Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 8 September 1995:
Vol. 269. no. 5229, pp. 1439 - 1443
DOI: 10.1126/science.7660129
Prev | Table of Contents | Next

Articles

Science, Vol 269, Issue 5229, 1439-1443
Copyright © 1995 by American Association for the Advancement of Science

articles

Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II

T Aso, WS Lane, JW Conaway, and RC Conaway

Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.

The Elongin (SIII) complex activates elongation by mammalian RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin is a heterotrimer composed of A, B, and C subunits of 110, 18, and 15 kilodaltons, respectively. Here, the mammalian Elongin A gene was isolated and expressed, and the Elongin (SIII) complex reconstituted with recombinant subunits. Elongin A is shown to function as the transcriptionally active component of Elongin (SIII) and Elongin B and C as regulatory subunits. Whereas Elongin C assembles with Elongin A to form an AC complex with increased specific activity, Elongin B, a member of the ubiquitin-homology gene family, appears to serve a chaperone-like function, facilitating assembly and enhancing stability of the Elongin (SIII) complex.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Direct Inhibition of RNA Polymerase II Transcription by RECQL5.
O. Aygun, X. Xu, Y. Liu, H. Takahashi, S. E. Kong, R. C. Conaway, J. W. Conaway, and J. Q. Svejstrup (2009)
J. Biol. Chem. 284, 23197-23203
   Abstract »    Full Text »    PDF »
Elongin B/C Recruitment Regulates Substrate Binding by CIS.
J. Piessevaux, L. De Ceuninck, D. Catteeuw, F. Peelman, and J. Tavernier (2008)
J. Biol. Chem. 283, 21334-21346
   Abstract »    Full Text »    PDF »
Pseudohypoxic Pathways in Renal Cell Carcinoma.
G. Bratslavsky, S. Sudarshan, L. Neckers, and W. M. Linehan (2007)
Clin. Cancer Res. 13, 4667-4671
   Abstract »    Full Text »    PDF »
ELA1 and CUL3 Are Required Along with ELC1 for RNA Polymerase II Polyubiquitylation and Degradation in DNA-Damaged Yeast Cells.
B. Ribar, L. Prakash, and S. Prakash (2007)
Mol. Cell. Biol. 27, 3211-3216
   Abstract »    Full Text »    PDF »
Requirement of ELC1 for RNA Polymerase II Polyubiquitylation and Degradation in Response to DNA Damage in Saccharomyces cerevisiae..
B. Ribar, L. Prakash, and S. Prakash (2006)
Mol. Cell. Biol. 26, 3999-4005
   Abstract »    Full Text »    PDF »
A sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS..
Y. Ling, A. J. Smith, and G. T. Morgan (2006)
Nucleic Acids Res. 34, 2219-2229
   Abstract »    Full Text »    PDF »
Suppressors of Cytokine Signaling 4 and 5 Regulate Epidermal Growth Factor Receptor Signaling.
E. Kario, M. D. Marmor, K. Adamsky, A. Citri, I. Amit, N. Amariglio, G. Rechavi, and Y. Yarden (2005)
J. Biol. Chem. 280, 7038-7048
   Abstract »    Full Text »    PDF »
ASB2 Is an Elongin BC-interacting Protein That Can Assemble with Cullin 5 and Rbx1 to Reconstitute an E3 Ubiquitin Ligase Complex.
M. L. Heuze, F. C. Guibal, C. A. Banks, J. W. Conaway, R. C. Conaway, Y. E. Cayre, A. Benecke, and P. G. Lutz (2005)
J. Biol. Chem. 280, 5468-5474
   Abstract »    Full Text »    PDF »
VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.
T. Kamura, K. Maenaka, S. Kotoshiba, M. Matsumoto, D. Kohda, R. C. Conaway, J. W. Conaway, and K. I. Nakayama (2004)
Genes & Dev. 18, 3055-3065
   Abstract »    Full Text »    PDF »
In Vivo Requirement of the RNA Polymerase II Elongation Factor Elongin A for Proper Gene Expression and Development.
