Merlin Crossley

{{Short description|Australian molecular biologist}} {{Use dmy dates|date=September 2016}} {{Use Australian English|date=September 2016}}

{{Infobox scientist/Wikidata|fetchwikidata=ALL}}

'''Merlin Crossley''', {{post-nominals|country=AUS|AM}}<ref name="frs">{{cite web|url=https://www.unsw.edu.au/news/2023/06/unsw-community-recognised-in-2023-king-s-birthday-honours |publisher=UNSW|location=Sydney|title=UNSW community recognised in 2023 King's Birthday Honours}}</ref> is an Australian molecular biologist, university teacher, and administrator. He is Deputy Vice-Chancellor for Academic Quality at the University of New South Wales.<ref>{{Cite web| author1=Zmcomedia |url=http://www.newsroom.unsw.edu.au/news/general/merlin-crossley-appointed-unsw-deputy-vice-chancellor | title=Merlin Crossley | work=UNSW Newsroom | date=19 February 2016 | publisher=unsw.edu.au}}</ref>

==Early life and career== Crossley attended Mount View Primary School, Glen Waverley, Victoria, then was awarded an entrance scholarship to Melbourne Grammar School, where he was dux. He undertook a Bachelor of Science at the University of Melbourne, as a resident of Queen's College (University of Melbourne), then a doctorate at the University of Oxford supported by a Rhodes Scholarship at Magdalen College, Oxford.<ref>{{cite web |url=http://www.rhodeshouse.ox.ac.uk/about/rhodes-scholars/rhodes-scholars-complete-list |archive-url=https://web.archive.org/web/20131106034818/http://www.rhodeshouse.ox.ac.uk/about/rhodes-scholars/rhodes-scholars-complete-list |url-status=dead |archive-date=2013-11-06 |access-date=2014-05-02 |df=dmy-all | title=Rhodes Scholars: Complete List, 1903-2013}}</ref> He worked at Oxford, Harvard and the University of Sydney, before moving to UNSW as Dean of Science.<ref>{{Cite web| author1=z3081268 |url=https://newsroom.unsw.edu.au/news/science/merlin-crossley-reappointed-science-dean | title=Merlin Crossley reappointed Science Dean | date=14 Jan 2014 | website=UNSW Sydney }}</ref> In recognition of his service on the Trust of the Australian Museum a new species of butterfly bobtail squid was named in his honour - ''Iridoteuthis merlini'' - Merlin's bobtail squid.<ref>{{cite web |url=https://newsroom.unsw.edu.au/news/general/new-species-bobtail-squid-named-honour-professor-merlin-crossley | title=New species of bobtail squid named in honour of Professor Merlin Crossley | date=3 August 2021 |access-date=7 August 2021}}</ref><ref>{{cite web |url=https://australian.museum/blog/amri-news/fire-shooting-butterfly-bobtail-named-in-honour-of-professor-merlin-crossley/ |title=Fire shooting 'butterfly bobtail' named in honour of Professor Merlin Crossley! |access-date=7 August 2021}}</ref>

==University leadership== Crossley has held senior roles at both the University of Sydney and the University of New South Wales. He has led the research portfolio, and the teaching portfolio. He is most well known for overseeing the introduction, in 2017, of [https://www.education.unsw.edu.au/teaching/education-focussed-careers Education Focussed Careers] at University of New South Wales. The idea was to formally recognise that the university relied on academics who were primarily dedicated to teaching and to supporting students. Previously the university had sought to ensure that all academics were 'research active', but now appreciates that a good team requires batters, bowlers, and all-rounders. Academics can be promoted for their work in any area. Many argue that, as well as boosting morale, this change has improved the student experience and even contributed to an uplift in the overall quality of research, as only those committed to research generate outputs.

