Frontiers in Education Technology 

Vol. 6, No.3, 2023 

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ISSN 2576-1846 (Print) ISSN 2576-1854 (Online) 

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Original Paper 

Photograph 51, Rosalind Franklin and DNA Structure 

Steven B. Oppenheimer1 

1 Department of Biology and Center for Cancer and Developmental Biology, California State University, 

Northridge, Northridge, CA USA 

 

Received: April 17, 2023           Accepted: May 3, 2023      Online Published: May 17, 2023 

doi:10.22158/fet.v6n3p1             URL: http://dx.doi.org/10.22158/fet.v6n3p1 

 

Abstract 

The Nobel Prize in Physiology/Medicine was awarded in 1962 to Watson, Crick and Wilkins, after the 

death of Rosalind Franklin who passed away in 1958. This mini-review focuses on Franklin’s 

contributions to the double helix discovery. The title of this paper, Photograph 51, describes a x-ray 

diffraction image of DNA (B form) taken by Franklin and her graduate student Raymond Gosling (Note 

1). Its importance will be described, as well as Franklin’s other contributions to the double helix 

discovery. Of immense importance is what Crick and Watson themselves said: Without Franklin’s data, 

“the formulation of our structure would have been most unlikely, if not impossible” (Note 2). This 

statement makes it clear that Franklin rightly deserves to be the 4th partner in the discovery of the 

structure of DNA, along with Crick, Watson and Wilkins. 

 

1. Introduction 

Matthew Cobb’s and Nathaniel Comfort’s 2023 Nature Commentary, What Watson and Crick Really 

Took from Franklin, Nature 616: April 27, 2023, pages 657-660, is a major reference for this 

mini-review (Note 3). It, like this paper, concludes that Franklin is rightly a 4th partner in this great 

discovery (Crick, Watson, Wilkins, Franklin), one of the greatest of all time. The references in this 

paper are twofold: One: those based on the DNA story (Notes 1-4) and Two: why am I telling this story 

(Notes 5-97)? These latter references show my credibility in research science, some recognition: US 

Presidential Award, AAAS Fellow, CSU system statewide Trustees Outstanding Professor; and my 

personal friendship with the late Dr. Crick, who visited here for about 10 years in the 1990s. 

There are two DNA forms. The A form—is crystalline and “dry.” The second is the B form, that is 

“wetter” and called the paracrystalline form. A form can be converted to B form by increasing humidity. 

B form can be converted to A by reducing humidity. Cells contain lots of water and therefore the B 

form of DNA is likely the biologically functional form. Maurice Wilkins who supervised Crick, Watson 



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and Franklin obtained some very pure A form DNA from Swiss chemist Rudolf Signer and some less 

pure DNA from the Austrian biochemist Erwin Chargaff (Notes 3). 

Attention is often given to the purest form of a chemical, in this case the A form of DNA. Watson and 

Crick had many interactions with colleagues. For example, Erwin Chargaff told them that there was 

rough equivalences of thymine (T)/adenine (A) and guanine (G)/cytosine (C). This helped them think 

that A binds with T and C binds with G (Notes 4). At first Crick and Watson in building models thought 

the bases were in the aldose form that was wrong and their models did not work.  

Watson and Crick showed their models to Jerry Donohue, an American crystallographer who shared an 

office with Watson. 

Jerry said that the DNA bases would most likely be in the ketose form in water, not the aldose from that 

they had been using. An aldose contains an aldehyde group (CHO) consisting of carbon, hydrogen and 

oxygen while a ketose contains a ketone group (CO) consisting of carbon and oxygen. 

When they switched their thinking that the bases were in the ketose form, the cardboard models 

“worked.” A paired with T and C paired with G. Here again, interactions with colleague(s) helped 

Watson and Crick arrive at a correct piece of the puzzle. 

From Ross Hardison, the Pennsylvania State University (denoted by “ ”): 

 

2. B-form of DNA 

 “B-DNA is the Watson–Crick form of the double helix that most people are familiar with. 

 They proposed two strands of DNA — each in a right-hand helix — wound around the same 

axis. The two strands are held together by H-bonding between the bases (in anti-conformation). 

 The two strands of the duplex are antiparallel and plectonemically coiled. The nucleotides 

arrayed in a 5′ to 3′ orientation on one strand align with complementary nucleotides in the 3′ to 

5′ orientation of the opposite strand. 

 Bases fit in the double helical model if pyrimidine on one strand is always paired with purine on 

the other. From Chargaff’s rules, the two strands will pair A with T and G with C. This pairs a 

keto base with an amino base, a purine with a pyrimidine. Two H-bonds can form between A and 

T, and three can form between G and C. 

