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RESEARCH
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David Eisenberg, Ph.D.
Contact Information:
Fax Number:
(310) 206-3914
Lab Number:
1 (310) 206-3642
Work Phone Number:
1 (310) 825-3754
Laboratory Address:
Paul Boyer Hall 205 UNITED STATES
Mailing Address:
201A Paul Boyer Hall CAMPUS - 157005 Los Angeles, CA
Work Address:
Paul Boyer Hall 201A
Director,
UCLA-DOE Institute for Genomics & Proteomics
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Distinguished Professor,
Biological Chemistry
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Lab Director,
Eisenberg Lab
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Professor,
Chemistry and Biochemistry
Biochemistry, Molecular Biology |
Paul D. Boyer Professor of Molecular Biology & Biochemistry,
Molecular Biology Institute
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Member,
ACCESS Program: Dept. of Biological Chemistry
JCCC Signal Transduction and Therapeutics Program Area
NanoBiotechnology and Biomaterials
California NanoSystems Institute
Molecular Biology Institute
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Faculty,
Bioinformatics IDP
Molecular, Cellular, and Integrative Physiology IDP
Molecular Biology IDP
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Researcher,
Biochemistry
Biophysics and Structural Biology
Proteomics and Bioinformatics
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A Short Biography:
David Eisenberg is also Professor of Chemistry and Biochemistry and of Biological Chemistry at the University of California, Los Angeles, and Director of the UCLA-DOE Institute for Genomics and Proteomics. He received his undergraduate degree in biochemical sciences from Harvard College and his D.Phil. degree in theoretical chemistry from Oxford University. His postdoctoral research was on ice and water with Walter Kauzmann at Princeton and in protein crystallography with Richard Dickerson. Dr. Eisenberg is a member of the National Academy of Sciences and the Institute of Medicine. He is a recipient of the 2004 UCLA Seaborg Medal, the 2005 Harvard Westheimer Medal, and the 2008 Emily Gray Award from the Biophysical Society.
Awards and Honors:
Pierce Award of the Immunotoxin Society
Amgen Award of the Protein Society
UCLA
McCoy Award
Biophysical Society
Emily M. Gray Award
Technion - Israel Institute of Technology
Harvey Prize in Human Health
Preceptor for the 2009 Nobel Laureate Signature Award for Graduate Education in Chemistry
Harvard
Westheimer Medal
UCLA
Seaborg Medal
Howard Hughes Medical Institute
Investigator
National Academy of Sciences
Elected Member
American Philosophical Society
Member
American Association for the Advancement of Science
Fellow
Institute of Medicine
Member
Research Interest:
Protein Structure, Folding, and Design
<p>David Eisenberg focuses on protein interactions. In his experiments he studies the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. In bioinformatic work, he derives information on protein interactions from genomic and proteomic data. His goal is to learn the networks of interacting proteins in cells.</p>
Detailed Biography:
David Eisenberg is currently Professor of Chemistry and Biochemistry and Biological Chemistry, as well as HHMI Investigator and Director of the UCLA-DOE Institute for Genomics and Proteomics. Before he came to UCLA, Eisenberg earned an A.B. in Biochemical Sciences from Harvard College and a D.Phil. from Oxford University in Theoretical Chemistry on a Rhodes Scholarship. After postdoctoral study at Princeton University on water and hydrogen bonding and at Caltech on protein crystallography, he joined the faculty at UCLA. Currently he studies protein interactions by X-ray crystallography, bioinformatics, and biochemistry, with an emphasis on amyloid-forming proteins. This recently recognized protein state offers opportunities to understand cells in health and disease, and in synthesizing new materials and in understanding processes as diverse as biofilms and corrosion. Eisenberg has published over 300 papers and reviews, holds half a dozen patents. His awards include: the UCLA Distinguished Teaching Award, John Simon Guggenheim Fellowship, the UCLA Faculty Research Lectureship, the Stein and Moore Award of the Protein Society, the ACS Faculty Mentoring Award, and membership in the National Academy of Sciences, the American Academy of Arts and Sciences, the American Philosophical Society, and the Institute of Medicine.
