Hui-Ling Chiang

2.1k total citations · 1 hit paper
28 papers, 1.8k citations indexed

About

Hui-Ling Chiang is a scholar working on Cell Biology, Molecular Biology and Epidemiology. According to data from OpenAlex, Hui-Ling Chiang has authored 28 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Cell Biology, 19 papers in Molecular Biology and 9 papers in Epidemiology. Recurrent topics in Hui-Ling Chiang's work include Endoplasmic Reticulum Stress and Disease (24 papers), Cellular transport and secretion (15 papers) and Autophagy in Disease and Therapy (9 papers). Hui-Ling Chiang is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (24 papers), Cellular transport and secretion (15 papers) and Autophagy in Disease and Therapy (9 papers). Hui-Ling Chiang collaborates with scholars based in United States. Hui-Ling Chiang's co-authors include Stanley R. Terlecky, J. Fred Dice, Randy Schekman, C. Randell Brown, Pei‐Hsin Huang, Susan Hamamoto, Jingjing Liu, Bruce A. Stanley, Dongying Cui and Yong Chen and has published in prestigious journals such as Nature, Science and Journal of Biological Chemistry.

In The Last Decade

Hui-Ling Chiang

28 papers receiving 1.7k citations

Hit Papers

A Role for a 70-Kilodalton Heat Shock Protein in Lysosoma... 1989 2026 2001 2013 1989 250 500 750

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Hui-Ling Chiang United States 19 1.3k 836 563 126 113 28 1.8k
Jason A. MacGurn United States 17 1.5k 1.2× 907 1.1× 509 0.9× 90 0.7× 109 1.0× 30 2.2k
Ryan J. Schulze United States 18 806 0.6× 426 0.5× 759 1.3× 325 2.6× 111 1.0× 26 2.0k
Jean H. Overmeyer United States 20 941 0.8× 545 0.7× 579 1.0× 119 0.9× 142 1.3× 28 1.8k
Eric D. Spear United States 13 1.0k 0.8× 819 1.0× 329 0.6× 109 0.9× 131 1.2× 18 1.4k
Robert Gauss Germany 12 790 0.6× 667 0.8× 292 0.5× 85 0.7× 144 1.3× 13 1.1k
Thomas A. Vida United States 16 1.5k 1.2× 1.4k 1.7× 281 0.5× 158 1.3× 71 0.6× 29 2.1k
Koichiro Takeshige Japan 8 848 0.7× 589 0.7× 931 1.7× 98 0.8× 73 0.6× 11 1.5k
Li‐Lin Du China 28 2.0k 1.6× 841 1.0× 505 0.9× 201 1.6× 71 0.6× 102 2.6k
Alexei Korennykh United States 22 1.7k 1.3× 1.3k 1.5× 608 1.1× 99 0.8× 502 4.4× 31 2.5k
Adriana L. Rojas Spain 19 940 0.8× 644 0.8× 169 0.3× 266 2.1× 123 1.1× 44 1.6k

Countries citing papers authored by Hui-Ling Chiang

Since Specialization
Citations

This map shows the geographic impact of Hui-Ling Chiang's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Hui-Ling Chiang with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Hui-Ling Chiang more than expected).

Fields of papers citing papers by Hui-Ling Chiang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Hui-Ling Chiang. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Hui-Ling Chiang. The network helps show where Hui-Ling Chiang may publish in the future.