 These are the complementary base pairs. The base-pairing scheme immediately suggests a way 

to replicate and copy the genetic information. 

 34 nm between bp, 3.4 nm per turn, about 10 bp per turn 

 9 nm (about 2.0 nm or 20 Angstroms) in diameter. 

 34o helix pitch; -6o base-pair tilt; 36o twist angle” 

 

 

 

 



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3. A-form DNA 

 “The major difference between A-form and B-form nucleic acid is in the confirmation of the 

deoxyribose sugar ring. It is in the C2′ endoconformation for B-form, whereas it is in the C3′ 

endoconformation in A-form. 

 A second major difference between A-form and B-form nucleic acid is the placement of 

base-pairs within the duplex. In B-form, the base-pairs are almost centered over the helical axis 

but in A-form, they are displaced away from the central axis and closer to the major groove. The 

result is a ribbon-like helix with a more open cylindrical core in A-form. 

 Right-handed helix 

 11 bp per turn; 0.26 nm axial rise; 28o helix pitch; 20o base-pair tilt 

 33o twist angle; 2.3nm helix diameter” 

Rosalind Franklin, a jewish woman scientist, was not allowed in the scientist lounge, as anti-female and 

anti-semitic culture prevailed at that time. So while Crick and Watson had the “luxury” of interacting 

with many other scientists, Rosalind Franklin did not. And it is often said that Franklin’s science 

suffered for it (Note 3). It is not likely that Crick and Watson would have achieved the correct model 

before others such as Linus Pauling, who was close on their tracks and had won two Nobel Prizes, had 

they not had extensive interaction with others. 

Rosalind Franklin should have shared in the glory of the discovery. She likely would have shared in the 

Nobel prize had she not past away before it was awarded. Her input included photograph 51. When 

Wilkins showed this photo to Watson, he quickly thought that it was probably a helix. Franklin left for 

a position elsewhere and was instructed to leave her DNA work with Wilkins. Franklin’s student Ryan 

Gosling, who together with Franklin produced photo 51, gave it to Wilkins when Franklin left. Wilkins 

showed it to Watson, who after conversations with Crick, thought it was a likely helix. The models built 

by Crick and Watson, by themselves, were not experimental evidence for a helix. But photo 51 was 

experimental evidence, helping to confirm the helix structure. One photo, photo 51, is just one piece of 

experimental evidence. But together with the modeling, a strong case was made for the helix structure 

of DNA. It made sense. 

For photo 51 the B form of DNA was exposed to x-rays for 62 hours to produce one of the finest and 

clearest x-ray photos ever taken. It was the 51st photo taken. The cartoon by Emily Willoughby shows 

some of the features of photo 51. Franklin said that photo 51 suggests a helical structure, most likely a 

double helix with ten bases per turn with the bases on the inside and the phosphate groups on the 

outside. She suggested that the DNA double helix had a diameter of 20 Angstroms with 3.4 Angstroms 

between base pairs and 10 base pairs per turn with 34 Angstroms between repeated units. A missing 

layer line suggested a double helix not a single helix. This all is shown in the cartoon that helps in the 

understanding of what Photo 51 shows. There is some controversy about what came first, Crick and 

Watson’s models or Franklin and Gosling’s experimental evidence, photo 51. The statement made by 

Crick and Watson regarding Franklin’s data, “the formulation of our structure would have been most 



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unlikely, if not impossible,” (Note 2) without Franklin’s data, This statement suggests that Crick and 

Watson knew about Franklin’s work before they completed their correct model of the structure of DNA. 

They suggest that Franklin’s work was instrumental in the development of the correct DNA model 

(Note 2) 

This conclusion was stated in Cobb and Comfort’s 2023 Nature Commentary (Note 3) and represents a 

new twist to the DNA story. Also noted was a Medical Research Council report in which Franklin and 

Wilkins independently suggest that the B form of DNA is helical with two intertwined chains with a 

sugar-phosphate backbone on the outside of the helix and a 34 Angstrom repeat (Note 1). The correct 

model of the DNA double helix was displayed at the Royal Society Conversazione in June 1953 and 

signed by Crick, Watson, Wilkins and Franklin (Note 3). 

