Christiane Veit

741 total citations
18 papers, 554 citations indexed

About

Christiane Veit is a scholar working on Molecular Biology, Cell Biology and Biotechnology. According to data from OpenAlex, Christiane Veit has authored 18 papers receiving a total of 554 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 7 papers in Cell Biology and 7 papers in Biotechnology. Recurrent topics in Christiane Veit's work include Glycosylation and Glycoproteins Research (12 papers), Polysaccharides and Plant Cell Walls (7 papers) and Transgenic Plants and Applications (6 papers). Christiane Veit is often cited by papers focused on Glycosylation and Glycoproteins Research (12 papers), Polysaccharides and Plant Cell Walls (7 papers) and Transgenic Plants and Applications (6 papers). Christiane Veit collaborates with scholars based in Austria, United Kingdom and Argentina. Christiane Veit's co-authors include Richard Strasser, Jennifer Schoberer, Friedrich Altmann, Ulrike Vavra, Silvia Hüttner, Eva Liebminger, Lukas Mach, Martin Pabst, Josephine Grass and Cyril Zipfel and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and The Plant Cell.

In The Last Decade

Christiane Veit

18 papers receiving 549 citations

Peers

Christiane Veit

BIOTE

IMMUN

Eva Liebminger Austria

Ulrike Vavra Austria

Sophie Pagny France

Barbara Svoboda Austria

Claude Saint‐Jore‐Dupas France

Anne‐Catherine Fitchette‐Lainé France

Cecilia D’Alessio Argentina

Qi Yan United States

Maurice Henquet Netherlands

Megumi Maeda Japan

Eva Liebminger Austria

Christiane Veit

552 ×1.4

270 ×1.2

207 ×1.0

BIOTE

107 ×0.9

121 ×1.0

IMMUN

Citations per year, relative to Christiane Veit Christiane Veit (= 1×) peers Eva Liebminger

Countries citing papers authored by Christiane Veit

Since Specialization

Citations

This map shows the geographic impact of Christiane Veit's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Christiane Veit with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Christiane Veit more than expected).

Fields of papers citing papers by Christiane Veit

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Christiane Veit. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Christiane Veit. The network helps show where Christiane Veit may publish in the future.

Co-authorship network of co-authors of Christiane Veit

This figure shows the co-authorship network connecting the top 25 collaborators of Christiane Veit. A scholar is included among the top collaborators of Christiane Veit based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Christiane Veit. Christiane Veit is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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18 of 18 papers shown

Schoberer, Jennifer, Yun‐Ji Shin, Ulrike Vavra, Christiane Veit, & Richard Strasser. (2024). Analysis of Protein Glycosylation in the ER. Methods in molecular biology. 2772. 221–238. 1 indexed citations

Vavra, Ulrike, Yun‐Ji Shin, Christiane Veit, et al.. (2022). In Planta Production of the Receptor-Binding Domain From SARS-CoV-2 With Human Blood Group A Glycan Structures. Frontiers in Chemistry. 9. 816544–816544. 12 indexed citations

Schoberer, Jennifer, Christiane Veit, Ulrike Vavra, et al.. (2019). A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD. Nature Communications. 10(1). 3701–3701. 28 indexed citations

Schoberer, Jennifer, Eva Liebminger, Ulrike Vavra, et al.. (2019). The Golgi Localization of GnTI Requires a Polar Amino Acid Residue within Its Transmembrane Domain. PLANT PHYSIOLOGY. 180(2). 859–873. 18 indexed citations

Veit, Christiane, et al.. (2018). Processing of the Terminal Alpha-1,2-Linked Mannose Residues From Oligomannosidic N-Glycans Is Critical for Proper Root Growth. Frontiers in Plant Science. 9. 1807–1807. 17 indexed citations

Shin, Yun‐Ji, Ulrike Vavra, Christiane Veit, & Richard Strasser. (2018). The glycan‐dependent ERAD machinery degrades topologically diverse misfolded proteins. The Plant Journal. 94(2). 246–259. 19 indexed citations

Schoberer, Jennifer, Yun‐Ji Shin, Ulrike Vavra, Christiane Veit, & Richard Strasser. (2017). Analysis of Protein Glycosylation in the ER. Methods in molecular biology. 1691. 205–222. 23 indexed citations

Xue, Hui, Christiane Veit, Lindy Abas, et al.. (2017). Arabidopsis thaliana FLA4 functions as a glycan‐stabilized soluble factor via its carboxy‐proximal Fasciclin 1 domain. The Plant Journal. 91(4). 613–630. 43 indexed citations

Vavra, Ulrike, Christiane Veit, & Richard Strasser. (2016). Hormone Receptor Glycosylation. Methods in molecular biology. 1497. 205–220. 2 indexed citations

10.

Veit, Christiane, Ulrike Vavra, & Richard Strasser. (2014). N-Glycosylation and Plant Cell Growth. Methods in molecular biology. 1242. 183–194. 9 indexed citations

11.

Schoberer, Jennifer, Eva Liebminger, Ulrike Vavra, et al.. (2014). The transmembrane domain of N –acetylglucosaminyltransferase I is the key determinant for its Golgi subcompartmentation. The Plant Journal. 80(5). 809–822. 24 indexed citations

12.

Hüttner, Silvia, Christiane Veit, Ulrike Vavra, et al.. (2014). A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation. Biochemical Journal. 464(3). 401–411. 23 indexed citations

13.

Hüttner, Silvia, Christiane Veit, Ulrike Vavra, et al.. (2014). Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum–Associated Degradation of Misfolded Glycoproteins. The Plant Cell. 26(4). 1712–1728. 61 indexed citations

14.

Malinovsky, Frederikke Gro, et al.. (2013). Specialized Roles of the Conserved Subunit OST3/6 of the Oligosaccharyltransferase Complex in Innate Immunity and Tolerance to Abiotic Stresses . PLANT PHYSIOLOGY. 162(1). 24–38. 49 indexed citations

15.

Hüttner, Silvia, Christiane Veit, Jennifer Schoberer, Josephine Grass, & Richard Strasser. (2012). Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins. Plant Molecular Biology. 79(1-2). 21–33. 66 indexed citations

16.

Liebminger, Eva, Christiane Veit, Martin Pabst, et al.. (2011). β-N-Acetylhexosaminidases HEXO1 and HEXO3 Are Responsible for the Formation of Paucimannosidic N-Glycans in Arabidopsis thaliana. Journal of Biological Chemistry. 286(12). 10793–10802. 69 indexed citations

17.

Castilho, Alexandra, Martin Pabst, Renaud Léonard, et al.. (2008). Construction of a Functional CMP-Sialic Acid Biosynthesis Pathway in Arabidopsis. PLANT PHYSIOLOGY. 147(1). 331–339. 54 indexed citations

18.

Léonard, Renaud, Martin Pabst, Jayakumar Singh Bondili, et al.. (2008). Identification of an Arabidopsis gene encoding a GH95 alpha1,2-fucosidase active on xyloglucan oligo- and polysaccharides. Phytochemistry. 69(10). 1983–1988. 36 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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