Narinder Sanghera

834 total citations
17 papers, 695 citations indexed

About

Narinder Sanghera is a scholar working on Molecular Biology, Infectious Diseases and Cell Biology. According to data from OpenAlex, Narinder Sanghera has authored 17 papers receiving a total of 695 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Infectious Diseases and 4 papers in Cell Biology. Recurrent topics in Narinder Sanghera's work include Prion Diseases and Protein Misfolding (7 papers), Infectious Encephalopathies and Encephalitis (4 papers) and Neurological diseases and metabolism (2 papers). Narinder Sanghera is often cited by papers focused on Prion Diseases and Protein Misfolding (7 papers), Infectious Encephalopathies and Encephalitis (4 papers) and Neurological diseases and metabolism (2 papers). Narinder Sanghera collaborates with scholars based in United Kingdom, United States and Russia. Narinder Sanghera's co-authors include Teresa J. T. Pinheiro, Catherine Vénien‐Bryan, Jurate Kazlauskaite, Ian Sylvester, Judith Klein‐Seetharaman, Megan Grabenauer, Susan E. Slade, Mark J. Howard, Michael T. Bowers and A. Katrine Wallis and has published in prestigious journals such as Journal of the American Chemical Society, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Narinder Sanghera

17 papers receiving 679 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Narinder Sanghera United Kingdom 13 559 141 123 112 105 17 695
Kris Pauwels Belgium 17 580 1.0× 78 0.6× 495 4.0× 61 0.5× 59 0.6× 35 1.0k
Jörgen Ådén Sweden 18 655 1.2× 84 0.6× 178 1.4× 33 0.3× 82 0.8× 42 967
Dan Yin United States 18 740 1.3× 45 0.3× 115 0.9× 22 0.2× 128 1.2× 27 1.0k
Takashi Higurashi Japan 15 676 1.2× 107 0.8× 187 1.5× 116 1.0× 92 0.9× 19 746
Axelle Balguerie France 9 405 0.7× 50 0.4× 99 0.8× 57 0.5× 119 1.1× 9 490
Karen E. Marshall United Kingdom 15 721 1.3× 55 0.4× 582 4.7× 57 0.5× 51 0.5× 30 1.1k
Alexandra A. Kulikova Russia 16 438 0.8× 149 1.1× 409 3.3× 20 0.2× 42 0.4× 28 782
M. Schwalbe Germany 11 497 0.9× 19 0.1× 257 2.1× 34 0.3× 98 0.9× 12 674
Andrew J. Benie Denmark 15 370 0.7× 35 0.2× 80 0.7× 28 0.3× 19 0.2× 26 671
Michael A. Baldwin United States 8 1.0k 1.8× 509 3.6× 170 1.4× 497 4.4× 21 0.2× 9 1.1k

Countries citing papers authored by Narinder Sanghera

Since Specialization
Citations

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

Fields of papers citing papers by Narinder Sanghera

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Narinder Sanghera

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

All Works

17 of 17 papers shown
1.
Sanghera, Narinder, et al.. (2020). Angiotensin Converting Enzyme (ACE): A Marker for Personalized Feedback on Dieting. Nutrients. 12(3). 660–660. 10 indexed citations
2.
Sanghera, Narinder, et al.. (2019). Towards personalised molecular feedback for weight loss. BMC Obesity. 6(1). 20–20. 5 indexed citations
3.
Sanghera, Narinder, et al.. (2019). A marker for personalised feedback on dieting: Angiotensin Converting Enzyme. Proceedings of The Nutrition Society. 78(OCE2). 3 indexed citations
4.
Mohammadyani, Dariush, Naveena Yanamala, Alejandro K. Samhan‐Arias, et al.. (2018). Structural characterization of cardiolipin-driven activation of cytochrome c into a peroxidase and membrane perturbation. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860(5). 1057–1068. 32 indexed citations
5.
Freedman, Robert B., Lee J. Byrne, Jack W. Heal, et al.. (2017). ‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI). Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865(11). 1383–1394. 31 indexed citations
6.
Ye, Libin, Suvrajit Maji, Narinder Sanghera, et al.. (2017). Structure and dynamics of the insulin receptor: implications for receptor activation and drug discovery. Drug Discovery Today. 22(7). 1092–1102. 26 indexed citations
7.
Sanghera, Narinder, et al.. (2016). Insulin biosensor development: a case study. International Journal of Parallel Emergent and Distributed Systems. 32(1). 119–138. 9 indexed citations
8.
Irvine, Alistair G., A. Katrine Wallis, Narinder Sanghera, et al.. (2014). Protein Disulfide-Isomerase Interacts with a Substrate Protein at All Stages along Its Folding Pathway. PLoS ONE. 9(1). e82511–e82511. 43 indexed citations
9.
Sanghera, Narinder, Bruno E. Correia, Joana Simões‐Correia, et al.. (2011). Deciphering the Molecular Details for the Binding of the Prion Protein to Main Ganglioside GM1 of Neuronal Membranes. Chemistry & Biology. 18(11). 1422–1431. 33 indexed citations
10.
Grabenauer, Megan, Thomas Wyttenbach, Narinder Sanghera, et al.. (2010). Conformational Stability of Syrian Hamster Prion Protein PrP(90−231). Journal of the American Chemical Society. 132(26). 8816–8818. 28 indexed citations
11.
Hilton, Gillian R., Konstantinos Thalassinos, Megan Grabenauer, et al.. (2010). Structural analysis of prion proteins by means of drift cell and traveling wave ion mobility mass spectrometry. Journal of the American Society for Mass Spectrometry. 21(5). 845–854. 41 indexed citations
12.
Sanghera, Narinder, et al.. (2009). Insight into early events in the aggregation of the prion protein on lipid membranes. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788(10). 2245–2251. 28 indexed citations
13.
Sanghera, Narinder, Mark J. Wall, Catherine Vénien‐Bryan, & Teresa J. T. Pinheiro. (2008). Globular and pre-fibrillar prion aggregates are toxic to neuronal cells and perturb their electrophysiology. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1784(6). 873–881. 23 indexed citations
14.
Newman, William G., Sara Hamilton, J G Ayres, et al.. (2007). Array comparative genomic hybridization for diagnosis of developmental delay – an exploratory cost‐consequences analysis. Clinical Genetics. 71(3). 254–259. 21 indexed citations
15.
Kazlauskaite, Jurate, Narinder Sanghera, Ian Sylvester, Catherine Vénien‐Bryan, & Teresa J. T. Pinheiro. (2003). Structural Changes of the Prion Protein in Lipid Membranes Leading to Aggregation and Fibrillization. Biochemistry. 42(11). 3295–3304. 135 indexed citations
16.
Sanghera, Narinder & Teresa J. T. Pinheiro. (2002). Binding of prion protein to lipid membranes and implications for prion conversion. Journal of Molecular Biology. 315(5). 1241–1256. 161 indexed citations
17.
Sanghera, Narinder & Teresa J. T. Pinheiro. (2000). Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles. Protein Science. 9(6). 1194–1202. 66 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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