Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach
Rupasree Brahma, H. Raghuraman
Emerging Topics in Life Sciences (2021) Vol. 5, Iss. 1, pp. 89-101
Open Access | Times Cited: 17

Showing 17 citing articles:

Structural Dynamics of the Slide Helix of Inactive/Closed Conformation of KirBac1.1 in Micelles and Membranes: A Fluorescence Approach
Arpan Bysack, Chandrima Jash, H. Raghuraman
The Journal of Membrane Biology (2025)
Open Access
Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores
Rupasree Brahma, A. Das, H. Raghuraman
STAR Protocols (2022) Vol. 3, Iss. 1, pp. 101200-101200
Open Access | Times Cited: 11
Hydration Dynamics in Biological Membranes: Emerging Applications of Terahertz Spectroscopy
Sreetama Pal, Amitabha Chattopadhyay
The Journal of Physical Chemistry Letters (2021) Vol. 12, Iss. 39, pp. 9697-9709
Closed Access | Times Cited: 15
Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins
Rupasree Brahma, H. Raghuraman
The Journal of Membrane Biology (2022) Vol. 255, Iss. 4-5, pp. 469-483
Closed Access | Times Cited: 10
Cholesterol modulates the structural dynamics of the paddle motif loop of KvAP voltage sensor
A. Das, Arpan Bysack, H. Raghuraman
Current Research in Structural Biology (2024) Vol. 7, pp. 100137-100137
Open Access | Times Cited: 1
Conformational heterogeneity of the voltage sensor loop of KvAP in micelles and membranes: A fluorescence approach
A. Das, H. Raghuraman
Biochimica et Biophysica Acta (BBA) - Biomembranes (2021) Vol. 1863, Iss. 5, pp. 183568-183568
Closed Access | Times Cited: 9
Fluorescence Emission of Self‐assembling Amyloid‐like Peptides: Solution versus Solid State
Carlo Diaferia, Chiara Schiattarella, Enrico Gallo, et al.
ChemPhysChem (2021) Vol. 22, Iss. 21, pp. 2215-2221
Open Access | Times Cited: 9
Effectiveness of dual-detergent strategy using Triton X-100 in membrane protein purification
Anindita Das, Arpan Bysack, H. Raghuraman
Biochemical and Biophysical Research Communications (2021) Vol. 578, pp. 122-128
Closed Access | Times Cited: 9
Characterization of a novel MgtE homolog and its structural dynamics in membrane mimetics
Rupasree Brahma, H. Raghuraman
Biophysical Journal (2023) Vol. 123, Iss. 14, pp. 1968-1983
Open Access | Times Cited: 3
Environment-Sensitive Fluorescence of 7-Nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-Labeled Ligands for Serotonin Receptors
Parijat Sarkar, Kaleeckal G. Harikumar, Satinder S. Rawat, et al.
Molecules (2021) Vol. 26, Iss. 13, pp. 3848-3848
Open Access | Times Cited: 8
Cost‐effective Purification of Membrane Proteins using a Dual‐detergent Strategy
Rupasree Brahma, H. Raghuraman
Current Protocols (2022) Vol. 2, Iss. 6
Open Access | Times Cited: 5
A Thermodynamic Model for Interpreting Tryptophan Excitation-Energy-Dependent Fluorescence Spectra Provides Insight Into Protein Conformational Sampling and Stability
A Kwok, Inês S. Camacho, Samuel D. Winter, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 7
Multi-Site Red-Edge Excitation Shift Reveals the Residue-Specific Solvation Dynamics during the Native to Amyloid-like Transition of an Amyloidogenic Protein
Sonal R More, Santosh Kumar Jha
The Journal of Physical Chemistry B (2024)
Closed Access
Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition
Annmaree K. Warrender, Jolyn Pan, C.J. Pudney, et al.
Journal of The Royal Society Interface (2023) Vol. 20, Iss. 208
Open Access | Times Cited: 1
Lack of Environmental Sensitivity of a Naturally Occurring Fluorescent Analog of Cholesterol
Amitabha Chattopadhyay, Samares C. Biswas, R. Rukmini, et al.
Journal of Fluorescence (2021) Vol. 31, Iss. 5, pp. 1401-1407
Closed Access | Times Cited: 3
Comparative Analysis of Tryptophan Dynamics in Spectrin and Its Constituent Domains: Insights from Fluorescence
Sreetama Pal, Dipayan Bose, Abhijit Chakrabarti, et al.
The Journal of Physical Chemistry B (2021) Vol. 126, Iss. 5, pp. 1045-1053
Closed Access | Times Cited: 3
Delving into Membrane Heterogeneity Utilizing Fluorescence Lifetime Distribution Analysis
Sourav Haldar
The Journal of Membrane Biology (2022) Vol. 255, Iss. 4-5, pp. 553-561
Closed Access | Times Cited: 2
Page 1

Scroll to top