
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:
Kinetics theories to understand the mechanism of aggregation of a protein and to design strategies for its inhibition
Shilpa Sharma, Priya Modi, Gargi Sharma, et al.
Biophysical Chemistry (2021) Vol. 278, pp. 106665-106665
Closed Access | Times Cited: 39
Shilpa Sharma, Priya Modi, Gargi Sharma, et al.
Biophysical Chemistry (2021) Vol. 278, pp. 106665-106665
Closed Access | Times Cited: 39
Showing 1-25 of 39 citing articles:
Intrinsically disordered proteins/regions and insight into their biomolecular interactions
Pinak Chakrabarti, Devlina Chakravarty
Biophysical Chemistry (2022) Vol. 283, pp. 106769-106769
Closed Access | Times Cited: 53
Pinak Chakrabarti, Devlina Chakravarty
Biophysical Chemistry (2022) Vol. 283, pp. 106769-106769
Closed Access | Times Cited: 53
A mechanistic survey of Alzheimer's disease
Yijing Tang, Dong Zhang, Xiong Gong, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106735-106735
Open Access | Times Cited: 45
Yijing Tang, Dong Zhang, Xiong Gong, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106735-106735
Open Access | Times Cited: 45
Inhibition of fibril formation by polyphenols: molecular mechanisms, challenges, and prospective solutions
Shilpa Sharma, Shashank Deep
Chemical Communications (2024) Vol. 60, Iss. 53, pp. 6717-6727
Closed Access | Times Cited: 6
Shilpa Sharma, Shashank Deep
Chemical Communications (2024) Vol. 60, Iss. 53, pp. 6717-6727
Closed Access | Times Cited: 6
Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis
Laxmikant Gadhe, Arunima Sakunthala, Semanti Mukherjee, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106736-106736
Closed Access | Times Cited: 39
Laxmikant Gadhe, Arunima Sakunthala, Semanti Mukherjee, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106736-106736
Closed Access | Times Cited: 39
Tetrabutylammonium based ionic liquids (ILs) inhibit the amyloid aggregation of superoxide dismutase 1 (SOD1)
Meena Kumari, Shilpa Sharma, Shashank Deep
Journal of Molecular Liquids (2022) Vol. 353, pp. 118761-118761
Closed Access | Times Cited: 20
Meena Kumari, Shilpa Sharma, Shashank Deep
Journal of Molecular Liquids (2022) Vol. 353, pp. 118761-118761
Closed Access | Times Cited: 20
Biophysical and spectroscopical insights into structural modulation of species in the aggregation pathway of superoxide dismutase 1
Vijay Raj Tomar, Shilpa Sharma, Soumik Siddhanta, et al.
Communications Chemistry (2025) Vol. 8, Iss. 1
Open Access
Vijay Raj Tomar, Shilpa Sharma, Soumik Siddhanta, et al.
Communications Chemistry (2025) Vol. 8, Iss. 1
Open Access
Whole process of fab antibody aggregation in intestinal environment and their aggregation regulation: An insight from static and concentration perturbation aggregations
Minquan Xia, Lixian Ding, Dong U. Ahn, et al.
International Journal of Biological Macromolecules (2025), pp. 140756-140756
Closed Access
Minquan Xia, Lixian Ding, Dong U. Ahn, et al.
International Journal of Biological Macromolecules (2025), pp. 140756-140756
Closed Access
Osthole's capacity to prevent tau aggregation, a key protein in tauopathy and Alzheimer's disease
Weiwei Liu, Hui-lian Xu, Chen Wang, et al.
International Journal of Biological Macromolecules (2025), pp. 143235-143235
Closed Access
Weiwei Liu, Hui-lian Xu, Chen Wang, et al.
International Journal of Biological Macromolecules (2025), pp. 143235-143235
Closed Access
Graphene quantum dots obstruct the membrane axis of Alzheimer's amyloid beta
Huayuan Tang, Yuhuan Li, Aleksandr Käkinen, et al.
Physical Chemistry Chemical Physics (2021) Vol. 24, Iss. 1, pp. 86-97
Open Access | Times Cited: 25
Huayuan Tang, Yuhuan Li, Aleksandr Käkinen, et al.
Physical Chemistry Chemical Physics (2021) Vol. 24, Iss. 1, pp. 86-97
Open Access | Times Cited: 25
Sulfation of hyaluronic acid reconfigures the mechanistic pathway of bone morphogenetic protein-2 aggregation
Devi Prasanna Behera, Suchismita Subadini, Uwe Freudenberg, et al.
International Journal of Biological Macromolecules (2024) Vol. 263, pp. 130128-130128
Closed Access | Times Cited: 3
Devi Prasanna Behera, Suchismita Subadini, Uwe Freudenberg, et al.
International Journal of Biological Macromolecules (2024) Vol. 263, pp. 130128-130128
Closed Access | Times Cited: 3
Inhibitory effects of carbon quantum dots towards hen egg white lysozyme amyloidogenesis through formation of a stable protein complex
M.P. Taraka Prabhu, Nandini Sarkar
Biophysical Chemistry (2021) Vol. 280, pp. 106714-106714
Closed Access | Times Cited: 23
M.P. Taraka Prabhu, Nandini Sarkar
Biophysical Chemistry (2021) Vol. 280, pp. 106714-106714
Closed Access | Times Cited: 23
Naringenin-Functionalized Gold Nanoparticles and Their Role in α-Synuclein Stabilization
Anupam Maity, Animesh Mondal, Shubham Kundu, et al.
Langmuir (2023) Vol. 39, Iss. 21, pp. 7231-7248
Closed Access | Times Cited: 9
Anupam Maity, Animesh Mondal, Shubham Kundu, et al.