M. Gerber, J. C. Eissenberg, S. Kong, K. Tenney, J. W. Conaway, R. C. Conaway, and A. Shilatifard (2004)
Mol. Cell. Biol. 24, 9911-9919
   Abstract »    Full Text »    PDF »
Both BC-Box Motifs of Adenovirus Protein E4orf6 Are Required To Efficiently Assemble an E3 Ligase Complex That Degrades p53.
P. Blanchette, C. Y. Cheng, Q. Yan, G. Ketner, D. A. Ornelles, T. Dobner, R. C. Conaway, J. W. Conaway, and P. E. Branton (2004)
Mol. Cell. Biol. 24, 9619-9629
   Abstract »    Full Text »    PDF »
Elongation by RNA polymerase II: the short and long of it.
R. J. Sims III, R. Belotserkovskaya, and D. Reinberg (2004)
Genes & Dev. 18, 2437-2468
   Abstract »    Full Text »    PDF »
The von Hippel-Lindau Tumor Suppressor Protein Is a Molten Globule under Native Conditions: IMPLICATIONS FOR ITS PHYSIOLOGICAL ACTIVITIES.
H. Sutovsky and E. Gazit (2004)
J. Biol. Chem. 279, 17190-17196
   Abstract »    Full Text »    PDF »
Tumor Suppressor von Hippel-Lindau (VHL) Stabilization of Jade-1 Protein Occurs through Plant Homeodomains and Is VHL Mutation Dependent.
M. I. Zhou, H. Wang, R. L. Foy, J. J. Ross, and H. T. Cohen (2004)
Cancer Res. 64, 1278-1286
   Abstract »    Full Text »    PDF »
Molecular Evidence That the Eukaryotic THO/TREX Complex Is Required for Efficient Transcription Elongation.
A. G. Rondon, S. Jimeno, M. Garcia-Rubio, and A. Aguilera (2003)
J. Biol. Chem. 278, 39037-39043
   Abstract »    Full Text »    PDF »
Mammalian Elongin A Is Not Essential for Cell Viability but Is Required for Proper Cell Cycle Progression with Limited Alteration of Gene Expression.
K. Yamazaki, T. Aso, Y. Ohnishi, M. Ohno, K. Tamura, T. Shuin, S. Kitajima, and Y. Nakabeppu (2003)
J. Biol. Chem. 278, 13585-13589
   Abstract »    Full Text »    PDF »
A three-dimensional model of Suppressor Of Cytokine Signalling 1 (SOCS-1).
F. Giordanetto and R. T. Kroemer (2003)
Protein Eng. Des. Sel. 16, 115-124
   Abstract »    Full Text »    PDF »
The von Hippel-Lindau Tumor Suppressor Stabilizes Novel Plant Homeodomain Protein Jade-1.
M. I. Zhou, H. Wang, J. J. Ross, I. Kuzmin, C. Xu, and H. T. Cohen (2002)
J. Biol. Chem. 277, 39887-39898
   Abstract »    Full Text »    PDF »
Identification and Biochemical Characterization of a Novel Transcription Elongation Factor, Elongin A3.
K. Yamazaki, L. Guo, K. Sugahara, C. Zhang, H. Enzan, Y. Nakabeppu, S. Kitajima, and T. Aso (2002)
J. Biol. Chem. 277, 26444-26451
   Abstract »    Full Text »    PDF »
Endoplasmic Reticulum Stress-inducible Protein, Herp, Enhances Presenilin-mediated Generation of Amyloid beta -Protein.
X. Sai, Y. Kawamura, K. Kokame, H. Yamaguchi, H. Shiraishi, R. Suzuki, T. Suzuki, M. Kawaichi, T. Miyata, T. Kitamura, et al. (2002)
J. Biol. Chem. 277, 12915-12920
   Abstract »    Full Text »    PDF »
Hpr1 Is Preferentially Required for Transcription of Either Long or G+C-Rich DNA Sequences in Saccharomyces cerevisiae.