 

4. Conclusions 

While the exact timeline of who did what first may be controversial, there is no doubt that Rosalind 

Franklin deserves to be a 4th partner in the DNA structure discovery along with Crick, Watson and 

Wilkins. This discovery is one of the most important of all time. Franklin’s experimental evidence as 

well at Watson and Crick’s modeling were both essential in the DNA structure discovery as stated by 

Crick and Watson. Franklin’s contributions were instrumental. Without them… “the formulation of our 

structure would have been most unlikely, if not impossible.” While the 2023 Nature Commentary is 

read by practicing scientists, this mini-review is primarily for educators and everyone, bringing a new 

understanding of one of the greatest discoveries of all time. While it is generally known that Rosalind 

Franklin had something to do with the discovery, what is presented here is not widely known. The 

discussion on Photograph 51 is an especially relevant addition to frontiers in education technology. As 

a US Presidential Awardee, Fellow AAAS, CSU system Trustees Outstanding Professor, friend of Dr. 

Crick, and author with my students of many peer reviewed publications (Notes 5-97), I am happy to 

present this paper to the public. 

 

Acknowledgements 

Thanks to Carolyn Oppenheimer for expert figure placements and formatting and to my colleagues and 

university leadership for outstanding support over a 50 plus year period. 

 



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Notes 

Note 1. Franklin, R.E., Gosling, R.G., Molecular Configuration in Sodium Thymonucleate, Nature171, 

340-341 (1953). 

Note 2. Crick, F.H.C., Watson, J.D., The Complementary Structure of Deoxyribonucleic Acid, Proc. R. 

Soc. Lond., A223, 80-96 (1954). 

Note 3. Cobb, M., Comfort, N., What Watson and Crick Really Took From Franklin, Nature 616, 

657-660 (2023). 

Note 4. Zamenhof, S., Brawerman, G., and Chargaff, E. On the deoxypentose nucleic acids from 

several microorganisms, Biochim et Biophys. Acta, 9, 402-405 (1952). 

Note 5. S. Oppenheimer, M. Berman, H. Chun, A. Lundgren, S. Tanaka, A Antoniou, T. Miller, G. Zem, 

Applied Science Research for All Part 1 Pre-College Level, American Journal of Applied Scientific 

Research 6: 72-75 (2020). Doi:10.11648/j.ajasr.20200606.11. 

Note 6. S. Oppenheimer, Covid-19 Pandemic, Glycobiology, Glycan Shields, Vaccine Strategies, 

Heparin Sulfate: A Mini Review, American Journal of Applied Scientific Research 6(2): 46-48 (2020). 

Note 7. S. Oppenheimer, Cell Clusters in Cancer Metastasis: A Mini Review, American Journal of 

Applied Scientific Research 6(2): 43-45 (2020). Doi: 10.11648//j.ajasr.20200602.13. 

Note 8. Smith, T., Oppenheimer, S.B., Involvement of L-rhamnose in Sea Urchin Gastrulation: A Live 

Embryo Assay, Zygote, doi:10.1017/S0967199413000452 (2013) 



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Note 9. Singh, S., Karabidian, E., Kandel, A., Metzenberg, S., Carroll, Jr. E., Oppenheimer, S.B., A 

Role for Polyglucans in a Model Sea Urchin Embryo Cellular Interaction, Zygote 

doi:10.1017/S0967199413000038 (2013) 

Note 10. Ghazarian, H, B. Idoni, S. Oppenheimer. A Glycobiology Review: Carbohydrates, Lectins, 

and Implications in Cancer Therapeutics. Acta Histochemica, vol. 113, pages 236-247 (2011) PMCID 

PMC3027850. On the order of 10,000 downloads. One of the most of all time. 

Note 11. Dreyfuss, J. and S. Oppenheimer. Cyclodextrins and cellular interactions in E. Bilensoy, ed., 

Cyclodextrins in Pharmaceutics, Cosmetics, and Biomedicine, Current and Future Industrial 

Applications, John Wiley and Sons, Hoboken, N.J., Chapter 15, pp. 287-295. (2010) 

Note 12. Idoni, B. H. Ghazarian, S. Metzenberg, V. Hutchins-Carroll, S. Oppenheimer, and E. Carroll Jr. 

Use of Specific Glycosidases to Probe Cellular Interactions in the Sea Urchin Embryo. Experimental 

Cell Research, vol. 316, pp. 2204-2211 (2010) PMCID PMC2921930 

Note 13. Alvarez, M., Nnoli, J., Carroll, E.J., Jr., Hutchins-Carroll, V., Razinia, Z., Oppenheimer, S.B., 

Exogenous Hyalin and Sea Urchin Gastrulation, Part II: Hyalin, An Interspecies Cell Adhesion 

Molecule, Zygote 16: 73-78 (2008). PMCID PMC2557437 

Note 14. Carroll, E.J., Jr., Hutchins-Carroll, V., Coyle-Thompson, C., Oppenheimer, S. B., Hyalin is a 

