: P. Schanda, Ē. Kupče, B. Brutscher, Journal of Biomolecular NMR 33 (2005)
    199–211.
date_created: 2020-09-18T10:13:59Z
date_published: 2005-12-01T00:00:00Z
date_updated: 2021-01-12T08:19:38Z
day: '01'
doi: 10.1007/s10858-005-4425-x
extern: '1'
intvolume: '        33'
issue: '4'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '12'
oa_version: None
page: 199-211
publication: Journal of Biomolecular NMR
publication_identifier:
  issn:
  - 0925-2738
  - 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation
  spectra of proteins within a few seconds
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 33
year: '2005'
...
---
_id: '8492'
abstract:
- lang: eng
  text: We demonstrate for different protein samples that 2D 1H−15N correlation NMR
    spectra can be recorded in a few seconds of acquisition time using a new band-selective
    optimized flip-angle short-transient heteronuclear multiple quantum coherence
    experiment. This has enabled us to measure fast hydrogen−deuterium exchange rate
    constants along the backbone of a small globular protein fragment by real-time
    2D NMR.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Schanda P, Brutscher B. Very fast two-dimensional NMR spectroscopy for real-time
    investigation of dynamic events in proteins on the time scale of seconds. <i>Journal
    of the American Chemical Society</i>. 2005;127(22):8014-8015. doi:<a href="https://doi.org/10.1021/ja051306e">10.1021/ja051306e</a>
  apa: Schanda, P., &#38; Brutscher, B. (2005). Very fast two-dimensional NMR spectroscopy
    for real-time investigation of dynamic events in proteins on the time scale of
    seconds. <i>Journal of the American Chemical Society</i>. American Chemical Society.
    <a href="https://doi.org/10.1021/ja051306e">https://doi.org/10.1021/ja051306e</a>
  chicago: Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy
    for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of
    Seconds.” <i>Journal of the American Chemical Society</i>. American Chemical Society,
    2005. <a href="https://doi.org/10.1021/ja051306e">https://doi.org/10.1021/ja051306e</a>.
  ieee: P. Schanda and B. Brutscher, “Very fast two-dimensional NMR spectroscopy for
    real-time investigation of dynamic events in proteins on the time scale of seconds,”
    <i>Journal of the American Chemical Society</i>, vol. 127, no. 22. American Chemical
    Society, pp. 8014–8015, 2005.
  ista: Schanda P, Brutscher B. 2005. Very fast two-dimensional NMR spectroscopy for
    real-time investigation of dynamic events in proteins on the time scale of seconds.
    Journal of the American Chemical Society. 127(22), 8014–8015.
  mla: Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy
    for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of
    Seconds.” <i>Journal of the American Chemical Society</i>, vol. 127, no. 22, American
    Chemical Society, 2005, pp. 8014–15, doi:<a href="https://doi.org/10.1021/ja051306e">10.1021/ja051306e</a>.
  short: P. Schanda, B. Brutscher, Journal of the American Chemical Society 127 (2005)
    8014–8015.
date_created: 2020-09-18T10:14:05Z
date_published: 2005-05-14T00:00:00Z
date_updated: 2021-01-12T08:19:39Z
day: '14'
doi: 10.1021/ja051306e
extern: '1'
intvolume: '       127'
issue: '22'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '05'
oa_version: None
page: 8014-8015
publication: Journal of the American Chemical Society
publication_identifier:
  issn:
  - 0002-7863
  - 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic
  events in proteins on the time scale of seconds
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 127
year: '2005'
...