S. Chavez, M. Garcia-Rubio, F. Prado, and A. Aguilera (2001)
Mol. Cell. Biol. 21, 7054-7064
   Abstract »    Full Text »    PDF »
Molecular Pathogenesis of the Von Hippel-Lindau Hereditary Cancer Syndrome: Implications for Oxygen Sensing.
H. Yang and W. G. Kaelin Jr. (2001)
Cell Growth Differ. 12, 447-455
   Full Text »    PDF »
The Elongation Domain of ELL Is Dispensable but Its ELL-Associated Factor 1 Interaction Domain Is Essential for MLL-ELL-Induced Leukemogenesis.
R. T. Luo, C. Lavau, C. Du, F. Simone, P. E. Polak, S. Kawamata, and M. J. Thirman (2001)
Mol. Cell. Biol. 21, 5678-5687
   Abstract »    Full Text »    PDF »
VHL tumor suppressor regulates Cl-/HCO3- exchange and Na+/H+ exchange activities in renal carcinoma cells.
S. A. KARUMANCHI, L. JIANG, B. KNEBELMANN, A. K. STUART-TILLEY, S. L. ALPER, and V. P. SUKHATME (2001)
Physiol Genomics 5, 119-128
   Abstract »    Full Text »    PDF »
A New Hyperrecombination Mutation Identifies a Novel Yeast Gene, THP1, Connecting Transcription Elongation With Mitotic Recombination.
M. Gallardo and A. Aguilera (2001)
Genetics 157, 79-89
   Abstract »    Full Text »
Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products.
A. R. Schoenfeld, E. J. Davidowitz, and R. D. Burk (2000)
PNAS 97, 8507-8512
   Abstract »    Full Text »    PDF »
Elongin from Saccharomyces cerevisiae.
C. M. Koth, M. V. Botuyan, R. J. Moreland, D. B. Jansma, J. W. Conaway, R. C. Conaway, W. J. Chazin, J. D. Friesen, C. H. Arrowsmith, and A. M. Edwards (2000)
J. Biol. Chem. 275, 11174-11180
   Abstract »    Full Text »    PDF »
Identification and Characterization of Elongin A2, a New Member of the Elongin Family of Transcription Elongation Factors, Specifically Expressed in the Testis.
T. Aso, K. Yamazaki, K. Amimoto, A. Kuroiwa, H. Higashi, Y. Matsuda, S. Kitajima, and M. Hatakeyama (2000)
J. Biol. Chem. 275, 6546-6552
   Abstract »    Full Text »    PDF »
Vaccinia Virus Gene A18R DNA Helicase Is a Transcript Release Factor.
C. A. Lackner and R. C. Condit (2000)
J. Biol. Chem. 275, 1485-1494
   Abstract »    Full Text »    PDF »
Dual Roles for Transcription Factor IIF in Promoter Escape by RNA Polymerase II.
Q. Yan, R. J. Moreland, J. W. Conaway, and R. C. Conaway (1999)
J. Biol. Chem. 274, 35668-35675
   Abstract »    Full Text »    PDF »
von Hippel-Lindau Protein Induces Hypoxia-regulated Arrest of Tyrosine Hydroxylase Transcript Elongation in Pheochromocytoma Cells.
S. L. Kroll, W. R. Paulding, P. O. Schnell, M. C. Barton, J.W. Conaway, R. C. Conaway, and M. F. Czyzyk-Krzeska (1999)
J. Biol. Chem. 274, 30109-30114
   Abstract »    Full Text »    PDF »
Regulation of the Urokinase-type Plasminogen Activator System by the von Hippel-Lindau Tumor Suppressor Gene.
M. Los, S. Zeamari, J. A. Foekens, M. F. B. G. Gebbink, and E. E. Voest (1999)
Cancer Res. 59, 4440-4445
   Abstract »    Full Text »    PDF »
Studying interactions of four proteins in the yeast two-hybrid system: Structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box protein.