Cell Adhesion Molecule Involved in Mediating Archenteron-Blastocoel Roof Attachment, Acta 

Histochemica 110: 265-275 (2008). PMID 18262230 

Note 15. Contreras, A., Vitale, J., Hutchins-Carroll, V., Carroll, E.J., Oppenheimer, S.B., Exogenous 

Hyalin and Sea Urchin Gastrulation. Part III: Biological Activity of Hyalin Isolated from Lytechinus 

pictus embryos, Zygote 16: 355-361 (2008). PMCID PMC2586997 

Note 16. Oppenheimer, S.B., Alvarez, M., Nnoli, J., Carbohydrate-Based Experimental Therapeutics 

for Cancer, HIV/AIDS and Other Diseases, Acta Histochemica 110: 6-13 (2008). PMCID 

PMC2278011 

Note 17. Oppenheimer, S.B., Cellular Basis of Cancer Metastasis: A Review of Fundamentals and New 

Advances, Acta Histochemica, 108: 327-334 (2007). This paper garnered the most downloads of all 

papers in this Elsevier journal, August 06-March 07 (813 downloads). PMID16730054 

Note 18. Petrossian, K., Banner, L., Oppenheimer, S.B., Lectin Binding and Lectin Effects on Human 

Cancer and Non-Cancer Cell Lines: Examination of Issues of Interest in Drug Design Strategies, Acta 

Histochemica 109: 491-500 (2007). 

Note 19. Razinia, Z., Carroll, Jr., E.J., Oppenheimer, S.B., Microplate Assay for Quantifying 

Developmental Morphologies: Effects of Exogenous Hyalin on Sea Urchin Gastrulation, Zygote 15: 

1-6 (2007). 

Note 20. Sajadi, S., Rojas, P., Oppenheimer, S.B., Cyclodextrin, A Probe for Studying Adhesive 

Interactions, Acta Histochemica 109: 338-342 (2007). PMCID PMC 1988679 

Note 21. Zem, G.C., Badali, O., Gaytan, M. Hekmatjou, H., Alvarez, M., Nnoli, J., Katus, E., 

Oppenheimer, S.B., Microbead Analysis of Cell Binding to Immobilized Lectin: An Alternative to 



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Microarrays in the Development of Carbohydrate Drugs and Diagnostic Tests, Acta Histochemica 108: 

311-317 (2006). 

Note 22. Ghazarian, H., Coyle-Thompson, C., Dalrymple, W., Hutchins-Carroll, V., Metzenberg, S., 

Razinia, Z., Carroll, Jr., E.J., Oppenheimer, S.B., Exogenous Hyalin and Sea Urchin Gastrulation, Part 

IV: a Direct Adhesion Assay- Progress in Identifying Hyalin’s Active Sites, Zygote 18: 17-26 (2010). 

PMCID PMC2817981 

Note 23. Oppenheimer, S. & Meyer, J. (1982). Carbohydrate specificity of sea urchin blastula adhesion 

component, Experimental Cell Research, 139, 451-456. 

Note 24. Idoni, B., Ghazarian, H., Metzenberg, S., Hutchins-Carroll, V, Carroll, Jr., E., & Oppenheimer, 

S. (2010). Use of specific glycosidases to probe cellular interactions in the sea urchin embryo. 

Experimental Cell Research, 316, 2204-2211. 

Note 25. Liang, J., Aleksanyan, H., Metzenberg, S., & Oppenheimer, S. (2016). Involvement of 

L-rhamnose in sea urchin gastrulation. Part II: alpha rhamnosidase, Zygote 24, 37-377. 

Note 26. K. Crocker, J. Deleon, L. Telliyan, K. Aprelian, A. Rosenberg, N. Pouri, G. Beltran, V. 

Ramirez, D. Kaufman, A. Petrosyan, D. Nazarian, M. Magistrado, S. Matinian, D. Hanna, S. Eskandari, 

F. Atanante, A. Nerses, G. Zem, S. Oppenheimer A Kinetic Assay for Drug Discovery: Part 2, Sodium 

Sulfate American Journal of Applied Scientific Research 2020; 6(2): 39-42 

http://www.sciencepublishinggroup.com/j/ajasr
doi: 10.11648/j.ajasr.20200602.12
ISSN: 2471-9722 

(Print); ISSN: 2471-9730 (Online). 

Note 27. V. Nahapetyan, S. Delos Santos, K. Crocker, D. Tobar, D. Nazarian, H. Chirishyan, G. Beltran, 

R. Dubin, L. Reque, P. Singh, B. Cardona, G. Royce Bachinela, L. Sarkisyan, G. Zem, S. Oppenheimer, 

A manual kinetic assay in a fixed yeast model for drug discovery American Journal of Applied 

Scientific Research 5, No1: 28-35. Doi 10.11648/j.ajasr.20190501.15 (2019).  

