Shabir Najmudin

1.4k total citations
70 papers, 1.1k citations indexed

About

Shabir Najmudin is a scholar working on Biotechnology, Biomedical Engineering and Materials Chemistry. According to data from OpenAlex, Shabir Najmudin has authored 70 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Biotechnology, 29 papers in Biomedical Engineering and 27 papers in Materials Chemistry. Recurrent topics in Shabir Najmudin's work include Enzyme Production and Characterization (37 papers), Biofuel production and bioconversion (29 papers) and Polysaccharides and Plant Cell Walls (22 papers). Shabir Najmudin is often cited by papers focused on Enzyme Production and Characterization (37 papers), Biofuel production and bioconversion (29 papers) and Polysaccharides and Plant Cell Walls (22 papers). Shabir Najmudin collaborates with scholars based in Portugal, United Kingdom and Tunisia. Shabir Najmudin's co-authors include C.M.G.A. Fontes, Harry J. Gilbert, Maria João Romão, L.M.A. Ferreira, Victor D. Alves, José A. M. Prates, Pedro Bule, Ana Luı́sa Carvalho, Habib Nasri and Isabel Moura and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Shabir Najmudin

67 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shabir Najmudin Portugal 21 507 402 368 234 224 70 1.1k
Christian Isak Jørgensen Denmark 13 594 1.2× 719 1.8× 429 1.2× 399 1.7× 85 0.4× 18 1.2k
Hsin‐Hung Lin Taiwan 22 477 0.9× 417 1.0× 277 0.8× 296 1.3× 435 1.9× 54 1.5k
Limin Ning China 25 888 1.8× 305 0.8× 205 0.6× 105 0.4× 258 1.2× 51 1.5k
Luisa Ciano United Kingdom 12 425 0.8× 394 1.0× 249 0.7× 333 1.4× 98 0.4× 15 859
Claus C. Fuglsang Denmark 15 1.0k 2.0× 393 1.0× 530 1.4× 425 1.8× 167 0.7× 19 1.6k
Bertus van den Burg Netherlands 21 1.8k 3.6× 292 0.7× 636 1.7× 148 0.6× 502 2.2× 31 2.2k
Shijun Qian China 16 336 0.7× 99 0.2× 293 0.8× 258 1.1× 153 0.7× 43 808
Changrui Lu China 22 946 1.9× 176 0.4× 123 0.3× 162 0.7× 150 0.7× 59 1.6k
Ciarán Ó’Fágáin Ireland 17 821 1.6× 186 0.5× 162 0.4× 265 1.1× 163 0.7× 39 1.2k
Trine Christensen United States 20 633 1.2× 158 0.4× 187 0.5× 121 0.5× 120 0.5× 36 1.4k

Countries citing papers authored by Shabir Najmudin

Since Specialization
Citations

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

Fields of papers citing papers by Shabir Najmudin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shabir Najmudin