A. Pause, B. Peterson, G. Schaffar, R. Stearman, and R. D. Klausner (1999)
PNAS 96, 9533-9538
   Abstract »    Full Text »    PDF »
Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C.
M. V. Botuyan, C. M. Koth, G. Mer, A. Chakrabartty, J. W. Conaway, R. C. Conaway, A. M. Edwards, C. H. Arrowsmith, and W. J. Chazin (1999)
PNAS 96, 9033-9038
   Abstract »    Full Text »    PDF »
The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity.
J. Lisztwan, G. Imbert, C. Wirbelauer, M. Gstaiger, and W. Krek (1999)
Genes & Dev. 13, 1822-1833
   Abstract »    Full Text »
Molecular Biology of Neuroblastoma.
J. M. Maris and K. K. Matthay (1999)
J. Clin. Oncol. 17, 2264
   Abstract »    Full Text »    PDF »
Physical Interaction and Functional Antagonism between the RNA Polymerase II Elongation Factor ELL and p53.
N. Shinobu, T. Maeda, T. Aso, T. Ito, T. Kondo, K. Koike, and M. Hatakeyama (1999)
J. Biol. Chem. 274, 17003-17010
   Abstract »    Full Text »    PDF »
Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function.
D. Liakopoulos, T. Busgen, A. Brychzy, S. Jentsch, and A. Pause (1999)
PNAS 96, 5510-5515
   Abstract »    Full Text »    PDF »
The Elongin B Ubiquitin Homology Domain. IDENTIFICATION OF ELONGIN B SEQUENCES IMPORTANT FOR INTERACTION WITH ELONGIN C.
C. S. Brower, A. Shilatifard, T. Mather, T. Kamura, Y. Takagi, D. Haque, A. Treharne, S. I. Foundling, J. W. Conaway, and R. C. Conaway (1999)
J. Biol. Chem. 274, 13629-13636
   Abstract »    Full Text »    PDF »
Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function.
C. E. Stebbins, W. G. Kaelin Jr., and N. P. Pavletich (1999)
Science 284, 455-461
   Abstract »    Full Text »
Transcription-Dependent Nuclear-Cytoplasmic Trafficking Is Required for the Function of the von Hippel-Lindau Tumor Suppressor Protein.
S. Lee, M. Neumann, R. Stearman, R. Stauber, A. Pause, G. N. Pavlakis, and R. D. Klausner (1999)
Mol. Cell. Biol. 19, 1486-1497
   Abstract »    Full Text »    PDF »
The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families.
T. Kamura, S. Sato, D. Haque, L. Liu, W. G. Kaelin Jr., R. C. Conaway, and J. W. Conaway (1998)
Genes & Dev. 12, 3872-3881
   Abstract »    Full Text »
FCP1, the RAP74-Interacting Subunit of a Human Protein Phosphatase That Dephosphorylates the Carboxyl-terminal Domain of RNA Polymerase IIO.
J. Archambault, G. Pan, G. K. Dahmus, M. Cartier, N. Marshall, S. Zhang, M. E. Dahmus, and J. Greenblatt (1998)
J. Biol. Chem. 273, 27593-27601
   Abstract »    Full Text »    PDF »
Mechanism of Action of RNA Polymerase II Elongation Factor Elongin. MAXIMAL STIMULATION OF ELONGATION REQUIRES CONVERSION OF THE EARLY ELONGATION COMPLEX TO AN ELONGIN-ACTIVABLE FORM.
R. J. Moreland, J. S. Hanas, J. W. Conaway, and R. C. Conaway (1998)
J. Biol. Chem. 273, 26610-26617
   Abstract »    Full Text »    PDF »
Template End-to-End Transposition by RNA Polymerase II.
M. G. Izban, M. A. Parsons, and R. R. Sinden (1998)
J. Biol. Chem. 273, 27009-27016
   Abstract »    Full Text »    PDF »
The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor.