Note 28. Aleksanyan, H., Liang, J., Metzenberg, S., Oppenheimer, S.B., Terminal alpha-D-mannosides 

are critical during sea urchin gastrulation, Zygote doi: 10.1017/SO967199416000113 (2016). 

Note 29. A. Ghazarian, Oppenheimer, S., Microbead analysis of cell binding to immobilized lectin. Part 

II: quantitative kinetic profile assay for possible identification of anti-infectivity and anti-cancer 

reagents http://dx.doi.org/10.1016/j.acthis.2014.07.015, Acta Histochemica 116 (2014) 1514-1518. 

Note 30. Singh, E. Karabidian, A. Kandel, S. Metzenberg, E. Carroll, Jr,. S. Oppenheimer, A role for 

polyglucans in a model sea urchin embryo cellular interaction, Zygote (Cambridge University Press), 

(2013), doi.10.1017/S096719943000038 (2013). 

Note 31. H. Ghazarian, C. Coyle-Thompson, Dalrymple, V. Hutchins-Carroll, S. Metzenberg, Z. 

Razinia, E. Carroll, Jr., S. Oppenheimer, Exogenous Hyalin and Sea Urchin Gastrulation, Part IV: a 

Direct Adhesion Assay – Progress in Identifying Hyalin’s Active Sites Zygote 18: 17-26 (2010). 

Note 32. A. Contreras, Vitale, V. Hutchins-Carroll, E. Carroll, Jr, S. Oppenheimer. Exogenous Hyalin 

and Sea Urchin Gastrulation, Part III: Biological Activity of Hyalin Extracted from Lytechinus pictus 

embryos Zygote, vol. 16, pp. 355-361 (2008). 

http://dx.doi.org/10.1016/j.acthis.2014.07.015


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Note 33. E. Carroll, Jr., V. Hutchins-Carroll, C. Coyle Thompson, S. Oppenheimer, Hyalin is a Cell 

Adhesion Molecule Involved in Mediating Archenteron Blastocoel Roof Attachment, Acta 

Histochemica, vol. 110, pp. 265-275 (2008). 

Note 34. M. Alvarez, J. Nnoli, E. Carroll, Jr., V. Hutchins-Carroll, Z. Razinia, S. Oppenheimer, 

Exogenous Hyalin and Sea Urchin Gastrulation, Part II: Hyalin, An Interspecies Cell Adhesion 

Molecule, Zygote, vol. 16, pp. 73-78 (2008).  

Note 35. M. Alvarez, J. Nnoli, S. Oppenheimer, Carbohydrate-Based Experimental Therapeutics for 

Cancer, HIV/AIDS and Other Diseases, Acta Histochemica, vol. 110, pp. 6-13 (2008). 

Note 36. K. Petrossian, L. Banner, S. Oppenheimer, Lectin Binding and Effects in Culture on Human 

Cancer and Non-Cancer Cell Lines: Examination of Issues of Interest in Drug Design Strategies, Acta 

Histochemica, vol 109, pp. 491-500 (2007).  

Note 37. Z. Razinia, E. Carroll, Jr, S. Oppenheimer, Microplate Assay for Quantifying Developmental 

Morphologies: Effects of Exogenous Hyalin on Sea Urchin Gastrulation, Zygote, vol 15, pp. 1-6 

(2007). 

Note 38. S. Sajadi, Rojas, S. Oppenheimer, Cyclodextrin, A Probe for Studying Adhesive Interactions, 

Acta Histochemica, vol. 109, pp. 338-342 (2007). 

Note 39. S. Oppenheimer, Cellular Basis of Cancer Metastasis: A Review of Fundamentals and New 

Advances Acta Histochemica, vol. 108, pp. 327-334 (2006). 

Note 40. G. Zem, O. Badali, Gaytan, Hekmatjou, M. Alvarez, J. Nnoli, Katus, S. Oppenheimer, 

Microbead Analysis of Cell Binding to Immobilized Lectin: An Alternative to Microarrays in the 

Development of Carbohydrate Drugs and Diagnostic Tests, Acta Histochemica, vol. 108, pp. 311-317 

(2006). 

Note 41. L. Welty, E. Heinrich, C. Garcia, L. Banner, M. Summers, L. Baresi, S. Metzenberg, C 

Coyle-Thompson, S. Oppenheimer, Analysis of Unconventional Approaches for the Rapid Detection of 

Surface Lectin Binding Ligands on Human Cell Lines Acta Histochemica, vol. 107, pp. 411-420 

(2006). 

