Andreas Ostermann

2.7k total citations
66 papers, 2.0k citations indexed

About

Andreas Ostermann is a scholar working on Molecular Biology, Materials Chemistry and Radiation. According to data from OpenAlex, Andreas Ostermann has authored 66 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 33 papers in Materials Chemistry and 15 papers in Radiation. Recurrent topics in Andreas Ostermann's work include Enzyme Structure and Function (30 papers), Protein Structure and Dynamics (21 papers) and Hemoglobin structure and function (15 papers). Andreas Ostermann is often cited by papers focused on Enzyme Structure and Function (30 papers), Protein Structure and Dynamics (21 papers) and Hemoglobin structure and function (15 papers). Andreas Ostermann collaborates with scholars based in Germany, Japan and United States. Andreas Ostermann's co-authors include G. Ulrich Nienhaus, Tobias E. Schrader, F. Parak, Robert Waschipky, Nobuo Niimura, Ichiro Tanaka, Matthew P. Blakeley, Kazuo Kurihara, Toshiyuki Chatake and Leighton Coates and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Andreas Ostermann

64 papers receiving 2.0k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Andreas Ostermann Germany	26	1.4k	740	529	305	245	66	2.0k
Zhong Ren United States	28	2.2k 1.6×	1.4k 1.9×	535 1.0×	483 1.6×	326 1.3×	89	3.8k
L. Powers United States	28	1.3k 1.0×	357 0.5×	605 1.1×	222 0.7×	258 1.1×	72	2.3k
Danilo Roccatano Germany	37	2.3k 1.7×	756 1.0×	199 0.4×	519 1.7×	337 1.4×	97	3.7k
Jörg Fitter Germany	32	1.9k 1.4×	819 1.1×	204 0.4×	613 2.0×	365 1.5×	87	2.9k
Alfredo Di Nola Italy	35	2.4k 1.8×	721 1.0×	515 1.0×	952 3.1×	442 1.8×	133	3.8k
Matthew P. Blakeley France	27	1.6k 1.2×	1.4k 1.9×	121 0.2×	76 0.2×	421 1.7×	92	2.4k
Martine Moulin France	30	2.1k 1.5×	688 0.9×	191 0.4×	458 1.5×	328 1.3×	82	2.9k
Grazia Cottone Italy	20	885 0.6×	528 0.7×	305 0.6×	288 0.9×	85 0.3×	47	1.5k
Pernille Harris Denmark	31	1.0k 0.7×	534 0.7×	93 0.2×	646 2.1×	269 1.1×	133	2.8k
Julia M. Goodfellow United Kingdom	25	1.8k 1.3×	665 0.9×	148 0.3×	386 1.3×	341 1.4×	84	2.4k

Countries citing papers authored by Andreas Ostermann

Since Specialization

Citations

This map shows the geographic impact of Andreas Ostermann'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 Andreas Ostermann with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Andreas Ostermann more than expected).

Fields of papers citing papers by Andreas Ostermann

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Andreas Ostermann. 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 Andreas Ostermann. The network helps show where Andreas Ostermann may publish in the future.

Co-authorship network of co-authors of Andreas Ostermann

This figure shows the co-authorship network connecting the top 25 collaborators of Andreas Ostermann. A scholar is included among the top collaborators of Andreas Ostermann 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 Andreas Ostermann. Andreas Ostermann is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Yokoyama, Takeshi, et al.. (2022). Neutron crystallographic analysis of the nucleotide-binding domain of Hsp72 in complex with ADP. IUCrJ. 9(5). 562–572. 3 indexed citations

Joutsuka, Tatsuya, Keisuke Igarashi, Masakazu Sugishima, et al.. (2022). Neutron crystallography and quantum chemical analysis of bilin reductase PcyA mutants reveal substrate and catalytic residue protonation states. Journal of Biological Chemistry. 299(1). 102763–102763. 1 indexed citations

Schiebel, J., Linda C. Schmidt, Torsten Steinmetzer, et al.. (2021). How a Fragment Draws Attention to Selectivity Discriminating Features between the Related Proteases Trypsin and Thrombin. Journal of Medicinal Chemistry. 64(3). 1611–1625. 1 indexed citations

Aldeghi, Matteo, Matthew P. Blakeley, Andreas Ostermann, et al.. (2019). A molecular mechanism for transthyretin amyloidogenesis. Nature Communications. 10(1). 925–925. 100 indexed citations