X.-Y. Li and M. R Green (1998)
Genes & Dev. 12, 2992-2996
   Abstract »    Full Text »
pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation.
O. Iliopoulos, M. Ohh, and W. G. Kaelin Jr. (1998)
PNAS 95, 11661-11666
   Abstract »    Full Text »    PDF »
DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs.
T. Wada, T. Takagi, Y. Yamaguchi, A. Ferdous, T. Imai, S. Hirose, S. Sugimoto, K. Yano, G. A. Hartzog, F. Winston, et al. (1998)
Genes & Dev. 12, 343-356
   Abstract »    Full Text »
RNA Polymerase II Elongation Control.
J. PENG, M. LIU, J. MARION, Y. ZHU, and D.H. PRICE (1998)
Cold Spring Harb Symp Quant Biol 63, 365-370
   Abstract »    PDF »
Evidence for Covalent Modification of the Nuclear Dot-associated Proteins PML and Sp100 by PIC1/SUMO-1.
T. Sternsdorf, K. Jensen, and H. Will (1997)
J. Cell Biol. 139, 1621-1634
   Abstract »    Full Text »    PDF »
The yeast HPR1 gene has a functional role in transcriptional elongation that uncovers a novel source of genome instability.
S. Chavez and A. Aguilera (1997)
Genes & Dev. 11, 3459-3470
   Abstract »    Full Text »    PDF »
Formation and Crystallization of Yeast RNA Polymerase II Elongation Complexes.
A. Gnatt, J. Fu, and R. D. Kornberg (1997)
J. Biol. Chem. 272, 30799-30805
   Abstract »    Full Text »    PDF »
Identification of Elongin C Sequences Required for Interaction with the von Hippel-Lindau Tumor Suppressor Protein.
Y. Takagi, A. Pause, R. C. Conaway, and J. W. Conaway (1997)
J. Biol. Chem. 272, 27444-27449
   Abstract »    Full Text »    PDF »
Identification of the Region in Yeast S-II That Defines Species Specificity in Its Interaction with RNA Polymerase II.
M. Shimoaraiso, T. Nakanishi, T. Kubo, and S. Natori (1997)
J. Biol. Chem. 272, 26550-26554
   Abstract »    Full Text »    PDF »
Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitro.
Y. Zhu, T. Pe'ery, J. Peng, Y. Ramanathan, N. Marshall, T. Marshall, B. Amendt, M. B. Mathews, and D. H. Price (1997)
Genes & Dev. 11, 2622-2632
   Abstract »    Full Text »    PDF »
Interaction of Elongation Factors TFIIS and Elongin A with a Human RNA Polymerase II Holoenzyme Capable of Promoter-specific Initiation and Responsive to Transcriptional Activators.
G. Pan, T. Aso, and J. Greenblatt (1997)
J. Biol. Chem. 272, 24563-24571
   Abstract »    Full Text »    PDF »
The H3/H4 Tetramer Blocks Transcript Elongation by RNA Polymerase II in Vitro.
C.-H. Chang and D. S. Luse (1997)
J. Biol. Chem. 272, 23427-23434
   Abstract »    Full Text »    PDF »
Defective placental vasculogenesis causes embryonic lethality in VHL-deficient mice.
J. R. Gnarra, J. M. Ward, F. D. Porter, J. R. Wagner, D. E. Devor, A. Grinberg, M. R. Emmert-Buck, H. Westphal, R. D. Klausner, and W. M. Linehan (1997)
PNAS 94, 9102-9107
   Abstract »    Full Text »    PDF »
ELL2, a new member of an ELL family of RNA polymerase II elongation factors.
A. Shilatifard, D. R. Duan, D. Haque, C. Florence, W. H. Schubach, J. W. Conaway, and R. C. Conaway (1997)
PNAS 94, 3639-3643
   Abstract »    Full Text »    PDF »
The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins.