Apostol MI, Wiltzius JJ, Sawaya MR, Cascio D, Eisenberg D Atomic structures suggest determinants of transmission barriers in Mammalian prion disease.
Biochemistry.
2011;
50(13):
2456-63.
Zheng J, Liu C, Sawaya MR, Vadla B, Khan S, Woods RJ, Eisenberg D, Goux WJ, Nowick JS Macrocyclic ?-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.
J Am Chem Soc.
2011;
133(9):
3144-57.
Eisenberg D. Reflections on the past and future of integrative medicine from a lifelong student of the integration of Chinese and Western medicine.
Chin J Integr Med.
2011;
17(1):
3-5.
Eisenberg D. Reflections on the past and future of integrative medicine from a lifelong student of the integration of Chinese and Western medicine.
Chin J Integr Med.
2011;
17(1):
3-5.
Cong Liu, Michael R Sawaya & David Eisenberg ?2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
Nature Structural & Molecular Biology.
2011;
18:
49-55.
Apostol MI, Sawaya MR, Cascio D, Eisenberg D Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
J Biol Chem. .
2010;
285(39):
29671-5.
Khakshoor O, Lin AJ, Korman TP, Sawaya MR, Tsai SC, Eisenberg D, Nowick JS X-ray crystallographic structure of an artificial beta-sheet dimer.
J Am Chem Soc..
2010;
132(33):
11622-8.
Wiltzius JJ, Sievers SA, Sawaya MR, Cascio D, Popov D, Riekel C, Eisenberg D Atomic Structure of the Cross-Beta Spine of Islet Amyloid Polypeptide.
Protein Science.
2008;
17(9):
1467-74.
Wang L, Maji SK, Sawaya MR, Eisenberg D, Riek R Bacterial Inclusion Bodies Contain Amyloid-Like Structure.
PLoS Biol.
2008;
6(8):
.
Cruz, D. Watson, A. D. Miller, C. S. Montoya, D. Ochoa, M. T. Sieling, P. A. Gutierrez, M. A. Navab, M. Reddy, S. T. Witztum, J. L. Fogelman, A. M. Rea, T. H. Eisenberg, D. Berliner, J. Modlin, R. L. Host-derived oxidized phospholipids and HDL regulate innate immunity in human leprosy.
J Clin Invest.
2008;
118(8):
2917-28.
Riley, R., Pellegrini, M., Eisenberg, D. Identifying Cognate Binding Pairs Among a Large set of Paralogs: the Case of PE/PPE Proteins of Mycobacterium Tuberculosis.
PLoS Comput. Biol..
2008;
4(9):
.
Medrano-Soto, A. Pal, D. Eisenberg, D. Inferring molecular function: contributions from functional linkages.
Trends Genet.
2008;
24(12):
587-90.
Dunn B., Long J.W., Rolison D.R. Rethinking Multifunctions in Three Dimensions for Miniaturizing Electrical Energy Storage.
Interface.
2008;
17(3):
49.
Guo, Z. Eisenberg, D. The structure of a fibril-forming sequence, NNQQNY, in the context of a globular fold.
Protein Sci.
2008;
17(9):
1617-23.
White, E. L. Southworth, K. Ross, L. Cooley, S. Gill, R. B. Sosa, M. I. Manouvakhova, A. Rasmussen, L. Goulding, C. Eisenberg, D. Fletcher, T. M., 3rd A novel inhibitor of Mycobacterium tuberculosis pantothenate synthetase.
J Biomol Screen.
2007;
12(1):
100-5.
Tsemekhman, K. Goldschmidt, L. Eisenberg, D. Baker, D. Cooperative hydrogen bonding in amyloid formation.
Protein Sci.
2007;
16(4):
761-4.
Anderson, D. H. Kickhoefer, V. A. Sievers, S. A. Rome, L. H. Eisenberg, D. Draft crystal structure of the vault shell at 9-A resolution.
PLoS Biol.
2007;
5(11):
e318.