==Research== Crossley is interested in gene regulation. He studied an unusual genetic disorder termed Haemophilia B Leyden where patients recover after puberty.<ref>{{cite journal | pmid = 24138812 | doi=10.1016/j.tig.2013.09.007 | volume=30 | issue=1 | title=Hemophilia B Leyden and once mysterious cis-regulatory mutations | date=Jan 2014 | journal=Trends in Genetics | pages=18–23 | last1 = Funnell | first1 = AP | last2 = Crossley | first2 = M| hdl=1959.4/unsworks_49804 | hdl-access=free }}</ref> The condition results from mutations that disrupt the control region of the clotting factor IX gene.<ref>{{cite journal | pmid = 2342576 | doi=10.1038/345444a0 | volume=345 | issue=6274 | title=Disruption of a C/EBP binding site in the factor IX promoter is associated with haemophilia B | date=May 1990 | journal=Nature | pages=444–6 | last1 = Crossley | first1 = M | last2 = Brownlee | first2 = GG| bibcode=1990Natur.345..444C | s2cid=4261499 }}</ref><ref>{{cite journal | pmid = 23472758 | doi = 10.1016/j.ajhg.2013.02.003 | volume=92 | issue=3 | title=A CpG mutational hotspot in a ONECUT binding site accounts for the prevalent variant of hemophilia B Leyden | date=Mar 2013 | journal=American Journal of Human Genetics | pages=460–7 | pmc=3591849 | last1 = Funnell | first1 = AP | last2 = Wilson | first2 = MD | last3 = Ballester | first3 = B | last4 = Mak | first4 = KS | last5 = Burdach | first5 = J | last6 = Magan | first6 = N | last7 = Pearson | first7 = RC | last8 = Lemaigre | first8 = FP | last9 = Stowell | first9 = KM | last10 = Odom | first10 = DT | last11 = Flicek | first11 = P | last12 = Crossley | first12 = M}}</ref> A testosterone-responsive element accounts for post-pubertal recovery.<ref>{{cite journal | pmid = 1631558 | volume=257 | issue=5068 | title=Recovery from hemophilia B Leyden: an androgen-responsive element in the factor IX promoter | date=Jul 1992 | journal=Science | pages=377–9 | doi=10.1126/science.1631558 | last1 = Crossley | first1 = M | last2 = Ludwig | first2 = M | last3 = Stowell | first3 = KM | last4 = De Vos | first4 = P | last5 = Olek | first5 = K | last6 = Brownlee | first6 = GG| bibcode=1992Sci...257..377C }}</ref>

He has also investigated abnormal patterns of globin gene expression and his work on mutations associated with the lifelong expression of the fetal haemoglobin gene may help in the treatment of thalassemia and sickle cell anaemia.<ref>{{cite journal |pmid=25971621 |doi=10.1038/ncomms8085 |volume=6 |issue=7085 |title=Editing the genome to introduce a beneficial naturally occurring mutation associated with increased fetal globin |date=May 2015 |journal=Nature Communications |pages=377–9 |last1=Wienert |first1=B |last2=Funnell |first2=AP |last3=Norton |first3=LJ |last4=Pearson |first4=RC |last5=Wilkinson-White |first5=LE |last6=Lester |first6=K |last7=Vadolas |first7=J |last8=Porteus |first8=MH |last9=Matthews |first9=JM |last10=Quinlan |first10=KG |last11=Crossley |first11=M |bibcode=2015NatCo...6.7085W |doi-access=free |hdl=1959.4/unsworks_49831 |hdl-access=free}}</ref> He is using CRISPR-mediated gene editing to introduce beneficial mutations in cell lines as models for treating genetic diseases.<ref>{{Cite web|url=http://theconversation.com/turning-the-tables-using-genetic-mutations-to-fix-natures-problems-41593 | title=Turning the tables: using genetic mutations to fix nature's problems| date=13 May 2015| publisher=theconversation.com}}</ref><ref>{{Cite web|url=http://www.crossleylab.unsw.edu.au/ | title=Crossley Lab UNSW Science | publisher=unsw.edu.au}}</ref> Clinical trials by major gene editing companies are now introducing mutations that his lab described.

