Margaret E. Graham

1.6k total citations
29 papers, 1.3k citations indexed

About

Margaret E. Graham is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Margaret E. Graham has authored 29 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 21 papers in Cell Biology and 9 papers in Physiology. Recurrent topics in Margaret E. Graham's work include Cellular transport and secretion (21 papers), Lipid Membrane Structure and Behavior (13 papers) and Erythrocyte Function and Pathophysiology (7 papers). Margaret E. Graham is often cited by papers focused on Cellular transport and secretion (21 papers), Lipid Membrane Structure and Behavior (13 papers) and Erythrocyte Function and Pathophysiology (7 papers). Margaret E. Graham collaborates with scholars based in United Kingdom, United States and Italy. Margaret E. Graham's co-authors include Robert D. Burgoyne, Alan Morgan, Jeff W. Barclay, Brian W. McFerran, Philip Washbourne, Michael C. Wilson, Dermott W. O'Callaghan, Harvey T. McMahon, Richard Fisher and James R. Mathews and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Margaret E. Graham

29 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Margaret E. Graham United Kingdom 22 975 838 448 219 127 29 1.3k
Xuelin Lou United States 20 1.2k 1.2× 991 1.2× 878 2.0× 217 1.0× 139 1.1× 29 1.7k
Xiaofei Yang China 19 1.3k 1.4× 1.2k 1.4× 789 1.8× 159 0.7× 136 1.1× 30 1.7k
Lunbin Deng United States 16 1.1k 1.1× 636 0.8× 928 2.1× 177 0.8× 55 0.4× 17 1.5k
Mikyoung Park South Korea 16 1.1k 1.2× 562 0.7× 1.0k 2.3× 230 1.1× 38 0.3× 31 1.9k
Sergey V. Voronov United States 8 1.4k 1.5× 607 0.7× 409 0.9× 326 1.5× 83 0.7× 8 1.9k
Karen J. Smillie United Kingdom 18 720 0.7× 630 0.8× 367 0.8× 128 0.6× 76 0.6× 27 986
Charles T. Yokoyama United States 14 1.1k 1.1× 500 0.6× 824 1.8× 121 0.6× 62 0.5× 16 1.3k
Maki Deguchi‐Tawarada Japan 17 841 0.9× 592 0.7× 626 1.4× 133 0.6× 23 0.2× 19 1.2k
Ute Kistner Germany 9 1.1k 1.1× 564 0.7× 889 2.0× 106 0.5× 36 0.3× 9 1.5k
Andrea Betz Germany 21 2.0k 2.0× 1.6k 2.0× 1.2k 2.6× 268 1.2× 228 1.8× 26 2.8k

Countries citing papers authored by Margaret E. Graham

Since Specialization
Citations

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

Fields of papers citing papers by Margaret E. Graham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Margaret E. Graham. 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 Margaret E. Graham. The network helps show where Margaret E. Graham may publish in the future.