Sandra Orchard, Lukasz Salwinski, Samuel Kerrien, Luisa Montecchi-Palazzi, Matthias Oesterheld, Volker Stümpflen, Arnaud Ceol, Andrew Chatr-aryamontri, John Armstrong, Peter Woollard, John J Salama, Susan Moore, Jérôme Wojcik, Gary D Bader, Marc Vidal, Michael E Cusick, Mark Gerstein, Anne-Claude Gavin, Giulio Superti-Furga, Jack Greenblatt, Joel Bader, Peter Uetz, Mike Tyers, Pierre Legrain, Stan Fields, Nicola Mulder, Michael Gilson, Michael Niepmann, Lyle Burgoon, Javier De Las Rivas, Carlos Prieto, Victoria M Perreau, Chris Hogue, Hans-Werner Mewes, Rolf Apweiler, Ioannis Xenarios, David Eisenberg, Gianni Cesareni & Henning Hermjakob The minimum information required for reporting a molecular interaction experiment (MIMIx).
Nature Biotechnology.
2007;
25:
894-8.
Strong, M. Eisenberg, D. The protein network as a tool for finding novel drug targets.
Prog Drug Res.
2007;
64(number):
191, 193-215.
Goldschmidt, L. Cooper, D. R. Derewenda, Z. S. Eisenberg, D. Toward rational protein crystallization: A Web server for the design of crystallizable protein variants.
Protein Sci.
2007;
16(8):
1569-76.
Nelson, R. Eisenberg, D. Recent atomic models of amyloid fibril structure.
Curr Opin Struct Biol.
2006;
16(2):
260-5.
Eisenberg, D. Nelson, R. Sawaya, M. R. Balbirnie, M. Sambashivan, S. Ivanova, M. I. Madsen, A. O. Riekel, C. The structural biology of protein aggregation diseases: Fundamental questions and some answers.
Acc Chem Res.
2006;
39(9):
568-75.
Li, H. Pellegrini, M. Eisenberg, D. Detection of parallel functional modules by comparative analysis of genome sequences.
Nat Biotechnol.
2005;
23(2):
253-60.
Bowers, P. M. O'Connor, B. D. Cokus, S. J. Sprinzak, E. Yeates, T. O. Eisenberg, D. Utilizing logical relationships in genomic data to decipher cellular processes.
FEBS J.
2005;
272(20):
5110-8.
Kleiger, G. Panina, E. M. Mallick, P. Eisenberg, D. PFIT and PFRIT: bioinformatic algorithms for detecting glycosidase function from structure and sequence.
Protein Sci.
2004;
13(1):
221-9.
Salwinski, L. Eisenberg, D. Computational methods of analysis of protein-protein interactions.
Curr Opin Struct Biol.
2003;
13(3):
377-82.
Wang, S. Eisenberg, D. Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate.
Protein Sci.
2003;
12(5):
1097-108.
Strong, M. Mallick, P. Pellegrini, M. Thompson, M. J. Eisenberg, D. Inference of protein function and protein linkages in Mycobacterium tuberculosis based on prokaryotic genome organization: a combined computational approach.
Genome Biol.
2003;
4(9):
R59.
Lee, S. Eisenberg, D. Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process.
Nat Struct Biol.
2003;
10(9):
725-30.
McCarty, A. S. Kleiger, G. Eisenberg, D. Smale, S. T. Selective dimerization of a C2H2 zinc finger subfamily.
Mol Cell.
2003;
11(2):
459-70.
Cech, T. R. Eddy, S. R. Eisenberg, D. Hersey, K. Holtzman, S. H. Poste, G. H. Raikhel, N. V. Scheller, R. H. Singer, D. B. Waltham, M. C. Sharing publication-related data and materials: responsibilities of authorship in the life sciences.
Plant Physiol.
2003;
132(1):
19-24.
Liu, Y. Eisenberg, D. 3D domain swapping: as domains continue to swap.
Protein Sci.
2002;
11(6):
1285-99.
Duan, X. J. Xenarios, I. Eisenberg, D. Describing biological protein interactions in terms of protein states and state transitions: the LiveDIP database.
Mol Cell Proteomics.
2002;
1(2):
104-16.