Note 42. C. Coyle-Thompson, S. Oppenheimer, A Novel Approach to Study Adhesion Mechanisms by 

Isolation of the Interacting System, Acta Histochemica, vol. 107, pp. 243-251 (2005). 

Note 43. E. Heinrich, L. Welty, L. Banner, S. Oppenheimer, Direct Targeting of Cancer Cells: A 

Multiparameter Approach, Acta Histochemica, vol. 107, pp. 335-344 (2005).  

Note 44. M. Khurrum, Hernandez, Eskalaei, O. Badali, C. Coyle-Thompson, S. Oppenheimer, 

Carbohydrate Involvement in Sea Urchin Gastrula Cellular Interactions Acta Histochemica, vol. 106, 

pp. 97-106 (2004).  

Note 45. M. Maldonado, G. Weerasinghe, F. Ambroise, Yamoah, M. Londono, J. Pelayo, Grigorian, S. 

Oppenheimer, The Charged Milieu: A Major Player in Fertilization Reactions, Acta Histochemica, vol. 

106, pp. 3-10 (2004).  



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Note 46. L. Ngo, M. Barajas, G. Weerasinghe, G. Zem, S. Oppenheimer, A New Histochemical 

Approach for Studying Sperm Cell Surfaces, Acta Histochemica, vol. 105, pp. 21-28 (2003). 

Note 47. M. Khurrum, G. Weerasinghe, E. Soriano, R. Riman, O. Badali, S. Gipson, Medina, Alfaro, V. 

Navarro, C. Harieg, L. Ngo, T. Sakhakorn, L. Kirszenbaum, Khatibi, Abedi, M. Barajas, G. Zem, A. 

Kirszenbaum, Razi, S. Oppenheimer, Analysis of Surface Properties of Human Cancer Cells Using 

Derivatized Beads, Acta Histochemica, vol. 104, pp. 217-223 (2002). 

Note 48. V. Navarro, S. Walker, O. Badali, Abundis L. Ngo, G. Weerasinghe, M. Barajas, G. Zem, S. 

Oppenheimer, Analysis of Surface Properties of Fixed and Live Cells Using Derivatized Agarose Beads, 

Acta Histochemica, vol. 104, pp. 99-106 (2002).  

Note 49. B. Salbilla, H. Vaghefi, Chhabra, Hall, Bworn, Sadoughi, E. Francisco, L. Attas, S. Walker, 

Nguyen, S. Oppenheimer, Analysis of Cell Surface Properties Using Derivatized Agarose Beads, Acta 

histochemica, Vol. 101, pp. 271-279 (1999). 

Note 50. V. Latham, S. Oppenheimer, A Simple Image Analysis Method for Evaluating Cell Binding to 

Derivatized Beads, Acta histochemica, Vol. 101, pp. 263-270 (1999). 

Note 51. V. Latham, M. Tully, S. Oppenheimer, A Putative Role for Carbohydrates in Sea Urchin 

Gastrulation, Acta histochemica, Vol. 101, pp. 293-303 (1999). 

Note 52. V. Latham, L. Latham, S. Oppenheimer, Desktop Computer-Based Image Analysis of Cell 

Surface Fluorescence Patterning from a Photographic Source, Acta histochemica, vol. 98, pp. 295-300 

(1996).   

Note 53. J. Philip, Rodriguez, R. Bada, F. Ambroise and Hernandez, S. Oppenheimer, Charge 

Interactions in Sperm-Egg Recognition, Acta histochemica, Vol. 99, pp. 401-410 (1997).  

Note 54. Ghoneum, Vojdani, A. Banionis, Lagos and Gill, S. Oppenheimer, The Effects of 

Carcinogenic Methylcholanthrene on Carbohydrate Residues of NK cells, Toxicology and Industrial 

Health, Vol. 13, No. 6, pp. 727-741, 1997.  

Note 55. V. Latham, Martinez, L. Cazares, Hamburger M. Tully, S. Oppenheimer, Accessing the 

Embryo Interior Without Microinjection, Acta histochemica, Vol. 100, pp. 193-200 (1998).  

Note 56. R. Roque, S. Herrera, Yeh, J. Philip, T. Borisavljevic, L. Brunick, Miles, Haritunians, C. Addy, 

R. Bada, H. Vaghfi, S. Matsumoto, G. Picionelli and Rodriquez, S. Oppenheimer, Cell Adhesion 

Mechanisms: Modeling Using Derivatized Beads and Sea Urchin Cell Systems, Acta histochemica, Vol. 

98, pp. 441-451 (1996). 

