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:

Differential Neuropeptidomes of Dense Core Secretory Vesicles (DCSV) Produced at Intravesicular and Extracellular pH Conditions by Proteolytic Processing
Zhenze Jiang, Christopher B. Lietz, Sonia Podvin, et al.
ACS Chemical Neuroscience (2021) Vol. 12, Iss. 13, pp. 2385-2398
Open Access | Times Cited: 17

Showing 17 citing articles:

Peptidomics
Roland Hellinger, Arnar Sigurdsson, Wenxin Wu, et al.
Nature Reviews Methods Primers (2023) Vol. 3, Iss. 1
Open Access | Times Cited: 56
Cathepsin B Gene Knockout Improves Behavioral Deficits and Reduces Pathology in Models of Neurologic Disorders
Gregory Hook, Thomas Reinheckel, Junjun Ni, et al.
Pharmacological Reviews (2022) Vol. 74, Iss. 3, pp. 600-629
Open Access | Times Cited: 62
Dysregulation of Neuropeptide and Tau Peptide Signatures in Human Alzheimer’s Disease Brain
Sonia Podvin, Zhenze Jiang, Ben Boyarko, et al.
ACS Chemical Neuroscience (2022) Vol. 13, Iss. 13, pp. 1992-2005
Open Access | Times Cited: 26
Molecular Features of CA-074 pH-Dependent Inhibition of Cathepsin B
Michael C. Yoon, Mitchell P. Christy, Von V. Phan, et al.
Biochemistry (2022) Vol. 61, Iss. 4, pp. 228-238
Open Access | Times Cited: 23
Cathepsin B Dipeptidyl Carboxypeptidase and Endopeptidase Activities Demonstrated across a Broad pH Range
Michael C. Yoon, Vivian Hook, Anthony J. O’Donoghue
Biochemistry (2022) Vol. 61, Iss. 17, pp. 1904-1914
Open Access | Times Cited: 19
Simultaneous Counting of Molecules in the Halo and Dense‐Core of Nanovesicles by Regulating Dynamics of Vesicle Opening
Xiulan He, Andrew G. Ewing
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 15
Open Access | Times Cited: 13
Distinct Cleavage Properties of Cathepsin B Compared to Cysteine Cathepsins Enable the Design and Validation of a Specific Substrate for Cathepsin B over a Broad pH Range
Michael C. Yoon, Von V. Phan, Sonia Podvin, et al.
Biochemistry (2023) Vol. 62, Iss. 15, pp. 2289-2300
Open Access | Times Cited: 7
Multiplex substrate profiling by mass spectrometry for proteases
Peter J. Rohweder, Zhenze Jiang, Brianna M. Hurysz, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2022), pp. 375-411
Open Access | Times Cited: 12
Neurotransmitter Readily Escapes Detection at the Opposing Microelectrode Surface in Typical Amperometric Measurements of Exocytosis at Single Cells
Gregory S. McCarty, Lars E. Dunaway, J. Dylan Denison, et al.
Analytical Chemistry (2022) Vol. 94, Iss. 27, pp. 9548-9556
Open Access | Times Cited: 10
Human iN neuronal model of schizophrenia displays dysregulation of chromogranin B and related neuropeptide transmitter signatures
Sonia Podvin, Jeffrey R. Jones, Austin Kang, et al.
Molecular Psychiatry (2024) Vol. 29, Iss. 5, pp. 1440-1449
Open Access | Times Cited: 1
Distinct Dibasic Cleavage Specificities of Neuropeptide-Producing Cathepsin L and Cathepsin V Cysteine Proteases Compared to PC1/3 and PC2 Serine Proteases
Michael C. Yoon, Janneca Ames, Charles Mosier, et al.
ACS Chemical Neuroscience (2022) Vol. 13, Iss. 2, pp. 245-256
Open Access | Times Cited: 6
Mass Spectrometry Measurements of Neuropeptides: From Identification to Quantitation
Eduardo A. De La Toba, Sara E. Bell, Elena V. Romanova, et al.
Annual Review of Analytical Chemistry (2022) Vol. 15, Iss. 1, pp. 83-106
Open Access | Times Cited: 6
Simultaneous Counting of Molecules in the Halo and Dense‐Core of Nanovesicles by Regulating Dynamics of Vesicle Opening
Xiulan He, Andrew G. Ewing
Angewandte Chemie (2022) Vol. 134, Iss. 15
Open Access | Times Cited: 5
Untapped Potential: Real-Time Measurements of Opioid Exocytosis at Single Cells
J. Dylan Denison, A. Chathuri De Alwis, Ruby Shah, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 44, pp. 24071-24080
Closed Access | Times Cited: 2
Investigating the role of phenylalanine residues for amyloid formation of the neuropeptide neurokinin B
Bhawantha M. Jayawardena, A Azzi, Christopher E. Jones
Biochemical and Biophysical Research Communications (2024) Vol. 705, pp. 149732-149732
Open Access
Aspartic proteases are abundant and active in acidified wound fluid
Elany Barbosa da Silva, Meredith J. Crane, Lawrence Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Exploiting Microelectrode Geometry for Comprehensive Detection of Individual Exocytosis Events at Single Cells
A. Chathuri De Alwis, J. Dylan Denison, Ruby Shah, et al.
ACS Sensors (2023) Vol. 8, Iss. 8, pp. 3187-3194
Open Access | Times Cited: 1
Page 1

Scroll to top