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:

VPS35 binds farnesylated N-Ras in the cytosol to regulate N-Ras trafficking
Mo Zhou, Heidi H. Wiener, Wenjuan Su, et al.
The Journal of Cell Biology (2016) Vol. 214, Iss. 4, pp. 445-458
Open Access | Times Cited: 48

Showing 1-25 of 48 citing articles:

Kinase-mediated RAS signaling via membraneless cytoplasmic protein granules
Asmin Tulpule, Juan Guan, Dana S. Neel, et al.
Cell (2021) Vol. 184, Iss. 10, pp. 2649-2664.e18
Open Access | Times Cited: 138

ABHD17 regulation of plasma membrane palmitoylation and N-Ras-dependent cancer growth
Jarrett R. Remsberg, Radu M. Suciu, Noemi A. Zambetti, et al.
Nature Chemical Biology (2021) Vol. 17, Iss. 8, pp. 856-864
Open Access | Times Cited: 87

RAB27B controls palmitoylation-dependent NRAS trafficking and signaling in myeloid leukemia
Jian‐Gang Ren, Bowen Xing, Kaosheng Lv, et al.
Journal of Clinical Investigation (2023) Vol. 133, Iss. 12
Open Access | Times Cited: 23

Protein lipidation in cancer: mechanisms, dysregulation and emerging drug targets
Edward W. Tate, Lior Soday, Ana Losada de la Lastra, et al.
Nature reviews. Cancer (2024) Vol. 24, Iss. 4, pp. 240-260
Closed Access | Times Cited: 14

Ras and the Plasma Membrane: A Complicated Relationship
Yong Zhou, Priyanka Prakash, Alemayehu A. Gorfe, et al.
Cold Spring Harbor Perspectives in Medicine (2017) Vol. 8, Iss. 10, pp. a031831-a031831
Open Access | Times Cited: 85

Posttranslational Modifications of RAS Proteins
Ian M. Ahearn, Mo Zhou, Mark R. Philips
Cold Spring Harbor Perspectives in Medicine (2018) Vol. 8, Iss. 11, pp. a031484-a031484
Open Access | Times Cited: 78

The RAS-Effector Interface: Isoform-Specific Differences in the Effector Binding Regions
Hossein Nakhaeizadeh, Ehsan Amin, Saeideh Nakhaei‐Rad, et al.
PLoS ONE (2016) Vol. 11, Iss. 12, pp. e0167145-e0167145
Open Access | Times Cited: 66

Targeting the Ras palmitoylation/depalmitoylation cycle in cancer
David Lin, Nicholas G. Davis, Elizabeth Conibear
Biochemical Society Transactions (2017) Vol. 45, Iss. 4, pp. 913-921
Open Access | Times Cited: 62

Comprehensive palmitoyl‐proteomic analysis identifies distinct protein signatures for large and small cancer‐derived extracellular vesicles
Javier Mariscal, Tatyana Vagner, Minhyung Kim, et al.
Journal of Extracellular Vesicles (2020) Vol. 9, Iss. 1
Open Access | Times Cited: 55

Post-translational modification of RAS proteins
Sharon L. Campbell, Mark R. Philips
Current Opinion in Structural Biology (2021) Vol. 71, pp. 180-192
Open Access | Times Cited: 51

Palmitoylation as a Key Regulator of Ras Localization and Function
Carla Busquets-Hernández, Gemma Triola
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 44

Regulation of protein prenylation
Dominik Jung, Hagen S. Bachmann
Biomedicine & Pharmacotherapy (2023) Vol. 164, pp. 114915-114915
Open Access | Times Cited: 20

Evaluation of the selectivity and sensitivity of isoform- and mutation-specific RAS antibodies
Andrew M. Waters, Irem Ozkan‐Dagliyan, Angelina V. Vaseva, et al.
Science Signaling (2017) Vol. 10, Iss. 498
Open Access | Times Cited: 57

Intrinsic protein disorder in oncogenic KRAS signaling
Ruth Nussinov, Hyunbum Jang, Chung‐Jung Tsai, et al.
Cellular and Molecular Life Sciences (2017) Vol. 74, Iss. 17, pp. 3245-3261
Closed Access | Times Cited: 54

Deciphering lipid codes: K‐Ras as a paradigm
Yong Zhou, John F. Hancock
Traffic (2017) Vol. 19, Iss. 3, pp. 157-165
Open Access | Times Cited: 49

DNA and RNA sequencing identified a novel oncogene VPS35 in liver hepatocellular carcinoma
Guiji Zhang, Xia Tang, Li Liang, et al.
Oncogene (2020) Vol. 39, Iss. 16, pp. 3229-3244
Closed Access | Times Cited: 34

A comprehensive in vivo screen of yeast farnesyltransferase activity reveals broad reactivity across a majority of CXXX sequences
June H Kim, Emily R. Hildebrandt, Anushka Sarkar, et al.
G3 Genes Genomes Genetics (2023) Vol. 13, Iss. 7
Open Access | Times Cited: 11

GOLGA7 is essential for NRAS trafficking from the Golgi to the plasma membrane but not for its palmitoylation
Chenxuan Liu, Bo Jiao, Peihong Wang, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 4

The Legionella pneumophila effector DenR hijacks the host NRas proto-oncoprotein to downregulate MAPK signaling
Stephanie S. Lehman, Chad D. Williamson, Trisha Tucholski, et al.
Cell Reports (2024) Vol. 43, Iss. 4, pp. 114033-114033
Open Access | Times Cited: 4

A small-molecule ICMT inhibitor delays senescence of Hutchinson-Gilford progeria syndrome cells
Xue Chen, Haidong Yao, Muhammad Kashif, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 25

PDEδ Binding to Ras Isoforms Provides a Route to Proper Membrane Localization
Serena Muratcioğlu, Hyunbum Jang, Attila Gürsoy, et al.
The Journal of Physical Chemistry B (2017) Vol. 121, Iss. 24, pp. 5917-5927
Open Access | Times Cited: 29

TFEB controls retromer expression in response to nutrient availability
Rachel Curnock, Alessia Calcagnì, Andrea Ballabio, et al.
The Journal of Cell Biology (2019) Vol. 218, Iss. 12, pp. 3954-3966
Open Access | Times Cited: 27

Splice switching an oncogenic ratio of SmgGDS isoforms as a strategy to diminish malignancy
Anthony Brandt, Lisa McNally, Ellen Lorimer, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 7, pp. 3627-3636
Open Access | Times Cited: 25

Fluorescent Biosensor for Measuring Ras Activity in Living Cells
Ryan Weeks, Xin Zhou, Tina L. Yuan, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 38, pp. 17432-17440
Open Access | Times Cited: 16

Page 1 - Next Page

Scroll to top