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

All Works

20 of 20 papers shown
1.
Palmer, Rex A., Jon Cooper, C.E. Naylor, et al.. (2023). Ultra-high resolution X-ray structure of orthorhombic bovine pancreatic Ribonuclease A at 100K. BMC Chemistry. 17(1). 91–91. 2 indexed citations
2.
Viegas, Aldino, Victor D. Alves, José A. M. Prates, et al.. (2021). A dual cohesin–dockerin complex binding mode in Bacteroides cellulosolvens contributes to the size and complexity of its cellulosome. Journal of Biological Chemistry. 296. 100552–100552. 11 indexed citations
3.
Sharma, Kedar, C.M.G.A. Fontes, Shabir Najmudin, & Arun Goyal. (2019). Small angle X-ray scattering based structure, modeling and molecular dynamics analyses of family 43 glycoside hydrolase α-L-arabinofuranosidase fromClostridium thermocellum. Journal of Biomolecular Structure and Dynamics. 39(1). 209–218. 5 indexed citations
4.
Sharma, Kedar, C.M.G.A. Fontes, Shabir Najmudin, & Arun Goyal. (2019). Molecular organization and protein stability of the Clostridium thermocellum glucuronoxylan endo-β-1,4-xylanase of family 30 glycoside hydrolase in solution. Journal of Structural Biology. 206(3). 335–344. 5 indexed citations
5.
Bule, Pedro, Kate Cameron, José A. M. Prates, et al.. (2018). Structure–function analyses generate novel specificities to assemble the components of multienzyme bacterial cellulosome complexes. Journal of Biological Chemistry. 293(11). 4201–4212. 17 indexed citations
6.
Bule, Pedro, Sadanari Jindou, Bareket Dassa, et al.. (2017). Complexity of the Ruminococcus flavefaciens FD-1 cellulosome reflects an expansion of family-related protein-protein interactions. Scientific Reports. 7(1). 42355–42355. 39 indexed citations
7.
Bule, Pedro, Victor D. Alves, Ana Luı́sa Carvalho, et al.. (2017). Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes. Scientific Reports. 7(1). 759–759. 22 indexed citations
8.
Venditto, I., Julia Schückel, Pedro Bule, et al.. (2016). Complexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition.. HAL (Le Centre pour la Communication Scientifique Directe). 1 indexed citations
9.
Cameron, Kate, Shabir Najmudin, Victor D. Alves, et al.. (2015). Cell-surface Attachment of Bacterial Multienzyme Complexes Involves Highly Dynamic Protein-Protein Anchors. Journal of Biological Chemistry. 290(21). 13578–13590. 20 indexed citations
10.
Bule, Pedro, et al.. (2014). Overexpression, crystallization and preliminary X-ray characterization ofRuminococcus flavefaciensscaffoldin C cohesin in complex with a dockerin from an uncharacterized CBM-containing protein. Acta Crystallographica Section F Structural Biology Communications. 70(8). 1061–1064. 2 indexed citations
11.
Venditto, I., Helena Santos, L.M.A. Ferreira, et al.. (2014). Overproduction, purification, crystallization and preliminary X-ray characterization of the family 46 carbohydrate-binding module (CBM46) of endo-β-1,4-glucanase B (CelB) fromBacillus halodurans. Acta Crystallographica Section F Structural Biology Communications. 70(6). 754–757. 3 indexed citations
12.
Brás, Joana L. A., Victor D. Alves, Ana Luı́sa Carvalho, et al.. (2012). Novel Clostridium thermocellum Type I Cohesin-Dockerin Complexes Reveal a Single Binding Mode. Journal of Biological Chemistry. 287(53). 44394–44405. 26 indexed citations
13.
Brás, Joana L. A., Ana Luı́sa Carvalho, Aldino Viegas, et al.. (2012). Escherichia coli Expression, Purification, Crystallization, and Structure Determination of Bacterial Cohesin–Dockerin Complexes. Methods in enzymology on CD-ROM/Methods in enzymology. 510. 395–415. 6 indexed citations
14.
Cameron, Kate, Victor D. Alves, Pedro Bule, et al.. (2012). Purification, crystallization and preliminary X-ray characterization of theAcetivibrio cellulolyticustype I cohesin ScaC in complex with the ScaB dockerin. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(9). 1030–1033. 3 indexed citations
15.
Pinheiro, B., Joana L. A. Brás, Shabir Najmudin, et al.. (2012). Flexibility and specificity of the cohesin–dockerin interaction: implications for cellulosome assembly and functionality. Biocatalysis and Biotransformation. 30(3). 309–315. 4 indexed citations
16.
Luís, Ana S., Victor D. Alves, Maria João Romão, et al.. (2011). Overproduction, purification, crystallization and preliminary X-ray characterization of a novel carbohydrate-binding module of endoglucanase Cel5A fromEubacterium cellulosolvens. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(4). 491–493. 4 indexed citations
17.
Najmudin, Shabir, et al.. (2009). Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) fromDesulfovibrio gigas. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(7). 730–732. 9 indexed citations
18.
Najmudin, Shabir, B. Pinheiro, Maria João Romão, José A. M. Prates, & C.M.G.A. Fontes. (2008). Purification, crystallization and crystallographic analysis ofClostridium thermocellumendo-1,4-β-D-xylanase 10B in complex with xylohexaose. Revista de Estudos Anglo-Portugueses/Journal of Anglo-Portuguese Studies. 64(8). 715–718. 2 indexed citations
19.
Najmudin, Shabir, Catarina I. P. D. Guerreiro, Ana Luı́sa Carvalho, et al.. (2005). Xyloglucan Is Recognized by Carbohydrate-binding Modules That Interact with β-Glucan Chains. Journal of Biological Chemistry. 281(13). 8815–8828. 97 indexed citations
20.
Najmudin, Shabir, V. Nalini, H.P.C. Driessen, et al.. (1993). Structure of the bovine eye lens protein γB(γII)-crystallin at 1.47 Å. Acta Crystallographica Section D Biological Crystallography. 49(2). 223–233. 49 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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