Langmuir (2023) Vol. 39, Iss. 21, pp. 7231-7248
Closed Access | Times Cited: 9
Structural, kinetic, and thermodynamic aspects of insulin aggregation
Chinmaya Panda, Sachin Kumar, Sharad Gupta, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 36, pp. 24195-24213
Closed Access | Times Cited: 9
Chinmaya Panda, Sachin Kumar, Sharad Gupta, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 36, pp. 24195-24213
Closed Access | Times Cited: 9
Physicochemical Properties Altered by the Tail Group of Lipid Membranes Influence Huntingtin Aggregation and Lipid Binding
Maryssa Beasley, Nicolas C. Frazee, Sharon E. Groover, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 16, pp. 3067-3081
Closed Access | Times Cited: 14
Maryssa Beasley, Nicolas C. Frazee, Sharon E. Groover, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 16, pp. 3067-3081
Closed Access | Times Cited: 14
A computational strategy for therapeutic development against superoxide dismutase (SOD1) amyloid formation: effect of polyphenols on the various events in the aggregation pathway
Shilpa Sharma, Vijay Raj Tomar, Abhilash Jayaraj, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 8, pp. 6232-6246
Closed Access | Times Cited: 7
Shilpa Sharma, Vijay Raj Tomar, Abhilash Jayaraj, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 8, pp. 6232-6246
Closed Access | Times Cited: 7
Interactions of intrinsically disordered proteins with the unconventional chaperone human serum albumin: From mechanisms of amyloid inhibition to therapeutic opportunities
Karla Martinez Pomier, Rashik Ahmed, Giuseppe Melacini
Biophysical Chemistry (2021) Vol. 282, pp. 106743-106743
Closed Access | Times Cited: 16
Karla Martinez Pomier, Rashik Ahmed, Giuseppe Melacini
Biophysical Chemistry (2021) Vol. 282, pp. 106743-106743
Closed Access | Times Cited: 16
TAR DNA‐binding protein 43 oligomers in physiology and pathology
Yuh Shen Lye, Yun‐Ru Chen
IUBMB Life (2022) Vol. 74, Iss. 8, pp. 794-811
Closed Access | Times Cited: 12
Yuh Shen Lye, Yun‐Ru Chen
IUBMB Life (2022) Vol. 74, Iss. 8, pp. 794-811
Closed Access | Times Cited: 12
Stability of Protein Pharmaceuticals: Recent Advances
Mark C. Manning, Ryan E. Holcomb, R. W. Payne, et al.
Pharmaceutical Research (2024) Vol. 41, Iss. 7, pp. 1301-1367
Closed Access | Times Cited: 2
Mark C. Manning, Ryan E. Holcomb, R. W. Payne, et al.
Pharmaceutical Research (2024) Vol. 41, Iss. 7, pp. 1301-1367
Closed Access | Times Cited: 2
Improving the stability of insulin through effective chemical modifications: A Comprehensive review
Reyhane Kamelnia, Mahmood Ahmadi-Hamedani, Majid Darroudi, et al.
International Journal of Pharmaceutics (2024) Vol. 661, pp. 124399-124399
Closed Access | Times Cited: 2
Reyhane Kamelnia, Mahmood Ahmadi-Hamedani, Majid Darroudi, et al.
International Journal of Pharmaceutics (2024) Vol. 661, pp. 124399-124399
Closed Access | Times Cited: 2
Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots
Douglas B. Kell, Etheresia Pretorius
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 2
Douglas B. Kell, Etheresia Pretorius
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 2
Differential effect of polyol and sugar osmolytes on the refolding of homologous alpha amylases: A comparative study
Aziz Ahmad, Rajesh Mishra
Biophysical Chemistry (2021) Vol. 281, pp. 106733-106733
Closed Access | Times Cited: 15
Aziz Ahmad, Rajesh Mishra
Biophysical Chemistry (2021) Vol. 281, pp. 106733-106733
Closed Access | Times Cited: 15
Disordered regions tune order in chromatin organization and function
Shivangi Shukla, Prakhar Agarwal, Ashutosh Kumar
Biophysical Chemistry (2021) Vol. 281, pp. 106716-106716
Closed Access | Times Cited: 14
Shivangi Shukla, Prakhar Agarwal, Ashutosh Kumar
Biophysical Chemistry (2021) Vol. 281, pp. 106716-106716
Closed Access | Times Cited: 14
Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis
Emily Lewkowicz, Olga Gursky
Biophysical Chemistry (2021) Vol. 280, pp. 106699-106699
Open Access | Times Cited: 12
Emily Lewkowicz, Olga Gursky
Biophysical Chemistry (2021) Vol. 280, pp. 106699-106699
Open Access | Times Cited: 12
Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC
Helena Østergaard Rasmussen, Daniel E. Otzen, Jan Skov Pedersen
Journal of Biological Chemistry (2022) Vol. 298, Iss. 2, pp. 101569-101569
Open Access | Times Cited: 8
Helena Østergaard Rasmussen, Daniel E. Otzen, Jan Skov Pedersen
Journal of Biological Chemistry (2022) Vol. 298, Iss. 2, pp. 101569-101569
Open Access | Times Cited: 8
Mechanism of the interaction of toxic SOD1 fibrils with two potent polyphenols: curcumin and quercetin
Shilpa Sharma, Vijay Raj Tomar, Shashank Deep
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 34, pp. 23081-23091
Closed Access | Times Cited: 4
Shilpa Sharma, Vijay Raj Tomar, Shashank Deep
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 34, pp. 23081-23091
Closed Access | Times Cited: 4