Note 57. M. Daily, V. Latham, C. Garcia, C. Hockman, H. Chun, M. Oppenheimer, S. West, K. 

Rostamiani, R. Chao, E. Pollock, S. Oppenheimer, Producing Exposed Coat-Free Embryos, Zygote, Vol. 

2, pp. 221-225 (1994). 

Note 58. M. Spiegler, S. Oppenheimer, Extending the Viability of Sea Urchin Gametes, Cryobiology, 

Vol. 32, pp. 168-174 (1995).  



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Note 59. V. Latham, J. Ducut, K. Rostamiani, H. Chun, Lopez, S. Herrera, S. Oppenheimer, A Rapid 

Lectin Receptor Binding Assay: Comparative Evaluation of Sea Urchin Embryo Cell Surface Lectin 

Receptors, Acta histochemica, Vol. 97, p. 89-97 (1995).  

Note 60. V. Latham, S. Herrera, K. Rostamiani, H. Chun, S. Oppenheimer, Rapid Identification of 

Lectin Receptors and Their Possible Function in Sea Urchin Cell Systems, Acta histochemica, Vol.97, 

pp. 373-382 (1995). 

Note 61. M. Ghoneum, A. Banionis, Gill and Romero, S. Oppenheimer, Demonstration of Involvement 

of Mannose Residues on NK Cell Cytotoxicity using Lectin - Coupled Beads, Natural Immunity and 

Cell Growth Regulation 10:132 (1991). 

Note 62. S. Oppenheimer, Biology and Cultivation of Teratoma Cells, in Tests of Teratogenicity in 

Vitro, North Holland, Amsterdam, pp. 261-274. 

Note 63. S. Oppenheimer, Human Made Carcinogens vs. Natural Food Carcinogens: Which Post the 

Greatest Cancer Risk? American Clinical Products Review, Vol. 4, No. 2, pp. 16-19, February 1985. 

Note 64. S. Oppenheimer, Cancer and Stress, Longevity Letter, 2(6): 3, 1984.   

Note 65. S. Oppenheimer, Carcinogens in Food and Water, Longevity Letter, 2(9): 2-3, 1984.  

Note 66. S. Oppenheimer Carcinogens in the Home, Longevity Letter, 3(5): 2-4, May 1985. 

Note 67. S. Oppenheimer Preventing Cancer, American Longevity 1 (no.1), pp. 1-5, 1983.  

Note 68. Meyer, P. Thompson, R. Behringer, R. Steiner, Saxton, S. Oppenheimer, Protease Activity 

Associated with Loss of Adhesiveness in Mouse Teratocarcinoma, Exp. Cell Res., 143, pp. 63-70, 

1983.  

Note 69. Meyer, S. Oppenheimer, Carbohydrate Specificity of Sea Urchin Blastula Adhesion 

Component, Exp. Cell. Res., 139, pp. 451-456. 1982.  

Note 70. S. Oppenheimer Causes of Cancer: Gene Alteration Versus Gene Activation, Amer. Lab., pp. 

40-46, November 1982. 

Note 71. J. Meyer, S. Oppenheimer Isolation of Species-specific and Stage-specific Adhesion 

Promoting Component by Disaggregation of Intact Sea Urchin Embryo Cells, Exp. Cell Res., 137, pp. 

471-476, 1982. 

Note 72. C. Capelle, J. Meyer, S. Sorensen, S. Oppenheimer, Isolation of Aggregation Inhibitory Factor 

from Non-Adhesive Mouse Teratoma Cells, Exp. Cell Res., 131, pp. 470-476, 1981.  

Note 73. W. Childress, Freedman, C. Koprowski, Doolittle and P. Sheeler, S. Oppenheiimer, Surface 

Characteristics of Separated Subpopulations of Mouse Teratocarcinoma Cells, Exp. Cell Res., 122, pp. 

39-45, 1979. 

Note 74. M. Grodin, Nystrom, J. Scordato, M. Cantor, S. Oppenheimer, Relationship of Adhesiveness 

of Cells in Culture with Specific Enzyme Activity, Exp. Cell Res., 122, pp. 149-157, 1979.  

Note 75. M. Asao, S. Oppenheimer, Inhibitor of Cell Aggregation by Specific Carbohydrates, Exp. Cell. 

Res., 120, pp. 149-157, 1979.  



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Note 76. S. Oppenheimer Introduction to the Symposium and Studies on the Surfaces of Separated and 

Synchronized Tumor and Embryonic Cell Populations, American Zoologist, 19, pp. 801-808, 1979. 

Note 77. S. Oppenheimer, Cell Surface Carbohydrates in Adhesion and Migration, American Zoologist, 

18, pp. 12-23, 1978.  