---
_id: '12203'
abstract:
- lang: eng
  text: 'Geranylgeranyl diphosphate synthase (GGPPS, EC: 2.5.1.29) catalyzes the biosynthesis
    of geranylgeranyl diphosphate (GGPP), which is a key precursor for ginkgolide
    biosynthesis. Here we reported for the first time the cloning of a new full-length
    cDNA encoding GGPPS from the living fossil plant Ginkgo biloba. The full-length
    cDNA encoding G. biloba GGPPS (designated as GbGGPPS) was 1657bp long and contained
    a 1176bp open reading frame encoding a 391 amino acid protein. Comparative analysis
    showed that GbGGPPS possessed a 79 amino acid transit peptide at its N-terminal,
    which directed GbGGPPS to target to the plastids. Bioinformatic analysis revealed
    that GbGGPPS was a member of polyprenyltransferases with two highly conserved
    aspartate-rich motifs like other plant GGPPSs. Phylogenetic tree analysis indicated
    that plant GGPPSs could be classified into two groups, angiosperm and gymnosperm
    GGPPSs, while GbGGPPS had closer relationship with gymnosperm plant GGPPSs.'
acknowledgement: This study was financially supported by China National High-Tech
  “863” Program. The authors are very thankful to Dr Li Wang (School of Life Sciences,
  Fudan University, Shanghai, China) for her kind help with constructing the phylogenetic
  tree.
article_processing_charge: No
article_type: original
author:
- first_name: Zhihua
  full_name: Liao, Zhihua
  last_name: Liao
- first_name: Min
  full_name: Chen, Min
  last_name: Chen
- first_name: Yifu
  full_name: Gong, Yifu
  last_name: Gong
- first_name: Liang
  full_name: Guo, Liang
  last_name: Guo
- first_name: Qiumin
  full_name: Tan, Qiumin
  last_name: Tan
- first_name: Xiaoqi
  full_name: Feng, Xiaoqi
  id: e0164712-22ee-11ed-b12a-d80fcdf35958
  last_name: Feng
  orcid: 0000-0002-4008-1234
- first_name: Xiaofen
  full_name: Sun, Xiaofen
  last_name: Sun
- first_name: Feng
  full_name: Tan, Feng
  last_name: Tan
- first_name: Kexuan
  full_name: Tang, Kexuan
  last_name: Tang
citation:
  ama: Liao Z, Chen M, Gong Y, et al. A new geranylgeranyl Diphosphate synthase gene
    from Ginkgo biloba, which intermediates the biosynthesis of the key precursor
    for ginkgolides. <i>DNA Sequence</i>. 2004;15(2):153-158. doi:<a href="https://doi.org/10.1080/10425170410001667348">10.1080/10425170410001667348</a>
  apa: Liao, Z., Chen, M., Gong, Y., Guo, L., Tan, Q., Feng, X., … Tang, K. (2004).
    A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates
    the biosynthesis of the key precursor for ginkgolides. <i>DNA Sequence</i>. Informa
    UK Limited. <a href="https://doi.org/10.1080/10425170410001667348">https://doi.org/10.1080/10425170410001667348</a>
  chicago: Liao, Zhihua, Min Chen, Yifu Gong, Liang Guo, Qiumin Tan, Xiaoqi Feng,
    Xiaofen Sun, Feng Tan, and Kexuan Tang. “A New Geranylgeranyl Diphosphate Synthase
    Gene from Ginkgo Biloba, Which Intermediates the Biosynthesis of the Key Precursor
    for Ginkgolides.” <i>DNA Sequence</i>. Informa UK Limited, 2004. <a href="https://doi.org/10.1080/10425170410001667348">https://doi.org/10.1080/10425170410001667348</a>.
  ieee: Z. Liao <i>et al.</i>, “A new geranylgeranyl Diphosphate synthase gene from
    Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides,”
    <i>DNA Sequence</i>, vol. 15, no. 2. Informa UK Limited, pp. 153–158, 2004.
  ista: Liao Z, Chen M, Gong Y, Guo L, Tan Q, Feng X, Sun X, Tan F, Tang K. 2004.
    A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates
    the biosynthesis of the key precursor for ginkgolides. DNA Sequence. 15(2), 153–158.
  mla: Liao, Zhihua, et al. “A New Geranylgeranyl Diphosphate Synthase Gene from Ginkgo
    Biloba, Which Intermediates the Biosynthesis of the Key Precursor for Ginkgolides.”
