OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Role of protein conformation and weak interactions on γ-gliadin liquid-liquid phase separation
Line Sahli, D. Renard, Véronique Solé-Jamault, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 21

Showing 21 citing articles:

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins
Greta Bianchi, Sonia Longhi, Rita Grandori, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 17, pp. 6208-6208
Open Access | Times Cited: 95

Liquid–liquid phase separation in plants: Advances and perspectives from model species to crops
Qianwen Liu, Wenxuan Liu, Yiding Niu, et al.
Plant Communications (2023) Vol. 5, Iss. 1, pp. 100663-100663
Open Access | Times Cited: 16

Combining plant and dairy proteins in food colloid design
Emma B.A. Hinderink, Adeline Boire, D. Renard, et al.
Current Opinion in Colloid & Interface Science (2021) Vol. 56, pp. 101507-101507
Open Access | Times Cited: 29

Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations
Joel Markgren, Mikael S. Hedenqvist, Faiza Rasheed, et al.
Biomolecules (2020) Vol. 10, Iss. 8, pp. 1095-1095
Open Access | Times Cited: 30

Unraveling protein’s structural dynamics: from configurational dynamics to ensemble switching guides functional mesoscale assemblies
Exequiel Medina, Danielle R. Latham, Hugo Sanabria
Current Opinion in Structural Biology (2020) Vol. 66, pp. 129-138
Open Access | Times Cited: 21

Solubility Parameters of Amino Acids on Liquid–Liquid Phase Separation and Aggregation of Proteins
Akira Nomoto, Suguru Nishinami, Kentaro Shiraki
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 17

Evolution of CPEB4 Dynamics Across its Liquid–Liquid Phase Separation Transition
Manas Seal, Chandrima Jash, Reeba S. Jacob, et al.
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 47, pp. 12947-12957
Open Access | Times Cited: 17

Gliadin proteolytical resistant peptides: the interplay between structure and self-assembly in gluten-related disorders
María Georgina Herrera, Verónica I. Dodero
Biophysical Reviews (2021) Vol. 13, Iss. 6, pp. 1147-1154
Open Access | Times Cited: 17

Clustering and cross-linking of the wheat storage protein α-gliadin: A combined experimental and theoretical approach
Joel Markgren, Faiza Rasheed, Mikael S. Hedenqvist, et al.
International Journal of Biological Macromolecules (2022) Vol. 211, pp. 592-615
Open Access | Times Cited: 11

Semi-permeable vesicles produced by microfluidics to tune the phase behaviour of encapsulated macromolecules
Rémy Cochereau, D. Renard, Camille Noûs, et al.
Journal of Colloid and Interface Science (2020) Vol. 580, pp. 709-719
Closed Access | Times Cited: 17

Stimuli responsive self-assembled structural aggregates of ionic liquid based surfactants as the membrane free microreactors for dyes sequestration and drug encapsulation
Ankit Shah, Tapas Patel, Azza A. Al‐Ghamdi, et al.
Journal of Molecular Liquids (2022) Vol. 350, pp. 118555-118555
Closed Access | Times Cited: 8

Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding
Takunori Yasuda, Rikuri Morita, Yasuteru Shigeta, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 16, pp. 6610-6622
Open Access | Times Cited: 1

New exploration of the γ-gliadin structure through its partial hydrolysis
Line Sahli, Adeline Boire, Véronique Solé-Jamault, et al.
International Journal of Biological Macromolecules (2020) Vol. 165, pp. 654-664
Open Access | Times Cited: 7

Influence of Farming System and Forecrops of Spring Wheat on Protein Content in the Grain and the Physicochemical Properties of Unsonicated and Sonicated Gluten
Marta Tomczyńska‐Mleko, Cezary A. Kwiatkowski, Elżbieta Harasim, et al.
Molecules (2022) Vol. 27, Iss. 12, pp. 3926-3926
Open Access | Times Cited: 4

Redox-Sensitive Cysteines Confer Proximal Control of the Molecular Crowding Barrier in the Nuclear Pore
Wanzhen Zhang, Ryuji Watanabe, Hideaki Konishi, et al.
Cell Reports (2020) Vol. 33, Iss. 11, pp. 108484-108484
Open Access | Times Cited: 5

Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars
Daniel Hailegiorgis, Ephrem Seid, Chong Ae Lee, et al.
Journal of Crop Science and Biotechnology (2022) Vol. 25, Iss. 3, pp. 325-336
Closed Access | Times Cited: 3

Dense Phases of γ-Gliadins in Confined Geometries
Amélie Banc, Laurence Navailles, Jacques Leng, et al.
Colloids and Interfaces (2021) Vol. 5, Iss. 4, pp. 51-51
Open Access | Times Cited: 4

BEMM-GEN: A Toolkit for Generating a Biomolecular Environment-Mimicking Model for Molecular Dynamics Simulation
Takunori Yasuda, Rikuri Morita, Yasuteru Shigeta, et al.
Journal of Chemical Information and Modeling (2024)
Open Access

A story of two kingdoms: unravelling the intricacies of protein phase separation in plants and animals
Min Li, Xue Yang, Di Zhang, et al.
Critical Reviews in Biotechnology (2024), pp. 1-21
Open Access

Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed
Yuki Matsuoka, Tetsuya Yamada, Nobuyuki Maruyama
Transgenic Research (2021) Vol. 31, Iss. 1, pp. 43-58
Closed Access | Times Cited: 3

A Novel Physical Mechanism to Model Brownian Yet Non-Gaussian Diffusion: Theory and Application
Francisco E. Alban-Chacón, Erick Lamilla, Manuel S. Alvarez‐Alvarado
Materials (2022) Vol. 15, Iss. 17, pp. 5808-5808
Open Access | Times Cited: 1

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