This recent work is considered highly significant. Because co-inheriting mutations that generate lifelong fetal globin expression (so-called Hereditary Persistence of Fetal Hemoglobin or HPFH mutations) essentially prevents Sickle Cell Disease and beta-thalassemia, understanding the molecular mechanisms and mimicking them by CRISPR-gene editing has become the major therapeutic strategy.<ref>{{Cite journal |last=Orkin |first=Stuart H. |date=2025-06-05 |title=The Fetal-to-Adult Hemoglobin Switch — Mechanism and Therapy |url=http://www.nejm.org/doi/10.1056/NEJMra2405260 |journal=New England Journal of Medicine |language=en |volume=392 |issue=21 |pages=2135–2149 |doi=10.1056/NEJMra2405260 |pmid=40466067 |issn=0028-4793|url-access=subscription }}</ref>

Crossley’s lab made three seminal contributions: he showed all the natural point mutations in the fetal globin gene promoter that cause HPFH either create new sites for gene activating proteins<ref>{{Cite journal |last1=Wienert |first1=Beeke |last2=Funnell |first2=Alister P. W. |last3=Norton |first3=Laura J. |last4=Pearson |first4=Richard C. M. |last5=Wilkinson-White |first5=Lorna E. |last6=Lester |first6=Krystal |last7=Vadolas |first7=Jim |last8=Porteus |first8=Matthew H. |last9=Matthews |first9=Jacqueline M. |last10=Quinlan |first10=Kate G. R. |last11=Crossley |first11=Merlin |date=2015-05-14 |title=Editing the genome to introduce a beneficial naturally occurring mutation associated with increased fetal globin |url=https://www.nature.com/articles/ncomms8085 |journal=Nature Communications |language=en |volume=6 |issue=1 |article-number=7085 |doi=10.1038/ncomms8085 |pmid=25971621 |bibcode=2015NatCo...6.7085W |issn=2041-1723|doi-access=free |hdl=1959.4/unsworks_49831 |hdl-access=free }}</ref><ref>{{Cite journal |last1=Wienert |first1=Beeke |last2=Martyn |first2=Gabriella E. |last3=Kurita |first3=Ryo |last4=Nakamura |first4=Yukio |last5=Quinlan |first5=Kate G. R. |last6=Crossley |first6=Merlin |date=2017-08-10 |title=KLF1 drives the expression of fetal hemoglobin in British HPFH |url=https://ashpublications.org/blood/article/130/6/803/36785/KLF1-drives-the-expression-of-fetal-hemoglobin-in |journal=Blood |language=en |volume=130 |issue=6 |pages=803–807 |doi=10.1182/blood-2017-02-767400 |pmid=28659276 |issn=0006-4971|hdl=1959.4/unsworks_45515 |hdl-access=free }}</ref><ref>{{Cite journal |last1=Martyn |first1=Gabriella E. |last2=Wienert |first2=Beeke |last3=Kurita |first3=Ryo |last4=Nakamura |first4=Yukio |last5=Quinlan |first5=Kate G. R. |last6=Crossley |first6=Merlin |date=2019-02-21 |title=A natural regulatory mutation in the proximal promoter elevates fetal globin expression by creating a de novo GATA1 site |url=https://ashpublications.org/blood/article/133/8/852/260611/A-natural-regulatory-mutation-in-the-proximal |journal=Blood |language=en |volume=133 |issue=8 |pages=852–856 |doi=10.1182/blood-2018-07-863951 |issn=0006-4971}}</ref> or disrupt sites for repressors, BCL11A or ZBTB7A.<ref name=":0">{{Cite journal |last1=Martyn |first1=Gabriella E. |last2=Wienert |first2=Beeke |last3=Yang |first3=Lu |last4=Shah |first4=Manan |last5=Norton |first5=Laura J. |last6=Burdach |first6=Jon |last7=Kurita |first7=Ryo |last8=Nakamura |first8=Yukio |last9=Pearson |first9=Richard C. M. |last10=Funnell |first10=Alister P. W. |last11=Quinlan |first11=Kate G. R. |last12=Crossley |first12=Merlin |date=April 2018 |title=Natural regulatory mutations elevate the fetal globin gene via disruption of BCL11A or ZBTB7A binding |url=https://www.nature.com/articles/s41588-018-0085-0 |journal=Nature Genetics |language=en |volume=50 |issue=4 |pages=498–503 |doi=10.1038/s41588-018-0085-0 |pmid=29610478 |issn=1061-4036|url-access=subscription }}</ref><ref>{{Cite journal |last1=Wienert |first1=Beeke |last2=Martyn |first2=Gabriella E. |last3=Funnell |first3=Alister P.W. |last4=Quinlan |first4=Kate G.R. |last5=Crossley |first5=Merlin |date=December 2018 |title=Wake-up Sleepy Gene: Reactivating Fetal Globin for β-Hemoglobinopathies |url=https://linkinghub.elsevier.com/retrieve/pii/S0168952518301562 |journal=Trends in Genetics |language=en |volume=34 |issue=12 |pages=927–940 |doi=10.1016/j.tig.2018.09.004 |pmid=30287096 |url-access=subscription }}</ref> This is how he discovered ZBTB7A was one of the two major fetal globin repressors,<ref>{{Cite journal |last1=Masuda |first1=Takeshi |last2=Wang |first2=Xin |last3=Maeda |first3=Manami |last4=Canver |first4=Matthew C. |last5=Sher |first5=Falak |last6=Funnell |first6=Alister P. W. |last7=Fisher |first7=Chris |last8=Suciu |first8=Maria |last9=Martyn |first9=Gabriella E. |last10=Norton |first10=Laura J. |last11=Zhu |first11=Catherine |last12=Kurita |first12=Ryo |last13=Nakamura |first13=Yukio |last14=Xu |first14=Jian |last15=Higgs |first15=Douglas R. |date=2016-01-15 |title=Transcription factors LRF and BCL11A independently repress expression of fetal hemoglobin |journal=Science |language=en |volume=351 |issue=6270 |pages=285–289 |doi=10.1126/science.aad3312 |issn=0036-8075 |pmc=4778394 |pmid=26816381 |bibcode=2016Sci...351..285M }}</ref> and is how BCL11A was found to directly repress the fetal globin gene.<ref name=":0" /> He also showed how deletions in the beta-globin locus alleviate fetal globin silencing.<ref name=":1">{{Cite journal |last1=Topfer |first1=Sarah K. |last2=Feng |first2=Ruopeng |last3=Huang |first3=Peng |last4=Ly |first4=Lana C. |last5=Martyn |first5=Gabriella E. |last6=Blobel |first6=Gerd A. |last7=Weiss |first7=Mitchell J. |last8=Quinlan |first8=Kate G. R. |last9=Crossley |first9=Merlin |date=2022-04-07 |title=Disrupting the adult globin promoter alleviates promoter competition and reactivates fetal globin gene expression |url=https://ashpublications.org/blood/article/139/14/2107/483739/Disrupting-the-adult-globin-promoter-alleviates |journal=Blood |language=en |volume=139 |issue=14 |pages=2107–2118 |doi=10.1182/blood.2021014205 |issn=0006-4971 |pmc=8990374 |pmid=35090172}}</ref> There are many different deletions but they all remove the beta-globin gene promoter. This means that the fetal globin promoter no longer has competition from the beta-globin promoter and it can now access the large enhancer, the Locus Control Region.<ref name=":1" /> Finally, he showed that methylation, not only correlates with fetal globin silencing but that removing or adding back DNA methylation (using deadCas9-mediated epigenetic editing) can turn the gene on and off.<ref>{{Cite journal |last1=Bell |first1=Henry W. |last2=Feng |first2=Ruopeng |last3=Shah |first3=Manan |last4=Yao |first4=Yu |last5=Douglas |first5=James |last6=Doerfler |first6=Phillip A. |last7=Mayuranathan |first7=Thiyagaraj |last8=O’Dea |first8=Michael F. |last9=Li |first9=Yichao |last10=Wang |first10=Yong-Dong |last11=Zhang |first11=Jingjing |last12=Mackay |first12=Joel P. |last13=Cheng |first13=Yong |last14=Quinlan |first14=Kate G. R. |last15=Weiss |first15=Mitchell J. |date=2025-07-27 |title=Removal of promoter CpG methylation by epigenome editing reverses HBG silencing |journal=Nature Communications |language=en |volume=16 |issue=1 |article-number=6919 |doi=10.1038/s41467-025-62177-z |issn=2041-1723 |pmc=12297318 |pmid=40715076 |bibcode=2025NatCo..16.6919B }}</ref> This is significant as epigenetic editing does not cut the DNA so may be even safer than standard CRISPR-editing and base editing.