    <i>DNA Sequence</i>, vol. 15, no. 2, Informa UK Limited, 2004, pp. 153–58, doi:<a
    href="https://doi.org/10.1080/10425170410001667348">10.1080/10425170410001667348</a>.
  short: Z. Liao, M. Chen, Y. Gong, L. Guo, Q. Tan, X. Feng, X. Sun, F. Tan, K. Tang,
    DNA Sequence 15 (2004) 153–158.
date_created: 2023-01-16T09:24:50Z
date_published: 2004-01-01T00:00:00Z
date_updated: 2023-05-08T10:58:29Z
department:
- _id: XiFe
doi: 10.1080/10425170410001667348
extern: '1'
external_id:
  pmid:
  - '15352294'
intvolume: '        15'
issue: '2'
keyword:
- Endocrinology
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
oa_version: None
page: 153-158
pmid: 1
publication: DNA Sequence
publication_identifier:
  issn:
  - 1042-5179
publication_status: published
publisher: Informa UK Limited
quality_controlled: '1'
scopus_import: '1'
status: public
title: A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates
  the biosynthesis of the key precursor for ginkgolides
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 15
year: '2004'
...
---
_id: '11122'
abstract:
- lang: eng
  text: Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow
    traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes,
    the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble
    and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate
    a function for the conserved Nup107-160 complex in this process. Partial in vivo
    depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels
    of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion
    of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced
    nuclei with a continuous NE but no NPCs. This phenotype was reversible only if
    Nup107-160 complex was readded before closed NE formation. Depletion also prevented
    association of FG-repeat nucleoporins with chromatin. We propose a stepwise model
    in which postmitotic NPC assembly initiates on chromatin via early recruitment
    of the Nup107-160 complex.
article_processing_charge: No
article_type: original
author:
- first_name: Tobias C.
  full_name: Walther, Tobias C.
  last_name: Walther
- first_name: Annabelle
  full_name: Alves, Annabelle
  last_name: Alves
- first_name: Helen
  full_name: Pickersgill, Helen
  last_name: Pickersgill
- first_name: Isabelle
  full_name: Loı̈odice, Isabelle
  last_name: Loı̈odice
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
- first_name: Vincent
  full_name: Galy, Vincent
  last_name: Galy
- first_name: Bastian B.
  full_name: Hülsmann, Bastian B.
  last_name: Hülsmann
- first_name: Thomas
  full_name: Köcher, Thomas
  last_name: Köcher
- first_name: Matthias
  full_name: Wilm, Matthias
  last_name: Wilm
- first_name: Terry
  full_name: Allen, Terry
  last_name: Allen
- first_name: Iain W.
  full_name: Mattaj, Iain W.
  last_name: Mattaj
- first_name: Valérie
  full_name: Doye, Valérie
  last_name: Doye
citation:
  ama: Walther TC, Alves A, Pickersgill H, et al. The conserved Nup107-160 complex
    is critical for nuclear pore complex assembly. <i>Cell</i>. 2003;113(2):195-206.
    doi:<a href="https://doi.org/10.1016/s0092-8674(03)00235-6">10.1016/s0092-8674(03)00235-6</a>
  apa: Walther, T. C., Alves, A., Pickersgill, H., Loı̈odice, I., Hetzer, M., Galy,
    V., … Doye, V. (2003). The conserved Nup107-160 complex is critical for nuclear
    pore complex assembly. <i>Cell</i>. Elsevier. <a href="https://doi.org/10.1016/s0092-8674(03)00235-6">https://doi.org/10.1016/s0092-8674(03)00235-6</a>
  chicago: Walther, Tobias C., Annabelle Alves, Helen Pickersgill, Isabelle Loı̈odice,
    Martin Hetzer, Vincent Galy, Bastian B. Hülsmann, et al. “The Conserved Nup107-160
    Complex Is Critical for Nuclear Pore Complex Assembly.” <i>Cell</i>. Elsevier,
    2003. <a href="https://doi.org/10.1016/s0092-8674(03)00235-6">https://doi.org/10.1016/s0092-8674(03)00235-6</a>.
  ieee: T. C. Walther <i>et al.</i>, “The conserved Nup107-160 complex is critical
    for nuclear pore complex assembly,” <i>Cell</i>, vol. 113, no. 2. Elsevier, pp.
