Transmembranprotein (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "Transmembranprotein" in German language version.

refsWebsite
Global rank German rank
2nd place
3rd place
4th place
7th place

doi.org

  • K. L. Pierce, R. T. Premont, R. J. Lefkowitz: Seven-transmembrane receptors. In: Nature reviews. Molecular cell biology. Band 3, Nummer 9, September 2002, S. 639–650, doi:10.1038/nrm908, PMID 12209124.
  • M. S. Almén, K. J. Nordström, R. Fredriksson, H. B. Schiöth: Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin. In: BMC biology. Band 7, August 2009, S. 50, doi:10.1186/1741-7007-7-50, PMID 19678920, PMC 2739160 (freier Volltext).
  • D. Chaturvedi, R. Mahalakshmi: Transmembrane β-barrels: Evolution, folding and energetics. In: Biochimica et biophysica acta. Biomembranes. Band 1859, Nummer 12, Dezember 2017, S. 2467–2482, doi:10.1016/j.bbamem.2017.09.020, PMID 28943271, PMC 7115949 (freier Volltext).
  • L. K. Nicholson, T. A. Cross: Gramicidin cation channel: an experimental determination of the right-handed helix sense and verification of beta-type hydrogen bonding. In: Biochemistry. Band 28, Nummer 24, November 1989, S. 9379–9385, doi:10.1021/bi00450a019, PMID 2482072.
  • V. Kubyshkin, S. L. Grage, A. S. Ulrich, N. Budisa: Bilayer thickness determines the alignment of model polyproline helices in lipid membranes. In: Physical Chemistry Chemical Physics. Band 21, Nummer 40, Oktober 2019, S. 22396–22408, doi:10.1039/c9cp02996f, PMID 31577299.
  • V. Goder, M. Spiess: Topogenesis of membrane proteins: determinants and dynamics. In: FEBS letters. Band 504, Nummer 3, August 2001, S. 87–93, doi:10.1016/s0014-5793(01)02712-0, PMID 11532438.
  • J. S. Bonifacino, L. M. Traub: Signals for sorting of transmembrane proteins to endosomes and lysosomes. In: Annual review of biochemistry. Band 72, 2003, S. 395–447, doi:10.1146/annurev.biochem.72.121801.161800, PMID 12651740.
  • H. Y. Gee, J. Kim, M. G. Lee: Unconventional secretion of transmembrane proteins. In: Seminars in cell & developmental biology. Band 83, 11 2018, S. 59–66, doi:10.1016/j.semcdb.2018.03.016, PMID 29580969.
  • L. B. Case, J. A. Ditlev, M. K. Rosen: Regulation of Transmembrane Signaling by Phase Separation. In: Annual review of biophysics. Band 48, 05 2019, S. 465–494, doi:10.1146/annurev-biophys-052118-115534, PMID 30951647, PMC 6771929 (freier Volltext).
  • T. A. Cross, M. Sharma, M. Yi, H. X. Zhou: Influence of solubilizing environments on membrane protein structures. In: Trends in Biochemical Sciences. Band 36, Nummer 2, Februar 2011, S. 117–125, doi:10.1016/j.tibs.2010.07.005, PMID 20724162, PMC 3161620 (freier Volltext).
  • E. P. Carpenter, K. Beis, A. D. Cameron, S. Iwata: Overcoming the challenges of membrane protein crystallography. In: Current opinion in structural biology. Band 18, Nummer 5, Oktober 2008, S. 581–586, doi:10.1016/j.sbi.2008.07.001, PMID 18674618, PMC 2580798 (freier Volltext).

nih.gov

ncbi.nlm.nih.gov

  • K. L. Pierce, R. T. Premont, R. J. Lefkowitz: Seven-transmembrane receptors. In: Nature reviews. Molecular cell biology. Band 3, Nummer 9, September 2002, S. 639–650, doi:10.1038/nrm908, PMID 12209124.
  • M. S. Almén, K. J. Nordström, R. Fredriksson, H. B. Schiöth: Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin. In: BMC biology. Band 7, August 2009, S. 50, doi:10.1186/1741-7007-7-50, PMID 19678920, PMC 2739160 (freier Volltext).
  • D. Chaturvedi, R. Mahalakshmi: Transmembrane β-barrels: Evolution, folding and energetics. In: Biochimica et biophysica acta. Biomembranes. Band 1859, Nummer 12, Dezember 2017, S. 2467–2482, doi:10.1016/j.bbamem.2017.09.020, PMID 28943271, PMC 7115949 (freier Volltext).
  • L. K. Nicholson, T. A. Cross: Gramicidin cation channel: an experimental determination of the right-handed helix sense and verification of beta-type hydrogen bonding. In: Biochemistry. Band 28, Nummer 24, November 1989, S. 9379–9385, doi:10.1021/bi00450a019, PMID 2482072.
  • V. Kubyshkin, S. L. Grage, A. S. Ulrich, N. Budisa: Bilayer thickness determines the alignment of model polyproline helices in lipid membranes. In: Physical Chemistry Chemical Physics. Band 21, Nummer 40, Oktober 2019, S. 22396–22408, doi:10.1039/c9cp02996f, PMID 31577299.
  • V. Goder, M. Spiess: Topogenesis of membrane proteins: determinants and dynamics. In: FEBS letters. Band 504, Nummer 3, August 2001, S. 87–93, doi:10.1016/s0014-5793(01)02712-0, PMID 11532438.
  • J. S. Bonifacino, L. M. Traub: Signals for sorting of transmembrane proteins to endosomes and lysosomes. In: Annual review of biochemistry. Band 72, 2003, S. 395–447, doi:10.1146/annurev.biochem.72.121801.161800, PMID 12651740.
  • H. Y. Gee, J. Kim, M. G. Lee: Unconventional secretion of transmembrane proteins. In: Seminars in cell & developmental biology. Band 83, 11 2018, S. 59–66, doi:10.1016/j.semcdb.2018.03.016, PMID 29580969.
  • L. B. Case, J. A. Ditlev, M. K. Rosen: Regulation of Transmembrane Signaling by Phase Separation. In: Annual review of biophysics. Band 48, 05 2019, S. 465–494, doi:10.1146/annurev-biophys-052118-115534, PMID 30951647, PMC 6771929 (freier Volltext).
  • T. A. Cross, M. Sharma, M. Yi, H. X. Zhou: Influence of solubilizing environments on membrane protein structures. In: Trends in Biochemical Sciences. Band 36, Nummer 2, Februar 2011, S. 117–125, doi:10.1016/j.tibs.2010.07.005, PMID 20724162, PMC 3161620 (freier Volltext).
  • E. P. Carpenter, K. Beis, A. D. Cameron, S. Iwata: Overcoming the challenges of membrane protein crystallography. In: Current opinion in structural biology. Band 18, Nummer 5, Oktober 2008, S. 581–586, doi:10.1016/j.sbi.2008.07.001, PMID 18674618, PMC 2580798 (freier Volltext).