He is also known for the initial identification and cloning of a significant number of genes encoding DNA-binding proteins: KLF3,<ref>{{cite journal | pmid = 8657145 | volume=16 | issue=4 | title=Isolation and characterization of the cDNA encoding BKLF/TEF-2, a major CACCC-box-binding protein in erythroid cells and selected other cells | date = Apr 1996| journal=Mol. Cell. Biol. | pages = 1695–705 | doi=10.1128/mcb.16.4.1695 | pmc=231156 | last1 = Crossley | first1 = M | last2 = Whitelaw | first2 = E | last3 = Perkins | first3 = A | last4 = Williams | first4 = G | last5 = Fujiwara | first5 = Y | last6 = Orkin | first6 = SH| url=http://espace.library.uq.edu.au/view/UQ:367446/UQ367446_OA.pdf }}</ref> KLF8,<ref>{{cite journal | pmid = 10756197 | volume=28 | issue=9 | title=Human Krüppel-like factor 8: a CACCC-box binding protein that associates with CtBP and represses transcription| date=May 2000| journal=Nucleic Acids Research | pages=1955–62 | doi=10.1093/nar/28.9.1955 | pmc=103308 | last1 = van Vliet | first1 = J | last2 = Turner | first2 = J | last3 = Crossley | first3 = M}}</ref> KLF17,<ref>{{cite journal | pmid = 16460907| volume=87 | issue=4 | title=Human KLF17 is a new member of the Sp/KLF family of transcription factors| date= Apr 2006| journal = Genomics | pages=474–82 | doi=10.1016/j.ygeno.2005.12.011 | last1 = van Vliet | first1 = J | last2 = Crofts | first2 = LA | last3 = Quinlan | first3 = KG | last4 = Czolij | first4 = R | last5 = Perkins | first5 = AC | last6 = Crossley | first6 = M| doi-access = }}</ref> EOS IKZF4,<ref>{{cite journal | pmid = 10978333 | doi = 10.1074/jbc.M005457200 | volume=275 | issue=49 | title=Eos and pegasus, two members of the Ikaros family of proteins with distinct DNA binding activities.| date= Dec 2000 | journal = Journal of Biological Chemistry | pages=38347–54 | last1 = Perdomo | first1 = J | last2 = Holmes | first2 = M | last3 = Chong | first3 = B | last4 = Crossley | first4 = M| doi-access = free }}</ref> PEGASUS IKZF5,<ref>{{cite journal | pmid = 10978333 | doi = 10.1074/jbc.M005457200 | volume=275 | issue=49 | title=Eos and pegasus, two members of the Ikaros family of proteins with distinct DNA binding activities | date= Dec 2000 | journal = Journal of Biological Chemistry | pages=38347–54 | last1 = Perdomo | first1 = J | last2 = Holmes | first2 = M | last3 = Chong | first3 = B | last4 = Crossley | first4 = M| doi-access = free }}</ref> and their associated co-regulators: FOG1 ZFPM1,<ref>{{cite journal | pmid = 9230307 | volume=90 | issue=1 | title=FOG, a multitype zinc finger protein, acts as a cofactor for transcription factor GATA-1 in erythroid and megakaryocytic differentiation | date= Jul 1997 | journal = Cell | pages=109–19 | doi=10.1016/s0092-8674(00)80318-9 | last1 = Tsang | first1 = AP | last2 = Visvader | first2 = JE | last3 = Turner | first3 = CA | s2cid=2085524 |display-authors=etal | doi-access= free }}</ref> FOG2 ZFPM2,<ref>{{cite journal | pmid = 10438528 | volume=274 | issue=33 | title=hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2 and modulates GATA-mediated activation| date= Aug 1999 | journal = Journal of Biological Chemistry | pages=23491–890 | doi=10.1074/jbc.274.33.23491 | last1 = Holmes | first1 = M | last2 = Turner | first2 = J | last3 = Fox | first3 = A | last4 = Chisholm | first4 = O | last5 = Crossley | first5 = M | last6 = Chong | first6 = B| doi-access = free }}</ref> and CTBP2.<ref>{{cite journal | pmid = 9724649| volume=17 | issue=17 | title=Cloning and characterization of mCtBP2, a co-repressor that associates with basic Krüppel-like factor and other mammalian transcriptional regulators| date= Sep 1998 | journal = EMBO Journal | pages=5129–40 | doi=10.1093/emboj/17.17.5129 | pmc=1170841 | last1 = Turner | first1 = J | last2 = Crossley | first2 = M}}</ref> These genes encode gene regulatory proteins (also known as transcription factors) and their co-regulators that turn genes on and off. Identifying the proteins involved was an important foundational step in our understanding of how the genome is regulated.