Shimizu, Rumi, et al.. (2019). Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein. The Journal of Physical Chemistry Letters. 11(2). 492–496. 8 indexed citations

Li, Long, Motoyasu Adachi, Jian Yu, et al.. (2019). Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB. Acta Crystallographica Section F Structural Biology Communications. 75(3). 193–196. 2 indexed citations

Mahon, Brian P., Matthew P. Blakeley, Andreas Ostermann, et al.. (2019). Using neutron crystallography to elucidate the basis of selective inhibition of carbonic anhydrase by saccharin and a derivative. Journal of Structural Biology. 205(2). 147–154. 12 indexed citations

Schrader, Tobias E., Andreas Ostermann, Leighton Coates, et al.. (2018). Elucidation of Hydrogen Bonding Patterns in Ligand-Free, Lactose- and Glycerol-Bound Galectin-3C by Neutron Crystallography to Guide Drug Design. Journal of Medicinal Chemistry. 61(10). 4412–4420. 32 indexed citations

Schiebel, J., Roberto Gaspari, Hans‐Dieter Gerber, et al.. (2017). Ladungen verschieben Protonierungen: Neutronenbeugung zeigt, dass Anilin und 2‐Aminopyridin protoniert an Trypsin binden. Angewandte Chemie. 129(17). 4965–4969. 3 indexed citations

10.

Schiebel, J., Roberto Gaspari, Hans‐Dieter Gerber, et al.. (2017). Charges Shift Protonation: Neutron Diffraction Reveals that Aniline and 2‐Aminopyridine Become Protonated Upon Binding to Trypsin. Angewandte Chemie International Edition. 56(17). 4887–4890. 23 indexed citations

11.

Saraboji, K., Janina Sprenger, Ulf J. Nilsson, et al.. (2016). Perdeuteration, crystallization, data collection and comparison of five neutron diffraction data sets of complexes of human galectin-3C. Acta Crystallographica Section D Structural Biology. 72(11). 1194–1202. 15 indexed citations

12.

Casadei, Cecilia M., Andrea Gumiero, Clive Metcalfe, et al.. (2014). Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase. Science. 345(6193). 193–197. 118 indexed citations

13.

Coates, Leighton, Stephen J. Tomanicek, Tobias E. Schrader, et al.. (2014). Cryogenic neutron protein crystallography: routine methods and potential benefits. Journal of Applied Crystallography. 47(4). 1431–1434. 26 indexed citations

14.

Tomanicek, Stephen J., Robert F. Standaert, Kevin L. Weiss, et al.. (2012). Neutron and X-ray Crystal Structures of a Perdeuterated Enzyme Inhibitor Complex Reveal the Catalytic Proton Network of the Toho-1 β-Lactamase for the Acylation Reaction. Journal of Biological Chemistry. 288(7). 4715–4722. 35 indexed citations

15.

Achterhold, Klaus, Andreas Ostermann, Martine Moulin, et al.. (2011). Dynamical properties of the hydration shell of fully deuterated myoglobin. Physical Review E. 84(4). 41930–41930. 10 indexed citations

16.

Chatake, Toshiyuki, Andreas Ostermann, Kazuo Kurihara, et al.. (2003). Hydration structures in proteins and neutron diffraction experiment on dissimilatory sulfite reductase D (DsrD). Journal of Synchrotron Radiation. 11(1). 72–75. 7 indexed citations

17.

Chong, Song‐Ho, Yasumasa Joti, Akinori Kidera, et al.. (2001). Dynamical transition of myoglobin in a crystal: comparative studies of X-ray crystallography and Mössbauer spectroscopy. European Biophysics Journal. 30(5). 319–329. 41 indexed citations

18.

Achterhold, Klaus, Andreas Ostermann, U. van Bürck, et al.. (2000). Nuclear forward scattering of synchrotron radiation by deoxymyoglobin. European Biophysics Journal. 29(2). 146–152. 10 indexed citations

19.

Ostermann, Andreas, et al.. (2000). Protein Dynamics in an Intermediate State of Myoglobin: Optical Absorption, Resonance Raman Spectroscopy, and X-Ray Structure Analysis. Biophysical Journal. 78(4). 2081–2092. 37 indexed citations

20.

Ostermann, Andreas, et al.. (1998). From metmyoglobin to deoxy myoglobin: relaxations of an intermediate state. European Biophysics Journal. 27(2). 113–125. 27 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.

Explore authors with similar magnitude of impact