Co-authorship network of co-authors of Hui-Ling Chiang

This figure shows the co-authorship network connecting the top 25 collaborators of Hui-Ling Chiang. A scholar is included among the top collaborators of Hui-Ling Chiang based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Hui-Ling Chiang. Hui-Ling Chiang is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Hong‐Brown, Ly Q., et al.. (2020). Intracellular vesicle clusters are organelles that synthesize extracellular vesicle–associated cargo proteins in yeast. Journal of Biological Chemistry. 295(9). 2650–2663. 17 indexed citations
2.
Hong‐Brown, Ly Q., et al.. (2017). The Shape of Vesicle-Containing Organelles Is Critical for Their Functions in Vesicle Endocytosis. DNA and Cell Biology. 36(11). 909–921. 4 indexed citations
3.
Chiang, Hui-Ling, et al.. (2016). Yeast as a Model System to Study Trafficking of Small Vesicles Carrying Signal-less Proteins In and Out of the Cell. Current Protein and Peptide Science. 17(8). 808–820. 6 indexed citations
4.
Stanley, Bruce A., et al.. (2014). Glucose induces rapid changes in the secretome of Saccharomyces cerevisiae. Proteome Science. 12(1). 9–9. 38 indexed citations
5.
Stanley, Bruce A., et al.. (2012). Comparative proteomic analysis of transition of saccharomyces cerevisiae from glucose-deficient medium to glucose-rich medium. Proteome Science. 10(1). 40–40. 20 indexed citations
6.
Chiang, Hui-Ling, et al.. (2012). Vid30 is required for the association of Vid vesicles and actin patches in the vacuole import and degradation pathway. Autophagy. 8(1). 29–46. 21 indexed citations
7.
Chiang, Hui-Ling, et al.. (2012). Vps34p Is Required for the Decline of Extracellular Fructose-1,6-bisphosphatase in the Vacuole Import and Degradation Pathway. Journal of Biological Chemistry. 287(39). 33080–33093. 23 indexed citations
9.
Brown, Caroline & Hui-Ling Chiang. (2009). A selective autophagy pathway that degrades gluconeogenic enzymes during catabolite inactivation. Communicative & Integrative Biology. 2(2). 177–183. 15 indexed citations
10.
Brown, C. Randell, et al.. (2009). The Vacuole Import and Degradation Pathway Utilizes Early Steps of Endocytosis and Actin Polymerization to Deliver Cargo Proteins to the Vacuole for Degradation. Journal of Biological Chemistry. 285(2). 1516–1528. 22 indexed citations
11.
Brown, C. Randell, et al.. (2008). The Vacuolar Import and Degradation Pathway Merges with the Endocytic Pathway to Deliver Fructose-1,6-bisphosphatase to the Vacuole for Degradation. Journal of Biological Chemistry. 283(38). 26116–26127. 34 indexed citations
12.
Liu, Jingjing, C. Randell Brown, & Hui-Ling Chiang. (2005). Degradation of the Gluconeogenic Enzyme Fructose-1,6-Bisphosphatase is Dependent on the Vacuolar ATPase. Autophagy. 1(3). 146–156. 9 indexed citations
13.
Brown, C. Randell, et al.. (2004). Degradation of the Gluconeogenic Enzymes Fructose-1,6-bisphosphatase and Malate Dehydrogenase Is Mediated by Distinct Proteolytic Pathways and Signaling Events. Journal of Biological Chemistry. 279(47). 49138–49150. 88 indexed citations
14.
Brown, C. Randell, et al.. (2003). The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery. Journal of Biological Chemistry. 278(28). 25688–25699. 21 indexed citations
15.
Brown, C. Randell, et al.. (2002). Vid22p, a novel plasma membrane protein, is required for the fructose-1,6-bisphosphatase degradation pathway. Journal of Cell Science. 115(3). 655–666. 38 indexed citations
16.
Brown, C. Randell, et al.. (2001). Cyclophilin A Mediates Vid22p Function in the Import of Fructose-1,6-bisphosphatase into Vid Vesicles. Journal of Biological Chemistry. 276(51). 48017–48026. 54 indexed citations
17.
Chen, Yong, et al.. (2001). Biochemical Analysis of Fructose-1,6-bisphosphatase Import into Vacuole Import and Degradation Vesicles Reveals a Role for UBC1 in Vesicle Biogenesis. Journal of Biological Chemistry. 276(13). 10398–10406. 35 indexed citations
18.
Huang, Pei‐Hsin & Hui-Ling Chiang. (1997). Identification of Novel Vesicles in the Cytosol to Vacuole Protein Degradation Pathway. The Journal of Cell Biology. 136(4). 803–810. 79 indexed citations
19.
Chiang, Hui-Ling, Randy Schekman, & Susan Hamamoto. (1996). Selective Uptake of Cytosolic, Peroxisomal, and Plasma Membrane Proteins into the Yeast Lysosome for Degradation. Journal of Biological Chemistry. 271(17). 9934–9941. 91 indexed citations
20.
Chiang, Hui-Ling, et al.. (1989). A Role for a 70-Kilodalton Heat Shock Protein in Lysosomal Degradation of Intracellular Proteins. Science. 246(4928). 382–385. 774 indexed citations breakdown →

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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