Deane, C. M. Salwinski, L. Xenarios, I. Eisenberg, D. Protein interactions: two methods for assessment of the reliability of high throughput observations.
Mol Cell Proteomics.
2002;
1(5):
349-56.
Liu, Y. Gotte, G. Libonati, M. Eisenberg, D. Structures of the two 3D domain-swapped RNase A trimers.
Protein Sci.
2002;
11(2):
371-80.
Graeber, T. G. Eisenberg, D. Bioinformatic identification of potential autocrine signaling loops in cancers from gene expression profiles.
Nat Genet.
2001;
29(3):
295-300.
Wang Lei, Schubert David, Sawaya Michael R, Eisenberg David, Riek Roland Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States..
Angewandte Chemie.
2010;
49(23):
3904-8.
Eisenberg David L, Stika Catherine, Desai Ami, Baker David, Yost Kathleen J Providing contraception for women taking potentially teratogenic
medications: a survey of internal medicine physicians' knowledge,
attitudes and barriers..
Journal of general internal medicine.
2010;
25(4):
291-7.
Salwinski Lukasz, Licata Luana, Winter Andrew, Thorneycroft David, Khadake Jyoti, Ceol Arnaud, Aryamontri Andrew Chatr, Oughtred Rose, Livstone Michael, Boucher Lorrie, Botstein David, Dolinski Kara, Berardini Tanya, Huala Eva, Tyers Mike, Eisenberg David, Cesareni Gianni, Hermjakob Henning Recurated protein interaction datasets..
Nature methods.
2009;
6(12):
860-1.
Wiltzius Jed J W, Landau Meytal, Nelson Rebecca, Sawaya Michael R, Apostol Marcin I, Goldschmidt Lukasz, Soriaga Angela B, Cascio Duilio, Rajashankar Kanagalaghatta, Eisenberg David Molecular mechanisms for protein-encoded inheritance..
Nature structural & molecular biology.
2009;
16(9):
973-8.
Maji Samir K, Perrin Marilyn H, Sawaya Michael R, Jessberger Sebastian, Vadodaria Krishna, Rissman Robert A, Singru Praful S, Nilsson K Peter R, Simon Rozalyn, Schubert David, Eisenberg David, Rivier Jean, Sawchenko Paul, Vale Wylie, Riek Roland Functional amyloids as natural storage of peptide hormones in
pituitary secretory granules..
Science (New York, N.Y.).
2009;
325(5938):
328-32.
Wiltzius JJ, Sievers SA, Sawaya MR, Eisenberg D Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process.
Protein Science.
2009;
18(7):
1521-30.
Sprinzak Einat, Cokus Shawn J, Yeates Todd O, Eisenberg David, Pellegrini Matteo Detecting coordinated regulation of multi-protein complexes using
logic analysis of gene expression..
BMC systems biology.
2009;
3(1):
115.
Miallau Linda, Faller Michael, Chiang Janet, Arbing Mark, Guo Feng, Cascio Duilio, Eisenberg David Structure and proposed activity of a member of the VapBC family of
toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis..
The Journal of biological chemistry.
2009;
284(1):
276-83.
Sawaya, M. R. Wojtowicz, W. M. Andre, I. Qian, B. Wu, W. Baker, D. Eisenberg, D. Zipursky, S. L. A double S shape provides the structural basis for the extraordinary binding specificity of Dscam isoforms.
Cell.
2008;
134(6):
1007-18.
Wiltzius Jed J W, Sievers Stuart A, Sawaya Michael R, Cascio Duilio, Popov Dmitriy, Riekel Christian, Eisenberg David Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin).
Protein science : a publication of the Protein Society.
2008;
17(9):
1467-74.
Cruz, Watson, Miller, Montoya, Ochoa, Sieling, Gutierrez, Navab, Reddy, Witztum, Fogelman, Rea, Eisenberg, Berliner, Modlin Host-derived oxidized phospholipids and HDL regulate innate immunity in human leprosy..
J. Clin. Invest..
2008;
.
Miller Christopher S, Eisenberg David Using inferred residue contacts to distinguish between correct and incorrect protein models..
