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:

Showing 1-25 of 35 citing articles:

Mass Spectrometry Imaging in Alzheimer's Disease
Masaya Ikegawa, Nobuto Kakuda, Tomohiro Miyasaka, et al.
Brain Connectivity (2023) Vol. 13, Iss. 6, pp. 319-333
Open Access | Times Cited: 14

A near-infrared fluorescent probe for the detection of mitochondrial viscosity and its application in the imaging of Alzheimer’s disease mice brain
Xinghao Li, Sitong Hang, Yingyong Hou, et al.
Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy (2025) Vol. 334, pp. 125924-125924
Closed Access

Structure Elucidation and Discrimination of Peptides Epimers Induced by Chiral Residue by Ion Mobility Mass Spectrometry
Jianglong Du, Shutong Yang, Yanqiu Chu, et al.
Analytica Chimica Acta (2025), pp. 344000-344000
Closed Access

Does Data-Independent Acquisition Data Contain Hidden Gems? A Case Study Related to Alzheimer’s Disease
Evan E. Hubbard, Lilian R. Heil, Gennifer E. Merrihew, et al.
Journal of Proteome Research (2021) Vol. 21, Iss. 1, pp. 118-131
Open Access | Times Cited: 26

Species-level discrimination of microorganisms by high-resolution paper spray – Ion mobility – Mass spectrometry
Orobola E. Olajide, Yuyan Yi, Jingyi Zheng, et al.
International Journal of Mass Spectrometry (2022) Vol. 478, pp. 116871-116871
Closed Access | Times Cited: 15

PIMT-Mediated Labeling of l-Isoaspartic Acid with Tris Facilitates Identification of Isomerization Sites in Long-Lived Proteins
Jacob W. Silzel, Tyler R. Lambeth, Ryan R. Julian
Journal of the American Society for Mass Spectrometry (2022) Vol. 33, Iss. 3, pp. 548-556
Open Access | Times Cited: 13

Traversing through the cell signaling pathways of neuroprotection by betanin: therapeutic relevance to Alzheimer’s Disease and Parkinson’s Disease
Banashree Chetia Phukan, Rubina Roy, Rajib Paul, et al.
Metabolic Brain Disease (2023) Vol. 38, Iss. 3, pp. 805-817
Closed Access | Times Cited: 7

Mass spectrometric studies of the variety of beta‐amyloid proteoforms in Alzheimer's disease
Natalia V. Zakharova, А. С. Кононихин, Maria I. Indeykina, et al.
Mass Spectrometry Reviews (2022)
Closed Access | Times Cited: 11

Enhanced ion mobility resolution of Abeta isomers from human brain using high-resolution demultiplexing software
Soumya Mukherjee, John C. Fjeldsted, Colin L. Masters, et al.
Analytical and Bioanalytical Chemistry (2022) Vol. 414, Iss. 18, pp. 5683-5693
Closed Access | Times Cited: 11

Quantitative proteomics of tau and Aβ in detergent fractions from Alzheimer's disease brains
Soumya Mukherjee, Céline Dubois, Keyla Perez, et al.
Journal of Neurochemistry (2022) Vol. 164, Iss. 4, pp. 529-552
Closed Access | Times Cited: 11

Site-specific chirality-conferred structural compaction differentially mediates the cytotoxicity of Aβ42
Gongyu Li, Chae Kyung Jeon, M Ma, et al.
Chemical Science (2023) Vol. 14, Iss. 22, pp. 5936-5944
Open Access | Times Cited: 6

Distinct Effects of Beta-Amyloid, Its Isomerized and Phosphorylated Forms on the Redox Status and Mitochondrial Functioning of the Blood–Brain Barrier Endothelium
Aleksandra Petrovskaya, Artem M. Tverskoi, Evgeny P. Barykin, et al.
International Journal of Molecular Sciences (2022) Vol. 24, Iss. 1, pp. 183-183
Open Access | Times Cited: 10

The Hidden Role of Non-Canonical Amyloid β Isoforms in Alzheimer’s Disease
Lukas Busch, Simone Eggert, Kristina Endres, et al.
Cells (2022) Vol. 11, Iss. 21, pp. 3421-3421
Open Access | Times Cited: 9

Separation of amyloid β fragment peptides with racemised and isomerised aspartic acid residues using an original chiral resolution labeling reagent
Makoto Ozaki, Motoshi Shimotsuma, Takefumi Kuranaga, et al.
The Analyst (2023) Vol. 148, Iss. 6, pp. 1209-1213
Closed Access | Times Cited: 5

Role of Interaction between Zinc and Amyloid Beta in Pathogenesis of Alzheimer’s Disease
Sergey A. Kozin
Biochemistry (Moscow) (2023) Vol. 88, Iss. S1, pp. S75-S87
Closed Access | Times Cited: 5

Switching On/Off Amyloid Plaque Formation in Transgenic Animal Models of Alzheimer’s Disease
Sergey A. Kozin, Olga I. Kechko, Alexei A. Adzhubei, et al.
International Journal of Molecular Sciences (2023) Vol. 25, Iss. 1, pp. 72-72
Open Access | Times Cited: 5

Citrullination of Amyloid-β Peptides in Alzheimer’s Disease
Soumya Mukherjee, Keyla Perez, Céline Dubois, et al.
ACS Chemical Neuroscience (2021) Vol. 12, Iss. 19, pp. 3719-3732
Closed Access | Times Cited: 12

Influence of Asp Isomerization on Trypsin and Trypsin-like Proteolysis
Jacob W. Silzel, Gili Ben‐Nissan, Jin Tang, et al.
Analytical Chemistry (2022) Vol. 94, Iss. 44, pp. 15288-15296
Open Access | Times Cited: 8

Intermediate Antiparallel β Structure in Amyloid β Plaques Revealed by Infrared Spectroscopic Imaging
Brooke Holcombe, Abigail Foes, Siddhartha Banerjee, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 20, pp. 3794-3803
Closed Access | Times Cited: 4

Post-translational modifications of beta-amyloid alter its transport in the blood-brain barrier in vitro model
Kseniya B. Varshavskaya, Irina Yu. Petrushanko, Vladimir A. Mitkevich, et al.
Frontiers in Molecular Neuroscience (2024) Vol. 17
Open Access | Times Cited: 1

Beta-Amyloid and Its Asp7 Isoform: Morphological and Aggregation Properties and Effects of Intracerebroventricular Administration
Valeria Ushakova, Yana Zorkina, Olga Abramova, et al.
Brain Sciences (2024) Vol. 14, Iss. 10, pp. 1042-1042
Open Access | Times Cited: 1

Identification of isoAsp7-Aβ as a major Aβ variant in Alzheimer’s disease, dementia with Lewy bodies and vascular dementia
Sarah Schrempel, Anna Katharina Kottwitz, Anke Piechotta, et al.
Acta Neuropathologica (2024) Vol. 148, Iss. 1
Open Access | Times Cited: 1

The Dynamics of β-Amyloid Proteoforms Accumulation in the Brain of a 5xFAD Mouse Model of Alzheimer’s Disease
Anna E. Bugrova, Polina A. Strelnikova, Maria I. Indeykina, et al.
International Journal of Molecular Sciences (2021) Vol. 23, Iss. 1, pp. 27-27
Open Access | Times Cited: 10

Zn-dependent β-amyloid Aggregation and its Reversal by the Tetrapeptide HAEE
Vladimir A. Mitkevich, Evgeny P. Barykin, S. Yu. Eremina, et al.
Aging and Disease (2022)
Open Access | Times Cited: 6

Page 1 - Next Page

Scroll to top