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Bernhard Rupp
AmeriCorps VISTA
114Publications
30H-index
3,188Citations
Publications 114
Newest
Published on Jun 18, 2019in bioRxiv
Andreas Naschberger3
Estimated H-index: 3
,
Pauline Juyoux + 2 AuthorsMatthew W. Bowler22
Estimated H-index: 22
Afamin, a human blood plasma glycoprotein, a putative multi-functional transporter of hydrophobic molecules and a marker for metabolic syndrome, poses multiple challenges for crystallographic structure determination, both practically and in analysis of the models. Several hundred crystals were analysed, and unusual variability in cell volume and difficulty solving the structure despite a ~34% sequence identity with non-glycosylated human serum albumin indicated that the molecule exhibits variabl...
Published on May 31, 2019in ChemBioChem2.59
Janis Fricke3
Estimated H-index: 3
(Schiller International University),
Alexander Sherwood + 5 AuthorsDirk Hoffmeister31
Estimated H-index: 31
(FSU: University of Jena)
Published on Jun 20, 2018
Alexander Wlodawer65
Estimated H-index: 65
,
Zbigniew Dauter53
Estimated H-index: 53
+ 6 AuthorsBernhard Rupp30
Estimated H-index: 30
Published on Feb 20, 2018in Journal of Proteome Research3.78
Alessandra Altamirano1
Estimated H-index: 1
,
Andreas Naschberger3
Estimated H-index: 3
+ 19 AuthorsStefan Lechner3
Estimated H-index: 3
Afamin is an 87 kDa glycoprotein with five predicted N-glycosylation sites. Afamin’s glycan abundance contributes to conformational and chemical inhomogeneity presenting great challenges for molecular structure determination. For the purpose of studying the structure of afamin, various forms of recombinantly expressed human afamin (rhAFM) with different glycosylation patterns were thus created. Wild-type rhAFM and various hypoglycosylated forms were expressed in CHO, CHO-Lec1, and HEK293T cells....
Published on Feb 1, 2018in FEBS Journal4.74
Alexander Wlodawer65
Estimated H-index: 65
,
Zbigniew Dauter53
Estimated H-index: 53
(Argonne National Laboratory)
+ 6 AuthorsBernhard Rupp30
Estimated H-index: 30
(AmeriCorps VISTA)
The massive technical and computational progress of biomolecular crystallography has generated some adverse side effects. Most crystal structure models, produced by crystallographers or well-trained structural biologists, constitute useful sources of information, but occasional extreme outliers remind us that the process of structure determination is not fail-safe. The occurrence of severe errors or gross misinterpretations raises fundamental questions: Why do such aberrations emerge in the firs...
Published on Dec 6, 2017
Przemyslaw J. Porebski11
Estimated H-index: 11
,
Alexander Wlodawer65
Estimated H-index: 65
+ 6 AuthorsBernhard Rupp30
Estimated H-index: 30
Published on Dec 6, 2017
Robyn L. Stanfield49
Estimated H-index: 49
,
Bernhard Rupp30
Estimated H-index: 30
+ 6 AuthorsC.X. Weichenberger2
Estimated H-index: 2
Published on Dec 6, 2017
Przemyslaw J. Porebski11
Estimated H-index: 11
,
Alexander Wlodawer65
Estimated H-index: 65
+ 6 AuthorsBernhard Rupp30
Estimated H-index: 30
Published on Nov 29, 2017
Alexander Wlodawer65
Estimated H-index: 65
,
Zbigniew Dauter53
Estimated H-index: 53
+ 6 AuthorsBernhard Rupp30
Estimated H-index: 30
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