Bioinformatics.
2008;
24(14):
1575-82.
Kuriyan John, Eisenberg David The origin of protein interactions and allostery in colocalization..
Nature.
2007;
450(7172):
983-90.
Anderson Daniel H, Kickhoefer Valerie A, Sievers Stuart A, Rome Leonard H, Eisenberg David Draft crystal structure of the vault shell at 9-A resolution..
PLoS Biol..
2007;
5(11):
e318.
Galynker,, II Eisenberg, D. Matochik, J. A. Gertmenian-King, E. Cohen, L. Kimes, A. S. Contoreggi, C. Kurian, V. Ernst, M. Rosenthal, R. N. Prosser, J. London, E. D. Cerebral metabolism and mood in remitted opiate dependence.
Drug Alcohol Depend.
2007;
90(2-3):
166-74.
Kim Sul-Min, Bowers Peter M, Pal Debnath, Strong Michael, Terwilliger Thomas C, Kaufmann Markus, Eisenberg David Functional linkages can reveal protein complexes for structure determination..
Structure.
2007;
15(9):
1079-89.
Salwinski Lukasz, Eisenberg David The MiSink Plugin: Cytoscape as a graphical interface to the Database of Interacting Proteins..
Bioinformatics.
2007;
23(16):
2193-5.
Goldschmidt Lukasz, Cooper David R, Derewenda Zygmunt S, Eisenberg David Toward rational protein crystallization: A Web server for the design of crystallizable protein variants..
Protein Sci..
2007;
16(8):
1569-76.
Sawaya Michael R, Sambashivan Shilpa, Nelson Rebecca, Ivanova Magdalena I, Sievers Stuart A, Apostol Marcin I, Thompson Michael J, Balbirnie Melinda, Wiltzius Jed J W, McFarlane Heather T, Madsen Anders Ã, Riekel Christian, Eisenberg David Atomic structures of amyloid cross-beta spines reveal varied steric zippers..
Nature.
2007;
447(7143):
453-7.
Guo Zhefeng, Eisenberg David The mechanism of the amyloidogenic conversion of T7 endonuclease I..
J. Biol. Chem..
2007;
282(20):
14968-74.
Strong Michael, Eisenberg David The protein network as a tool for finding novel drug targets..
Mol. Ther..
2007;
64(1):
191, 193-215.
Goulding Celia W, Bowers Peter M, Segelke Brent, Lekin Tim, Kim Chang-Yub, Terwilliger Thomas C, Eisenberg David The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function..
J. Mol. Biol..
2007;
365(2):
275-83.
Bennett Melanie J, Sawaya Michael R, Eisenberg David Deposition diseases and 3D domain swapping..
Structure.
2006;
14(5):
811-24.
Guo Zhefeng, Eisenberg David Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I..
Proc. Natl. Acad. Sci. U.S.A..
2006;
103(21):
8042-7.
Strong Michael, Sawaya Michael R, Wang Shuishu, Phillips Martin, Cascio Duilio, Eisenberg David Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis..
Proc. Natl. Acad. Sci. U.S.A..
2006;
103(21):
8060-5.
Ivanova, M. I. Thompson, M. J. Eisenberg, D. A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments.
Proc Natl Acad Sci U S A.
2006;
103(11):
4079-82.
Thompson, M. J. Sievers, S. A. Karanicolas, J. Ivanova, M. I. Baker, D. Eisenberg, D. The 3D profile method for identifying fibril-forming segments of proteins.
Proc Natl Acad Sci U S A.
2006;
103(11):
4074-8.
Nelson Rebecca, Eisenberg David Structural models of amyloid-like fibrils..
Adv. Protein Chem..
2006;
73(2):
235-82.
Sambashivan, S. Liu, Y. Sawaya, M. R. Gingery, M. Eisenberg, D. Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.
Nature.
2005;
437(7056):
266-9.
Nelson, R. Sawaya, M. R. Balbirnie, M. Madsen, A. O. Riekel, C. Grothe, R. Eisenberg, D. Structure of the cross-beta spine of amyloid-like fibrils.