A. Pause, S. Lee, R. A. Worrell, D. Y. T. Chen, W. H. Burgess, W. M. Linehan, and R. D. Klausner (1997)
PNAS 94, 2156-2161
   Abstract »    Full Text »    PDF »
Developmental analysis and subcellular localization of the murine homologue of ELL.
M. J. Thirman, E. B. Diskin, S. S. Bin, H. S. Ip, J. M. Miller, and M. C. Simon (1997)
PNAS 94, 1408-1413
   Abstract »    Full Text »    PDF »
The general transcription factors of RNA polymerase II..
G Orphanides, T Lagrange, and D Reinberg (1996)
Genes & Dev. 10, 2657-2683
   PDF »
Characterization of Elongin C Functional Domains Required for Interaction with Elongin B and Activation of Elongin A.
Y. Takagi, R. C. Conaway, and J. W. Conaway (1996)
J. Biol. Chem. 271, 25562-25568
   Abstract »    Full Text »    PDF »
Overproduction, Purification, and Characterization of the XPC Subunit of the Human DNA Repair Excision Nuclease.
J. T. Reardon, D. Mu, and A. Sancar (1996)
J. Biol. Chem. 271, 19451-19456
   Abstract »    Full Text »    PDF »
Mutations in the Second Largest Subunit of RNA Polymerase II Cause 6-Azauracil Sensitivity in Yeast and Increased Transcriptional Arrest in Vitro.
W. Powell and D. Reines (1996)
J. Biol. Chem. 271, 6866-6873
   Abstract »    Full Text »    PDF »
Tumor suppression and transcription elongation: the dire consequences of changing partners.
A Krumm and M Groudine (1995)
Science 269, 1400-1401
   PDF »
Inhibition of transcription elongation by the VHL tumor suppressor protein.
D. Duan, A Pause, W. Burgess, T Aso, D. Chen, K. Garrett, R. Conaway, J. Conaway, W. Linehan, and R. Klausner (1995)
Science 269, 1402-1406
   Abstract »    PDF »
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C.
A Kibel, O Iliopoulos, J. DeCaprio, and W. Kaelin Jr (1995)
Science 269, 1444-1446
   Abstract »    PDF »
Herp, a New Ubiquitin-like Membrane Protein Induced by Endoplasmic Reticulum Stress.
K. Kokame, K. L. Agarwala, H. Kato, and T. Miyata (2000)
J. Biol. Chem. 275, 32846-32853
   Abstract »    Full Text »    PDF »
Participation of Transcription Elongation Factor XSII-K1 in Mesoderm-derived Tissue Development in Xenopus laevis.
Y. Taira, T. Kubo, and S. Natori (2000)
J. Biol. Chem. 275, 32011-32015
   Abstract »    Full Text »    PDF »
Transcription Factors TFIIF, ELL, and Elongin Negatively Regulate SII-induced Nascent Transcript Cleavage by Non-arrested RNA Polymerase II Elongation Intermediates.
B. J. Elmendorf, A. Shilatifard, Q. Yan, J. W. Conaway, and R. C. Conaway (2001)
J. Biol. Chem. 276, 23109-23114
   Abstract »    Full Text »    PDF »
A Mutant Form of JAB/SOCS1 Augments the Cytokine-induced JAK/STAT Pathway by Accelerating Degradation of Wild-type JAB/CIS Family Proteins through the SOCS-box.
T. Hanada, T. Yoshida, I. Kinjyo, S. Minoguchi, H. Yasukawa, S. Kato, H. Mimata, Y. Nomura, Y. Seki, M. Kubo, et al. (2001)
J. Biol. Chem. 276, 40746-40754
   Abstract »    Full Text »    PDF »
Transcription Elongation Factor S-II Confers Yeast Resistance to 6-Azauracil by Enhancing Expression of the SSM1 Gene.
M. Shimoaraiso, T. Nakanishi, T. Kubo, and S. Natori (2000)
J. Biol. Chem. 275, 29623-29627
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)