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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:

A look back at the molten globule state of proteins: thermodynamic aspects
Eva Judy, Nand Kishore
Biophysical Reviews (2019) Vol. 11, Iss. 3, pp. 365-375
Open Access | Times Cited: 47

Showing 26-50 of 47 citing articles:

Conformational stability of peroxidase from the latex of Artocarpus lakoocha: influence of pH, chaotropes, and temperature
Kirti Shila Sonkar, Manendra Pachauri, Amit Kumar, et al.
Frontiers in Plant Science (2024) Vol. 15
Open Access
Proline Isomerization and Molten Globular Property of TgPDCD5 Secreted from Toxoplasma gondii Confers Its Regulation of Heparin Sulfate Binding
Meng-Hsuan Lin, Tsunai Yu, Chi‐Fon Chang, et al.
JACS Au (2024) Vol. 4, Iss. 5, pp. 1763-1774
Open Access
Spectroscopic analysis of the bacterially expressed head domain of rotavirus VP6
Milaan Simone Strachan, Tshepo Mashapa, Samantha Gildenhuys
Bioscience Reports (2024) Vol. 44, Iss. 5
Open Access
Application of SUMO fusion technology for the enhancement of stability and activity of lysophospholipase from Pyrococcus abyssi
Arshia Nazir, Mohsin Shad, Hafiz Muzzammel Rehman, et al.
World Journal of Microbiology and Biotechnology (2024) Vol. 40, Iss. 6
Closed Access
Amino Acid Residue-Specific Ramachandran Distributions Derived from a Simple Mean Field Potential
Brian Andrews
ACS Physical Chemistry Au (2024) Vol. 4, Iss. 6, pp. 707-719
Open Access
Pyroptotic executioner pore-forming protein GSDMD forms oligomeric assembly and exhibits amyloid-like attributes that could contribute for its pore-forming function
Shamaita Chatterjee, Tarang Gupta, Gurvinder Kaur, et al.
Biochemical Journal (2024) Vol. 481, Iss. 22, pp. 1679-1705
Open Access
A simple method for computationally unstructuring proteins: some findings
Alexander M. Powell
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Probing Aromatic Side Chains Reveals the Site-Specific Melting in the SUMO1 Molten Globule
S. L. Arora, Sri Rama Koti Ainavarapu
Biochemistry (2024)
Closed Access
Human aldose reductase unfolds through an intermediate
Gurprit Sekhon, Ranvir Singh
F1000Research (2019) Vol. 8, pp. 564-564
Open Access | Times Cited: 5
Exploring the folding process of human βB2-crystallin using multiscale molecular dynamics and the Markov state model
José‐Luis Velasco‐Bolom, Laura Domı́nguez
Physical Chemistry Chemical Physics (2020) Vol. 22, Iss. 46, pp. 26753-26763
Closed Access | Times Cited: 5
Proteolytic processing induces a conformational switch required for antibacterial toxin delivery
Nicholas L. Bartelli, Victor J. Passanisi, K. Michalska, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 3
Structure and dynamics of the mitochondrial DNA-compaction factor Abf2 from S. cerevisiae
Jens Lidman, Ylber Sallova, Irena Matečko‐Burmann, et al.
Journal of Structural Biology (2023) Vol. 215, Iss. 3, pp. 108008-108008
Open Access | Times Cited: 1
Human aldose reductase unfolds through an intermediate.
Gurprit Sekhon, Ranvir Singh
F1000Research (2019) Vol. 8, pp. 564-564
Open Access | Times Cited: 3
The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin
Elek Telek, Kristóf Karádi, József Kardos, et al.
Journal of Biological Chemistry (2021) Vol. 297, Iss. 1, pp. 100716-100716
Open Access | Times Cited: 3
Unraveling the structural basis of urea-induced unfolding of Fasciola gigantica cytosolic malate dehydrogenase
Purna Bahadur Chetri, Rohit Shukla, Javed Masood Khan, et al.
Journal of Molecular Liquids (2021) Vol. 349, pp. 118170-118170
Closed Access | Times Cited: 3
Singlet oxygen quenching as a probe for cytochrome c molten globule state formation
Andrej Hovan, Dagmar Sedláková, Martin Berta, et al.
Physical Chemistry Chemical Physics (2022) Vol. 24, Iss. 21, pp. 13317-13324
Closed Access | Times Cited: 2
Conformational Stability of Peroxidase from latex ofArtocarpus lakoocha: Influence of pH, Chaotropes, and Temperature
Kirti Shila Sonkar, Manendra Pachauri, Amit Kumar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Thermodynamics of modulation of interaction of α-helix inducer 2, 2, 2-trifluoroethanol with lysozyme in presence of cationic, anionic and non-ionic surfactants
Anju Arya, Anu Jain, Nand Kishore
Journal of Biomolecular Structure and Dynamics (2023) Vol. 42, Iss. 14, pp. 7289-7303
Open Access
Single-chain Fv antibody covalently linked to antigen peptides and its structural evaluation
Takahiro Hayashi, Maki Kawasaki, Yuji O. Kamatari, et al.
Analytical Biochemistry (2021) Vol. 629, pp. 114312-114312
Closed Access | Times Cited: 1
Room Temperature Intrinsic Emission Ratio of BSA Correlates With Percent Aggregates During Long-Term Storage
Joel D. Manrrique, Zakiya K. Powell, Ryan M. Brock, et al.
Journal of Pharmaceutical Sciences (2020) Vol. 110, Iss. 3, pp. 1120-1129
Closed Access
Deciphering the mechanism of interaction between two key subunits from the Type IV Secretion System core complex: VirB9 and VirB7
Angy Liseth Davalos Macias
(2022)
Open Access
Polyols, increasing global stability of cytochrome c, destabilize the thermal unfolding intermediate
K. Tejaswi Naidu, N. Prakash Prabhu
Journal of Biomolecular Structure and Dynamics (2021) Vol. 40, Iss. 21, pp. 11216-11228
Closed Access
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