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:

Miniproteins as a Powerful Modality in Drug Development
Zachary R. Crook, Natalie W. Nairn, James M. Olson
Trends in Biochemical Sciences (2020) Vol. 45, Iss. 4, pp. 332-346
Open Access | Times Cited: 67

Showing 26-50 of 67 citing articles:

Multivalent designed proteins protect against SARS-CoV-2 variants of concern
Andrew C. Hunt, James Brett Case, Young‐Jun Park, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 15

Miniproteins in medicinal chemistry
Agnieszka Ciesiołkiewicz, Juan Lizandra Pérez, Łukasz Berlicki
Bioorganic & Medicinal Chemistry Letters (2022) Vol. 71, pp. 128806-128806
Open Access | Times Cited: 10

Engineering defensin α‐helix to produce high‐affinitySARS‐CoV‐2 spike protein binding ligands
Leonardo Antônio Fernandes, Anderson Gomes, B.G. Guimarães, et al.
Protein Science (2022) Vol. 31, Iss. 6
Open Access | Times Cited: 9

Engineering an autonomous VH domain to modulate intracellular pathways and to interrogate the eIF4F complex
Yuri Frosi, Yen‐Chu Lin, Shimin Jiang, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 8

Replicating enzymatic activity by positioning active sites with synthetic protein scaffolds
Yujing Ding, Shanshan Zhang, Henry Hess, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

A Cell Based Assay Using Virus-like Particles to Screen AM Type Mimics for SARS-CoV-2 Neutralisation
Neeraj Gaur, Shreegauri Urankar, Durba Sengupta, et al.
Biochemical and Biophysical Research Communications (2024) Vol. 718, pp. 150082-150082
Closed Access | Times Cited: 1

Mutational and biophysical robustness in a prestabilized monobody
Peter G. Chandler, Li Lynn Tan, Benjamin T. Porebski, et al.
Journal of Biological Chemistry (2021) Vol. 296, pp. 100447-100447
Open Access | Times Cited: 10

Ex silico engineering of cystine-dense peptides yielding a potent bispecific T cell engager
Zachary R. Crook, Emily J. Girard, Gregory P. Sevilla, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 645
Open Access | Times Cited: 6

Microproteins: from behind the scenes to the spotlight
Meiqian Jiang, Huiqiang Lou, Wenya Hou
Genome Instability & Disease (2021) Vol. 2, Iss. 4, pp. 225-239
Closed Access | Times Cited: 8

GCN sensitive protein translation in yeast
W. Andrew Barr, Ruchi B. Sheth, Jack Kwon, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 7

GCN sensitive protein translation in yeast
William Barr, Ruchi B. Sheth, Jack Kwon, et al.
PLoS ONE (2020) Vol. 15, Iss. 9, pp. e0233197-e0233197
Open Access | Times Cited: 7

Selective Preference of Antibody Mimetics over Antibody, as Binding Molecules, for Diagnostic and Therapeutic Applications in Cancer Therapy
Pankaj Garg
Biointerface Research in Applied Chemistry (2020) Vol. 11, Iss. 3, pp. 10765-10775
Open Access | Times Cited: 7

Antibody mimetic drug conjugate manufactured by high-yield Escherichia coli expression and non-covalent binding system
Kenzo Yamatsugu, Hiroto Katoh, Takefumi Yamashita, et al.
Protein Expression and Purification (2021) Vol. 192, pp. 106043-106043
Open Access | Times Cited: 6

Combination of High-Resolution Structures for the B Cell Receptor and Co-Receptors Provides an Understanding of Their Interactions with Therapeutic Antibodies
Puja Bhattacharyya, Richard I. Christopherson, Kristen K. Skarratt, et al.
Cancers (2023) Vol. 15, Iss. 11, pp. 2881-2881
Open Access | Times Cited: 2

Development of a novel peptide aptamer that interacts with the eIF4E capped-mRNA binding site using peptide epitope linker evolution (PELE)
Yuri Frosi, Simon Ng, Yen‐Chu Lin, et al.
RSC Chemical Biology (2022) Vol. 3, Iss. 7, pp. 916-930
Open Access | Times Cited: 4

Miniprotein-Based Artificial Retroaldolase
Katarzyna Ożga, Łukasz Berlicki
ACS Catalysis (2022) Vol. 12, Iss. 24, pp. 15424-15430
Open Access | Times Cited: 4

Computational Design of Miniprotein Binders
Younes Bouchiba, Manon Ruffini, Thomas Schiex, et al.
Methods in molecular biology (2022), pp. 361-382
Closed Access | Times Cited: 3

Pathological complete remission of relapsed tumor by photo‐activating antibody–mimetic drug conjugate treatment
Yudai Kaneko, Kenzo Yamatsugu, Takefumi Yamashita, et al.
Cancer Science (2022) Vol. 113, Iss. 12, pp. 4350-4362
Open Access | Times Cited: 3

KcsA-Kv1.x chimeras with complete ligand-binding sites provide improved predictivity for screening selective Kv1.x blockers
Patrik Szekér, Tamás Bodó, Katalin Klima, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 4, pp. 107155-107155
Open Access

AI Prediction of Structural Stability of Nanoproteins Based on Structures and Residue Properties by Mean Pooled Dual Graph Convolutional Network
Daixi Li, Yuqi Zhu, Wujie Zhang, et al.
Interdisciplinary Sciences Computational Life Sciences (2024)
Closed Access

Design and characterization of defined alpha-helix mini-proteins, with intrinsic cell permeability
Xinchun Chen, Xiang‐Wei Kong, Pin Chen, et al.
Computational Biology and Chemistry (2024) Vol. 113, pp. 108271-108271
Closed Access

Molecular Display of the Animal Meta-Venome for Discovery of Novel Therapeutic Peptides
Meng-Hsuan Hsiao, Yang Miao, Zixing Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Thermostable WW-Domain Scaffold to Design Functional β-Sheet Miniproteins
Christina Lindner, Anke Friemel, Niklas Schwegler, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 24, pp. 16590-16600
Closed Access

Miniprotein engineering for inhibition of PD‐1/PDL1 interaction
Agnieszka Ciesiołkiewicz, Juan Lizandra Pérez, Łukasz Skalniak, et al.
Protein Science (2024) Vol. 33, Iss. 8
Closed Access

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