    195–206, 2003.
  ista: Walther TC, Alves A, Pickersgill H, Loı̈odice I, Hetzer M, Galy V, Hülsmann
    BB, Köcher T, Wilm M, Allen T, Mattaj IW, Doye V. 2003. The conserved Nup107-160
    complex is critical for nuclear pore complex assembly. Cell. 113(2), 195–206.
  mla: Walther, Tobias C., et al. “The Conserved Nup107-160 Complex Is Critical for
    Nuclear Pore Complex Assembly.” <i>Cell</i>, vol. 113, no. 2, Elsevier, 2003,
    pp. 195–206, doi:<a href="https://doi.org/10.1016/s0092-8674(03)00235-6">10.1016/s0092-8674(03)00235-6</a>.
  short: T.C. Walther, A. Alves, H. Pickersgill, I. Loı̈odice, M. Hetzer, V. Galy,
    B.B. Hülsmann, T. Köcher, M. Wilm, T. Allen, I.W. Mattaj, V. Doye, Cell 113 (2003)
    195–206.
date_created: 2022-04-07T07:57:10Z
date_published: 2003-04-17T00:00:00Z
date_updated: 2022-07-18T08:57:42Z
day: '17'
doi: 10.1016/s0092-8674(03)00235-6
extern: '1'
external_id:
  pmid:
  - '12705868'
intvolume: '       113'
issue: '2'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '04'
oa_version: Published Version
page: 195-206
pmid: 1
publication: Cell
publication_identifier:
  issn:
  - 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The conserved Nup107-160 complex is critical for nuclear pore complex assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 113
year: '2003'
...
---
_id: '13436'
abstract:
- lang: eng
  text: Cross-metathesis reactions of α,β-unsaturated sulfones and sulfoxides in the
    presence of molybdenum and ruthenium pre-catalysts were tested. A selective metahesis
    reaction was achieved between functionalized terminal olefins and vinyl sulfones
    by using the ‘second generation’ ruthenium catalysts 1c–h while the highly active
    Schrock catalyst 1b was found to be functional group incompatible with vinyl sulfones.
    The cross-metathesis products were isolated in good yields with an excellent (E)-selectivity.
    Both the molybdenum and ruthenium-based complexes were, however, incompatible
    with α,β- and β,γ-unsaturated sulfoxides.
article_processing_charge: No
article_type: original
author:
- first_name: Anna
  full_name: Michrowska, Anna
  last_name: Michrowska
- first_name: Michał
  full_name: Bieniek, Michał
  last_name: Bieniek
- first_name: Mikhail
  full_name: Kim, Mikhail
  last_name: Kim
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
- first_name: Karol
  full_name: Grela, Karol
  last_name: Grela
citation:
  ama: Michrowska A, Bieniek M, Kim M, Klajn R, Grela K. Cross-metathesis reaction
    of vinyl sulfones and sulfoxides. <i>Tetrahedron</i>. 2003;59(25):4525-4531. doi:<a
    href="https://doi.org/10.1016/s0040-4020(03)00682-3">10.1016/s0040-4020(03)00682-3</a>
  apa: Michrowska, A., Bieniek, M., Kim, M., Klajn, R., &#38; Grela, K. (2003). Cross-metathesis
    reaction of vinyl sulfones and sulfoxides. <i>Tetrahedron</i>. Elsevier. <a href="https://doi.org/10.1016/s0040-4020(03)00682-3">https://doi.org/10.1016/s0040-4020(03)00682-3</a>
  chicago: Michrowska, Anna, Michał Bieniek, Mikhail Kim, Rafal Klajn, and Karol Grela.
    “Cross-Metathesis Reaction of Vinyl Sulfones and Sulfoxides.” <i>Tetrahedron</i>.
    Elsevier, 2003. <a href="https://doi.org/10.1016/s0040-4020(03)00682-3">https://doi.org/10.1016/s0040-4020(03)00682-3</a>.
  ieee: A. Michrowska, M. Bieniek, M. Kim, R. Klajn, and K. Grela, “Cross-metathesis
    reaction of vinyl sulfones and sulfoxides,” <i>Tetrahedron</i>, vol. 59, no. 25.
