G G Chang

442 total citations
26 papers, 391 citations indexed

About

G G Chang is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, G G Chang has authored 26 papers receiving a total of 391 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 6 papers in Materials Chemistry and 4 papers in Oncology. Recurrent topics in G G Chang's work include Enzyme Structure and Function (6 papers), Connexins and lens biology (5 papers) and Glutathione Transferases and Polymorphisms (4 papers). G G Chang is often cited by papers focused on Enzyme Structure and Function (6 papers), Connexins and lens biology (5 papers) and Glutathione Transferases and Polymorphisms (4 papers). G G Chang collaborates with scholars based in Taiwan, Japan and China. G G Chang's co-authors include H J Lee, Sy Han Chiou, Si‐Fu Tang, Tsu‐Chung Chang, Shan Tang, Shih‐Ming Huang, Wen‐Yi Chou, Shyh‐Horng Chiou, Tzu‐Yi Chuang and Ko‐Tao Lee and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Biochemical Journal.

In The Last Decade

G G Chang

25 papers receiving 384 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
G G Chang Taiwan 14 288 101 52 42 39 26 391
T Baranowski Poland 11 224 0.8× 98 1.0× 68 1.3× 97 2.3× 27 0.7× 54 418
Mohan S. Saini United States 10 211 0.7× 46 0.5× 34 0.7× 27 0.6× 87 2.2× 19 358
Ingeborg A. Brand Germany 12 265 0.9× 48 0.5× 30 0.6× 46 1.1× 57 1.5× 16 487
R.K. Wierenga Netherlands 4 287 1.0× 144 1.4× 36 0.7× 21 0.5× 9 0.2× 4 368
Debamita Paul United States 9 265 0.9× 71 0.7× 33 0.6× 38 0.9× 53 1.4× 16 466
I.B. Zbarsky Russia 13 417 1.4× 56 0.6× 37 0.7× 53 1.3× 15 0.4× 22 523
A Sillero Spain 16 413 1.4× 49 0.5× 47 0.9× 36 0.9× 164 4.2× 28 674
Judy M. Bratt United States 8 368 1.3× 77 0.8× 53 1.0× 38 0.9× 16 0.4× 10 446
H G Bock United States 9 390 1.4× 53 0.5× 215 4.1× 45 1.1× 30 0.8× 9 577
Malcolm J. Kavarana United States 11 262 0.9× 47 0.5× 27 0.5× 49 1.2× 12 0.3× 14 452

Countries citing papers authored by G G Chang

Since Specialization
Citations

This map shows the geographic impact of G G Chang'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 G G Chang with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites G G Chang more than expected).

Fields of papers citing papers by G G Chang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by G G Chang. 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 G G Chang. The network helps show where G G Chang may publish in the future.