Nature.
2005;
435(7043):
773-8.
Bowers, P. M. Cokus, S. J. Eisenberg, D. Yeates, T. O. Use of logic relationships to decipher protein network organization.
Science.
2004;
306(5705):
2246-9.
Ivanova, M. I. Sawaya, M. R. Gingery, M. Attinger, A. Eisenberg, D. An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril.
Proc Natl Acad Sci U S A.
2004;
101(29):
10584-9.
Goulding, C. W. Apostol, M. I. Gleiter, S. Parseghian, A. Bardwell, J. Gennaro, M. Eisenberg, D. Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis.
J Biol Chem.
2004;
279(5):
3516-24.
Salwinski, L. Miller, C. S. Smith, A. J. Pettit, F. K. Bowie, J. U. Eisenberg, D. The Database of Interacting Proteins: 2004 update.
Nucleic Acids Res.
2004;
32(Database issue):
D449-51.
Strong, M. Graeber, T. G. Beeby, M. Pellegrini, M. Thompson, M. J. Yeates, T. O. Eisenberg, D. Visualization and interpretation of protein networks in Mycobacterium tuberculosis based on hierarchical clustering of genome-wide functional linkage maps.
Nucleic Acids Res.
2003;
31(24):
7099-109.
Ivanova, M. I. Gingery, M. Whitson, L. J. Eisenberg, D. Role of the C-terminal 28 residues of beta2-microglobulin in amyloid fibril formation.
Biochemistry.
2003;
42(46):
13536-40.
Hsu, T. Hingley-Wilson, S. M. Chen, B. Chen, M. Dai, A. Z. Morin, P. M. Marks, C. B. Padiyar, J. Goulding, C. Gingery, M. Eisenberg, D. Russell, R. G. Derrick, S. C. Collins, F. M. Morris, S. L. King, C. H. Jacobs, W. R., Jr. The primary mechanism of attenuation of bacillus Calmette-Guerin is a loss of secreted lytic function required for invasion of lung interstitial tissue.
Proc Natl Acad Sci U S A.
2003;
100(21):
12420-5.
Eisenberg, D. The discovery of the alpha-helix and beta-sheet, the principal structural features of proteins.
Proc Natl Acad Sci U S A.
2003;
100(20):
11207-10.
Mura, C. Phillips, M. Kozhukhovsky, A. Eisenberg, D. Structure and assembly of an augmented Sm-like archaeal protein 14-mer.
Proc Natl Acad Sci U S A.
2003;
100(8):
4539-44.
Mura, C. Katz, J. E. Clarke, S. G. Eisenberg, D. Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity.
J Mol Biol.
2003;
326(5):
1559-75.
Anderson, D. H. Sawaya, M. R. Cascio, D. Ernst, W. Modlin, R. Krensky, A. Eisenberg, D. Granulysin crystal structure and a structure-derived lytic mechanism.
J Mol Biol.
2003;
325(2):
355-65.
Mallick, P. Weiss, R. Eisenberg, D. The directional atomic solvation energy: an atom-based potential for the assignment of protein sequences to known folds.
Proc Natl Acad Sci U S A.
2002;
99(25):
16041-6.
Kleiger, G. Eisenberg, D. GXXXG and GXXXA motifs stabilize FAD and NAD(P)-binding Rossmann folds through C(alpha)-H... O hydrogen bonds and van der waals interactions.
J Mol Biol.
2002;
323(1):
69-76.
Goulding, C. W. Sawaya, M. R. Parseghian, A. Lim, V. Eisenberg, D. Missiakas, D. Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD.
Biochemistry.
2002;
41(22):
6920-7.
Kleiger, G. Grothe, R. Mallick, P. Eisenberg, D. GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles.
Biochemistry.
2002;
41(19):
5990-7.
Kleiger, G. Perry, J. Eisenberg, D. 3D structure and significance of the GPhiXXG helix packing motif in tetramers of the E1beta subunit of pyruvate dehydrogenase from the archeon Pyrobaculum aerophilum.
Biochemistry.
2001;
40(48):
14484-92.
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