Co-authorship network of co-authors of Margaret E. Graham

This figure shows the co-authorship network connecting the top 25 collaborators of Margaret E. Graham. A scholar is included among the top collaborators of Margaret E. Graham 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 Margaret E. Graham. Margaret E. Graham 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.
2.
Burgoyne, Robert D., et al.. (2009). The Functions of Munc18‐1 in Regulated Exocytosis. Annals of the New York Academy of Sciences. 1152(1). 76–86. 42 indexed citations
3.
Graham, Margaret E., Mark Edwards, Lindy Holden‐Dye, et al.. (2008). UNC-18 Modulates Ethanol Sensitivity inCaenorhabditis elegans. Molecular Biology of the Cell. 20(1). 43–55. 31 indexed citations
4.
Boyd, Alan, Leonora F. Ciufo, Jeff W. Barclay, et al.. (2008). A Random Mutagenesis Approach to Isolate Dominant-Negative Yeastsec1Mutants Reveals a Functional Role for Domain 3a in Yeast and Mammalian Sec1/Munc18 Proteins. Genetics. 180(1). 165–178. 29 indexed citations
5.
Duncan, R. R., James R. Johnson, Lu‐Yun Lian, et al.. (2008). S-nitrosylation of syntaxin 1 at Cys145 is a regulatory switch controlling Munc18-1 binding. Biochemical Journal. 413(3). 479–491. 51 indexed citations
6.
Graham, Margaret E., et al.. (2005). Amisyn Regulates Exocytosis and Fusion Pore Stability by Both Syntaxin-dependent and Syntaxin-independent Mechanisms. Journal of Biological Chemistry. 280(36). 31615–31623. 36 indexed citations
7.
Rickman, Colin, José L. Jiménez, Margaret E. Graham, et al.. (2005). Conserved Prefusion Protein Assembly in Regulated Exocytosis. Molecular Biology of the Cell. 17(1). 283–294. 58 indexed citations
8.
Graham, Margaret E., Jeff W. Barclay, & Robert D. Burgoyne. (2004). Syntaxin/Munc18 Interactions in the Late Events during Vesicle Fusion and Release in Exocytosis. Journal of Biological Chemistry. 279(31). 32751–32760. 53 indexed citations
9.
Graham, Margaret E., Philip Washbourne, Michael C. Wilson, & Robert D. Burgoyne. (2002). Molecular Analysis of SNAP‐25 Function in Exocytosis. Annals of the New York Academy of Sciences. 971(1). 210–221. 24 indexed citations
10.
Graham, Margaret E., et al.. (2002). Complexin Regulates the Closure of the Fusion Pore during Regulated Vesicle Exocytosis. Journal of Biological Chemistry. 277(21). 18249–18252. 97 indexed citations
11.
Washbourne, Philip, et al.. (2001). Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. Biochemical Journal. 357(3). 625–625. 78 indexed citations
12.
Evans, Gareth J., Mark C. Wilkinson, Margaret E. Graham, et al.. (2001). Phosphorylation of Cysteine String Protein by Protein Kinase A. Journal of Biological Chemistry. 276(51). 47877–47885. 90 indexed citations
13.
Washbourne, Philip, et al.. (2001). Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. Biochemical Journal. 357(3). 625–634. 61 indexed citations
14.
Graham, Margaret E., Richard Fisher, & Robert D. Burgoyne. (2000). Measurement of exocytosis by amperometry in adrenal chromaffin cells: Effects of clostridial neurotoxins and activation of protein kinase C on fusion pore kinetics. Biochimie. 82(5). 469–479. 80 indexed citations
15.
Washbourne, Philip, et al.. (1999). Botulinum Neurotoxin E‐Insensitive Mutants of SNAP‐25 Fail to Bind VAMP but Support Exocytosis. Journal of Neurochemistry. 73(6). 2424–2433. 22 indexed citations
16.
McFerran, Brian W., Margaret E. Graham, & Robert D. Burgoyne. (1998). Neuronal Ca2+ Sensor 1, the Mammalian Homologue of Frequenin, Is Expressed in Chromaffin and PC12 Cells and Regulates Neurosecretion from Dense-core Granules. Journal of Biological Chemistry. 273(35). 22768–22772. 138 indexed citations
17.
Graham, Margaret E. & Robert D. Burgoyne. (1995). Effects of Calcium Channel Antagonists on Calcium Entry and Glutamate Release from Cultured Rat Cerebellar Granule Cells. Journal of Neurochemistry. 65(6). 2517–2524. 24 indexed citations
18.
Graham, Margaret E. & Robert D. Burgoyne. (1994). Activation of metabotropic glutamate receptors by L-AP4 stimulates survival of rat cerebellar granule cells in culture. European Journal of Pharmacology Molecular Pharmacology. 288(1). 115–123. 32 indexed citations
19.
Graham, Margaret E., et al.. (1992). Relationship Between Intracellular Free Calcium Concentration and NMDA‐induced Cerebellar Granule Cell Survival In Vitro. European Journal of Neuroscience. 4(12). 1369–1375. 25 indexed citations
20.
Graham, Margaret E. & Robert D. Burgoyne. (1991). stimulation of the survival of rat cerebellar granule cells in culture is not dependent upon increased c-fos expression and is not mimicked by protein kinase C activation. Neuroscience Letters. 130(2). 267–270. 14 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Xuelin Lou Breakdown of academic impact, for papers by Xiaofei Yang Breakdown of academic impact, for papers by Lunbin Deng Breakdown of academic impact, for papers by Mikyoung Park Breakdown of academic impact, for papers by Sergey V. Voronov Breakdown of academic impact, for papers by Karen J. Smillie Breakdown of academic impact, for papers by Charles T. Yokoyama Breakdown of academic impact, for papers by Maki Deguchi‐Tawarada Breakdown of academic impact, for papers by Ute Kistner Breakdown of academic impact, for papers by Andrea Betz
Rankless by CCL
2026