Enno Hartmann spends much of his time researching Biochemistry, Importin, Endoplasmic reticulum, Cell biology and Nuclear pore. His Importin research incorporates themes from Nuclear localization sequence, Importin-alpha and Alpha Karyopherins. His studies in Endoplasmic reticulum integrate themes in fields like Secretory protein, Sec61 and Membrane protein, Protein targeting.
His research integrates issues of Transport protein, SEC Translocation Channels and SEC63 in his study of Sec61. His work carried out in the field of Cell biology brings together such families of science as Integral membrane protein and Peripheral membrane protein. His Nuclear pore study combines topics from a wide range of disciplines, such as Nuclear export signal and Nuclear protein.
Enno Hartmann mainly investigates Cell biology, Biochemistry, Endoplasmic reticulum, Importin and Membrane protein. The various areas that he examines in his Cell biology study include Signal recognition particle and Chromosomal translocation. His work on Biochemistry is being expanded to include thematically relevant topics such as Biophysics.
His Endoplasmic reticulum study incorporates themes from Vesicle-associated membrane protein 8, Sec61, Translocon and Signal peptide. Enno Hartmann has researched Importin in several fields, including Nuclear localization sequence, Nuclear pore and Alpha Karyopherins. His Membrane protein research includes elements of Glycosylation and Transmembrane protein.
Enno Hartmann mainly focuses on Cell biology, Importin, Chromosomal translocation, Endoplasmic reticulum and Nuclear localization sequence. His studies deal with areas such as Influenza A virus, Sec61 and Ribosomal protein as well as Cell biology. His Importin study is concerned with the field of Nuclear transport as a whole.
His biological study spans a wide range of topics, including Resistant phenotype and Membrane protein, Translocon. His Nuclear localization sequence research integrates issues from Karyopherin, Neuropathic pain, Ataxin, Spinocerebellar ataxia and Nuclear pore. In vitro is a subfield of Biochemistry that Enno Hartmann tackles.
Enno Hartmann focuses on Cell biology, Endoplasmic reticulum, Translocon, Importin and Nuclear localization sequence. Enno Hartmann has included themes like Nuclear protein, Membrane transport protein and SEC61 Translocon in his Cell biology study. The Endoplasmic reticulum study combines topics in areas such as Vesicle-associated membrane protein 8, Protein structure, Sec61 and Signal recognition particle, Signal peptide.
His Translocon research includes themes of Transport protein, Integral membrane protein and Small interfering RNA. His Importin study integrates concerns from other disciplines, such as Karyopherin, Nuclear pore and Ataxin, Spinocerebellar ataxia. His specific area of interest is Nuclear localization sequence, where Enno Hartmann studies Alpha Karyopherins.
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X-ray structure of a protein-conducting channel
Bert van den Berg;William M. Clemons;Ian Collinson;Yorgo Modis.
Nature (2004)
Isolation of a protein that is essential for the first step of nuclear protein import
Dirk Görlich;Siegfried Prehn;Ronald A. Laskey;Enno Hartmann.
Cell (1994)
Predicting the orientation of eukaryotic membrane-spanning proteins
Enno Hartmann;Tom A. Rapoport;Harvey F. Lodish.
Proceedings of the National Academy of Sciences of the United States of America (1989)
Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope.
Dirk Görlich;Susanne Kostka;Regine Kraft;Colin Dingwall.
Current Biology (1995)
Distinct functions for the two importin subunits in nuclear protein import
Dirk Görlich;Frank Vogel;Anthony D. Mills;Enno Hartmann.
Nature (1995)
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
Steffen Panzner;Lars Dreier;Enno Hartmann;Susanne Kostka.
Cell (1995)
A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation
Dirk Görlich;Siegfried Prehn;Enno Hartmann;Kai-Uwe Kalies.
Cell (1992)
A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus.
D. Görlich;P. Henklein;R. A. Laskey;E. Hartmann.
The EMBO Journal (1996)
Identification of a tRNA-specific Nuclear Export Receptor
U. Kutay;G. Lipowsky;E. Izaurralde;F. R. Bischoff.
Molecular Cell (1998)
Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency.
Torben Lübke;Thorsten Marquardt;Amos Etzioni;Enno Hartmann.
Nature Genetics (2001)
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