    Elsevier, pp. 4525–4531, 2003.
  ista: Michrowska A, Bieniek M, Kim M, Klajn R, Grela K. 2003. Cross-metathesis reaction
    of vinyl sulfones and sulfoxides. Tetrahedron. 59(25), 4525–4531.
  mla: Michrowska, Anna, et al. “Cross-Metathesis Reaction of Vinyl Sulfones and Sulfoxides.”
    <i>Tetrahedron</i>, vol. 59, no. 25, Elsevier, 2003, pp. 4525–31, doi:<a href="https://doi.org/10.1016/s0040-4020(03)00682-3">10.1016/s0040-4020(03)00682-3</a>.
  short: A. Michrowska, M. Bieniek, M. Kim, R. Klajn, K. Grela, Tetrahedron 59 (2003)
    4525–4531.
date_created: 2023-08-01T10:39:34Z
date_published: 2003-06-16T00:00:00Z
date_updated: 2023-08-08T12:44:17Z
day: '16'
doi: 10.1016/s0040-4020(03)00682-3
extern: '1'
intvolume: '        59'
issue: '25'
keyword:
- Organic Chemistry
- Drug Discovery
- Biochemistry
language:
- iso: eng
month: '06'
oa_version: None
page: 4525-4531
publication: Tetrahedron
publication_identifier:
  eissn:
  - 1464-5416
  issn:
  - 0040-4020
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cross-metathesis reaction of vinyl sulfones and sulfoxides
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 59
year: '2003'
...
---
_id: '11124'
abstract:
- lang: eng
  text: Ran GTPase plays important roles in nucleocytoplasmic transport in interphase
    [1, 2] and in both spindle formation and nuclear envelope (NE) assembly during
    mitosis [3, 4, 5]. The latter functions rely on the presence of high local concentrations
    of GTP-bound Ran near mitotic chromatin [3, 4, 5]. RanGTP localization has been
    proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1,
    with chromatin [6, 7, 8, 9], but Ran is shown here to bind directly to chromatin
    in two modes, either dependent or independent of RCC1, and, where bound, to increase
    the affinity of chromatin for NE membranes. We propose that the Ran binding capacity
    of chromatin contributes to localized spindle and NE assembly.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Daniel
  full_name: Bilbao-Cortés, Daniel
  last_name: Bilbao-Cortés
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
- first_name: Gernot
  full_name: Längst, Gernot
  last_name: Längst
- first_name: Peter B.
  full_name: Becker, Peter B.
  last_name: Becker
- first_name: Iain W.
  full_name: Mattaj, Iain W.
  last_name: Mattaj
citation:
  ama: Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. Ran binds to chromatin
    by two distinct mechanisms. <i>Current Biology</i>. 2002;12(13):1151-1156. doi:<a
    href="https://doi.org/10.1016/s0960-9822(02)00927-2">10.1016/s0960-9822(02)00927-2</a>
  apa: Bilbao-Cortés, D., Hetzer, M., Längst, G., Becker, P. B., &#38; Mattaj, I.
    W. (2002). Ran binds to chromatin by two distinct mechanisms. <i>Current Biology</i>.
    Elsevier BV. <a href="https://doi.org/10.1016/s0960-9822(02)00927-2">https://doi.org/10.1016/s0960-9822(02)00927-2</a>
  chicago: Bilbao-Cortés, Daniel, Martin Hetzer, Gernot Längst, Peter B. Becker, and
    Iain W. Mattaj. “Ran Binds to Chromatin by Two Distinct Mechanisms.” <i>Current
    Biology</i>. Elsevier BV, 2002. <a href="https://doi.org/10.1016/s0960-9822(02)00927-2">https://doi.org/10.1016/s0960-9822(02)00927-2</a>.
  ieee: D. Bilbao-Cortés, M. Hetzer, G. Längst, P. B. Becker, and I. W. Mattaj, “Ran
    binds to chromatin by two distinct mechanisms,” <i>Current Biology</i>, vol. 12,
    no. 13. Elsevier BV, pp. 1151–1156, 2002.
  ista: Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. 2002. Ran binds
    to chromatin by two distinct mechanisms. Current Biology. 12(13), 1151–1156.
  mla: Bilbao-Cortés, Daniel, et al. “Ran Binds to Chromatin by Two Distinct Mechanisms.”