Note 78. B. Bales, Brenneman, L. Knapp, Lesin, A. Neri, E. Pollock, S. Oppenheimer Modulation of 

Agglutinability by Alteration of the Surface Topography in Mouse Ascites Tumor Cells, Exp. Cell Res., 

105, pp. 291-300, 1977. 

Note 79. B. Bales, Lesin, S. Oppenheimer On Cell Membrane Lipid Fluidity and Plant Lectin 

Agglutinability: A Spin Label Study of Mouse Ascites Tumor Cells, Biochemica et Biophysica Acta, 

465, pp. 400-407, 1977. 

Note 80. J. Meyer, S. Oppenheimer The Multicomponent Nature of Teratoma Cell Adhesion Factor, 

Exp. Cell Res., 102, pp. 359-364, 1976. 

Note 81. A. Neri, M. Roberson, D. Connolly, S. Oppenheimer, Quantitative Evaluation of Concanavalin 

A Receptor Site Distributions on the Surfaces of Specific Populations of Embryonic Cells, Nature, 258, 

pp. 342-344, 1975.  

Note 82. D. Connolly, S. Oppenheimer Cell Density-Dependent Stimulation of Glutamine Synthetase 

Activity in Cultured Mouse Teratoma Cells, Exp. Cell Res., 94, pp. 459-464, 1975. 

Note 83. M. Roberson, A. Neri, S. Oppenheimer, Distribution of Concanavalin A Receptor Sites on 

Specific Populations of Embryonic Cells, Science, 189, pp. 639-640, 1975. 

Note 84. S. Oppenheimer, Functional Involvement of Specific Carbohydrates in Teratoma Cell 

Adhesion Factor, Exp. Cell Res., 92, pp. 122-126, 1975. 

Note 85. M. Roberson, S. Oppenheimer, Quantitative Agglutination of Specific Populations of Sea 

Urchin Embryo Cells with Concanavalin A Exp. Cell Res. 91, pp. 263-268, 1975. 

Note 86. K. Krach, A. Green G. Nicolson, S. Oppenheimer Cell Surface Changes Occurring During Sea 

Urchin Embryonic Development Monitored by Quantitative Agglutination with Plant Lectins, Exp. 

Cell Res., 84, pp. 191-198, 1974. 

Note 87. S. Oppenheimer, Utilization of L-Glutamine in Intercellular Adhesion: Ascites Tumor and 

Embryonic Cells, Exp. Cell. Res., 77, pp. 175-182, 1983. 

Note 88. R. Potter M. Barber, S. Oppenheimer, Alteration of Sea Urchin Embryo Cell Surface 

Properties by Mycostatin, a Sterol Binding Antibiotic, Developmental Biology, 33, pp. 218-223.  

Note 89. S. Oppenheimer J. Odencrantz, A Quantitative Assay for Measuring Cell Agglutination: 

Agglutination of Sea Urchin Embryo and Mouse Teratoma Cells by Concanavalin A, Exp. Cell Res., 73, 

pp. 475-480, 1972. 

Note 90. S. Oppenheimer, T. Humphreys, Isolation of Specific Macromolecules Required for Adhesion 

of Mouse Tumor Cells, Nature, 232, pp. 125-127, 1971. 



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Note 91. S. Oppenheimer, M. Edidin, C. Orr and S. Roseman, An L-Glutamine Requirement for 

Intercellular Adhesion, Proceedings of the National Academy of Sciences USA, 63, pp. 1395-1402, 

1969.  

Note 92. S. Oppenheimer, Motivating College Students: Evidence from 20 years of Anonymous 

Student Evaluations, Higher Education Reseach, doi: 10.11648 (2019).  

Please Note: Most of the co-authors on these papers are students. These are only the full length 

peer-reviewed papers from the Oppenheimer lab. Published abstracts and national presentations are not 

included. 

Note 93. S. Oppenheimer, Lab Training: Undergraduate Research in Action, Nature 519, 158 (2015). 

Note 94. S. Oppenheimer, Include Mentoring Skills in Hiring and Promotion Criteria, Nature 554, 31 

(2018). 

Note 95. Camacho, N.L., ER Doctor’s Gift Honors Biology Professor for Changing the Trajectory of 

Her Life, CSUN Magazine, (May 30, 2018). 

Note 96. Oppenheimer, S., et al., Applied Science Research for All Part 2 College Level, American 

Journal of Applied Scientific Research 7(1): 1-7 (2020). 

Note 97. Oppenheimer, S., University on the Rise without Ph.D. Students, Nature 538: 171 (2016).