Co-authorship network of co-authors of G G Chang

This figure shows the co-authorship network connecting the top 25 collaborators of G G Chang. A scholar is included among the top collaborators of G G Chang 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 G G Chang. G G Chang 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.
Hung, Hui‐Chih, et al.. (2005). (De Biochemistry, 44:12737-12745)Functional roles of ATP-binding residues in the catalytic site of human mitochondrial NAD(P)(+)-dependent malic enzyme. 5 indexed citations
2.
Hung, Hui‐Chih, et al.. (2004). (Biochemistry, 43:7382-7390)Dual Functional Roles of ATP in Human Mitochondrial Malic Enzyme. 2 indexed citations
3.
Ignatius, Arun Alphonse, Sampath Srisailam, Thallapuranam Krishnaswamy Suresh Kumar, et al.. (2002). Structure and Stability of an Acidic Fibroblast Growth Factor from Notophthalmus viridescens. Journal of Biological Chemistry. 277(48). 46424–46432. 24 indexed citations
4.
Hung, Hui‐Chih, et al.. (2002). (PROTEIN SCIENCE , 11:332-341)Structural studies of the pigeon cytosolic NADP+-dependent malic enzyme.
5.
Huang, Shih‐Ming, et al.. (1998). Conformational stability of the N-terminal amino acid residues of mutated recombinant pigeon liver malic enzymes. Protein Engineering Design and Selection. 11(5). 371–376. 4 indexed citations
6.
Chou, Wen‐Yi, Shih‐Ming Huang, & G G Chang. (1997). Functional roles of the N-terminal amino acid residues in the Mn(II)-L- malate binding and subunit interactions of pigeon liver malic enzyme. Protein Engineering Design and Selection. 10(10). 1205–1211. 10 indexed citations
7.
Tang, Si‐Fu & G G Chang. (1996). Kinetic Characterization of the Endogenous Glutathione Transferase Activity of Octopus Lens S-Crystallin. The Journal of Biochemistry. 119(6). 1182–1188. 27 indexed citations
8.
Chou, Wen‐Yi, Shih‐Ming Huang, Youhua Liu, & G G Chang. (1994). Cloning and Expression of Pigeon Liver Cytosolic NADP+-Dependent Malic Enzyme cDNA and Some of Its Abortive Mutants. Archives of Biochemistry and Biophysics. 310(1). 158–166. 21 indexed citations
9.
Lee, Hwei‐Jen, et al.. (1994). Characterization of the Multiple Forms of Duck Lens δ-Crystallin with Endogenous Argininosuccinate Lyase Activity. Archives of Biochemistry and Biophysics. 314(1). 31–38. 7 indexed citations
10.
Chang, G G, et al.. (1994). Purification and Kinetic Mechanism of the Glutathione S-Transferase from C6/36, an Aedes albopictus Cell Line. Archives of Biochemistry and Biophysics. 310(1). 134–143. 11 indexed citations
11.
Lee, H J, Shyh‐Horng Chiou, & G G Chang. (1993). Inactivation of the endogenous argininosuccinate lyase activity of duck δ-crystallin by modification of an essential histidine residue with diethyl pyrocarbonate. Biochemical Journal. 293(2). 537–544. 11 indexed citations
12.
Chang, G G, et al.. (1992). Characterization of the tetramer-dimer-monomer equilibrium of the enzymically active subunits of pigeon liver malic enzyme. Biochemistry. 31(50). 12658–12664. 19 indexed citations
13.
Lee, H J, Sy Han Chiou, & G G Chang. (1992). Biochemical characterization and kinetic analysis of duck δ-crystallin with endogenous argininosuccinate lyase activity. Biochemical Journal. 283(2). 597–603. 31 indexed citations
14.
Chiou, Sy Han, et al.. (1991). Screening and kinetic analysis of delta-crystallins with endogenous argininosuccinate lyase activity in the lenses of vertebrates.. PubMed. 25(4). 705–13. 4 indexed citations
15.
Chang, G G, et al.. (1990). Modification of human placental alkaline phosphatase by periodate-oxidized 1,N6-ethenoadenosine monophosphate. Biochemical Journal. 272(3). 683–690. 18 indexed citations
16.
Chang, G G, et al.. (1989). Periodate-oxidized 3-aminopyridine adenine dinucleotide phosphate as a fluorescent affinity label for pigeon liver malic enzyme. Journal of Biological Chemistry. 264(1). 280–287. 18 indexed citations
17.
Chang, G G, et al.. (1988). Reversible dissociation of the catalytically active subunits of pigeon liver malic enzyme. Biochemical Journal. 254(1). 123–130. 26 indexed citations
18.
Li, Wen, et al.. (1988). Amino acid concentrations in serum and aqueous humor from subjects with extreme myopia or senile cataract.. Clinical Chemistry. 34(8). 1610–1613. 21 indexed citations
19.
Chang, G G, et al.. (1981). Periodate-oxidized AMP as a substrate, an inhibitor and an affinity label of human placental alkaline phosphatase. Biochemical Journal. 199(2). 281–287. 13 indexed citations
20.
Lee, Sang Chul, et al.. (1968). Gonadal Hormones in the Regulation of Methionine Adenosyltransferase Levels in Rat Liver. Experimental Biology and Medicine. 129(1). 161–165. 7 indexed citations

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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