    <i>Current Biology</i>, vol. 12, no. 13, Elsevier BV, 2002, pp. 1151–56, doi:<a
    href="https://doi.org/10.1016/s0960-9822(02)00927-2">10.1016/s0960-9822(02)00927-2</a>.
  short: D. Bilbao-Cortés, M. Hetzer, G. Längst, P.B. Becker, I.W. Mattaj, Current
    Biology 12 (2002) 1151–1156.
date_created: 2022-04-07T07:57:31Z
date_published: 2002-07-09T00:00:00Z
date_updated: 2022-07-18T08:58:05Z
day: '09'
doi: 10.1016/s0960-9822(02)00927-2
extern: '1'
external_id:
  pmid:
  - '12121625'
intvolume: '        12'
issue: '13'
keyword:
- General Agricultural and Biological Sciences
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/S0960-9822(02)00927-2
month: '07'
oa: 1
oa_version: Published Version
page: 1151-1156
pmid: 1
publication: Current Biology
publication_identifier:
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier BV
quality_controlled: '1'
scopus_import: '1'
status: public
title: Ran binds to chromatin by two distinct mechanisms
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 12
year: '2002'
...
---
_id: '13438'
abstract:
- lang: eng
  text: ICln is an ion channel identified by expression cloning using a cDNA library
    from Madin-Darby canine kidney cells. In all organisms tested so far, only one
    transcript for the ICln protein could be identified. Here we show that two splice
    variants of the ICln ion channel can be found in Caenorhabditis elegans. Moreover,
    we show that these two splice variants of the ICln channel protein, which we termed
    IClnN1 and IClnN2, can be functionally reconstituted and tested in an artificial
    lipid bilayer. In these experiments, the IClnN1-induced currents showed no voltage-dependent
    inactivation, whereas the IClnN2-induced currents fully inactivated at positive
    potentials. The molecular entity responsible for the voltage-dependent inactivation
    of IClnN2 is a cluster of positively charged amino acids encoded by exon 2a, which
    is absent in IClnN1. Our experiments suggest a mechanism of channel inactivation
    that is similar to the “ball and chain” model proposed for the Shaker potassium
    channel,i.e. a cluster of positively charged amino acids hinders ion permeation
    through the channel by a molecular and voltage-dependent interaction at the inner
    vestibulum of the pore. This hypothesis is supported by the finding that synthetic
    peptides with the same amino acid sequence as the positive cluster can transform
    the IClnN1-induced current to the current observed after reconstitution of IClnN2.
    Furthermore, we show that the nematode ICln gene is embedded in an operon harboring
    two additional genes, which we termed Nx and Ny. Co-reconstitution of Nx and IClnN2
    and functional analysis of the related currents revealed a functional interaction
    between the two proteins, as evidenced by the fact that the IClnN2-induced current
    in the presence of Nx was no longer voltage-sensitive. The experiments described
    indicate that the genome organization in nematodes allows an effective approach
    for the identification of functional partner proteins of ion channels.
acknowledgement: We are grateful to D. E. Clapham, E. Wöll, G. Meyer, and G. Botta
  for helpful discussion and/or reading of the manuscript. We also thank T. Stiernagle
  for providing the N2 strain of C. elegans and A. Wimmer and M. Frick for technical
  assistance
article_processing_charge: No
article_type: original
author:
- first_name: Johannes
  full_name: Fürst, Johannes
  last_name: Fürst
- first_name: Markus
  full_name: Ritter, Markus
  last_name: Ritter
- first_name: Jakob
  full_name: Rudzki, Jakob
  last_name: Rudzki
- first_name: Johann G
  full_name: Danzl, Johann G
  id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
  last_name: Danzl
  orcid: 0000-0001-8559-3973
- first_name: Martin
  full_name: Gschwentner, Martin
  last_name: Gschwentner
- first_name: Elke
  full_name: Scandella, Elke
  last_name: Scandella
- first_name: Martin
  full_name: Jakab, Martin
  last_name: Jakab
- first_name: Matthias
  full_name: König, Matthias
  last_name: König
- first_name: Bernhard
  full_name: Oehl, Bernhard
  last_name: Oehl
- first_name: Florian
  full_name: Lang, Florian
  last_name: Lang
- first_name: Peter
  full_name: Deetjen, Peter
  last_name: Deetjen
- first_name: Markus
  full_name: Paulmichl, Markus
  last_name: Paulmichl
citation:
  ama: Fürst J, Ritter M, Rudzki J, et al. ICln Ion channel splice variants in Caenorhabditis
    elegans. <i>Journal of Biological Chemistry</i>. 2002;277(6):4435-4445. doi:<a
    href="https://doi.org/10.1074/jbc.m107372200">10.1074/jbc.m107372200</a>
  apa: Fürst, J., Ritter, M., Rudzki, J., Danzl, J. G., Gschwentner, M., Scandella,
    E., … Paulmichl, M. (2002). ICln Ion channel splice variants in Caenorhabditis
    elegans. <i>Journal of Biological Chemistry</i>. Elsevier. <a href="https://doi.org/10.1074/jbc.m107372200">https://doi.org/10.1074/jbc.m107372200</a>
  chicago: Fürst, Johannes, Markus Ritter, Jakob Rudzki, Johann G Danzl, Martin Gschwentner,
    Elke Scandella, Martin Jakab, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
    Elegans.” <i>Journal of Biological Chemistry</i>. Elsevier, 2002. <a href="https://doi.org/10.1074/jbc.m107372200">https://doi.org/10.1074/jbc.m107372200</a>.
  ieee: J. Fürst <i>et al.</i>, “ICln Ion channel splice variants in Caenorhabditis
    elegans,” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6. Elsevier, pp.
    4435–4445, 2002.
  ista: Fürst J, Ritter M, Rudzki J, Danzl JG, Gschwentner M, Scandella E, Jakab M,
    König M, Oehl B, Lang F, Deetjen P, Paulmichl M. 2002. ICln Ion channel splice
    variants in Caenorhabditis elegans. Journal of Biological Chemistry. 277(6), 4435–4445.
  mla: Fürst, Johannes, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
    Elegans.” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6, Elsevier, 2002,
    pp. 4435–45, doi:<a href="https://doi.org/10.1074/jbc.m107372200">10.1074/jbc.m107372200</a>.
  short: J. Fürst, M. Ritter, J. Rudzki, J.G. Danzl, M. Gschwentner, E. Scandella,
    M. Jakab, M. König, B. Oehl, F. Lang, P. Deetjen, M. Paulmichl, Journal of Biological
    Chemistry 277 (2002) 4435–4445.
date_created: 2023-08-01T12:37:50Z
date_published: 2002-02-08T00:00:00Z
date_updated: 2023-08-01T12:55:54Z
day: '08'
ddc:
- '570'
doi: 10.1074/jbc.m107372200
extern: '1'
external_id:
  pmid:
  - '11706026'
file:
- access_level: open_access
  checksum: 13abe20f78eb37ab62beb006f62c69b7
  content_type: application/pdf
  creator: alisjak
  date_created: 2023-08-01T12:44:09Z
  date_updated: 2023-08-01T12:44:09Z
  file_id: '13439'
  file_name: 2002_JBC_Fuerst.pdf
  file_size: 798920
  relation: main_file
  success: 1
file_date_updated: 2023-08-01T12:44:09Z
has_accepted_license: '1'
intvolume: '       277'
issue: '6'
keyword:
- Cell Biology
- Molecular Biology
- Biochemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '02'
oa: 1
oa_version: Published Version
page: 4435-4445
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: ICln Ion channel splice variants in Caenorhabditis elegans
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 277
year: '2002'
...