Several additional discoveries are of note: in the early 2000s his lab noted that several gene regulatory proteins that turn genes off contained SUMOylation motifs within their repression domains.<ref>{{Cite journal |last1=Perdomo |first1=José |last2=Verger |first2=Alexis |last3=Turner |first3=Jeremy |last4=Crossley |first4=Merlin |date=2005-02-01 |title=Role for SUMO Modification in Facilitating Transcriptional Repression by BKLF |url=https://www.tandfonline.com/doi/full/10.1128/MCB.25.4.1549-1559.2005 |journal=Molecular and Cellular Biology |language=en |volume=25 |issue=4 |pages=1549–1559 |doi=10.1128/MCB.25.4.1549-1559.2005 |issn=1098-5549|pmc=548027 }}</ref><ref>{{Cite journal |last1=Verger |first1=Alexis |last2=Perdomo |first2=José |last3=Crossley |first3=Merlin |date=February 2003 |title=Modification with SUMO: A role in transcriptional regulation |journal=EMBO Reports |language=en |volume=4 |issue=2 |pages=137–142 |doi=10.1038/sj.embor.embor738 |issn=1469-221X |pmc=1315836 |pmid=12612601}}</ref> In 2023 a comprehensive study of the 2000 gene regulatory proteins in humans in ''Nature'' concluded that indeed repression domains do typically have SUMOylation sites, thus linking SUMOylation with gene repression.<ref>{{Cite journal |last1=DelRosso |first1=Nicole |last2=Tycko |first2=Josh |last3=Suzuki |first3=Peter |last4=Andrews |first4=Cecelia |last5=Aradhana |last6=Mukund |first6=Adi |last7=Liongson |first7=Ivan |last8=Ludwig |first8=Connor |last9=Spees |first9=Kaitlyn |last10=Fordyce |first10=Polly |last11=Bassik |first11=Michael C. |last12=Bintu |first12=Lacramioara |date=2023-04-13 |title=Large-scale mapping and mutagenesis of human transcriptional effector domains |journal=Nature |language=en |volume=616 |issue=7956 |pages=365–372 |doi=10.1038/s41586-023-05906-y |issn=0028-0836 |pmc=10484233 |pmid=37020022 |bibcode=2023Natur.616..365D }}</ref> The second discovery involves zinc fingers, small protein domains usually known for DNA-binding. His lab was involved in showing that zinc fingers can also mediate protein-protein interactions, best characterized by the interaction between the blood gene regulatory proteins, GATA1 and Friend of GATA.<ref>{{Cite journal |last1=Tsang |first1=Alice P |last2=Visvader |first2=Jane E |last3=Turner |first3=C.Alexander |last4=Fujiwara |first4=Yuko |last5=Yu |first5=Channing |last6=Weiss |first6=Mitchell J |last7=Crossley |first7=Merlin |last8=Orkin |first8=Stuart H |date=July 1997 |title=FOG, a Multitype Zinc Finger Protein, Acts as a Cofactor for Transcription Factor GATA-1 in Erythroid and Megakaryocytic Differentiation |url=https://linkinghub.elsevier.com/retrieve/pii/S0092867400803189 |journal=Cell |language=en |volume=90 |issue=1 |pages=109–119 |doi=10.1016/S0092-8674(00)80318-9|url-access=subscription }}</ref><ref>{{Cite journal |last1=Fox |first1=Archa H. |last2=Liew |first2=Chu |last3=Holmes |first3=Melissa |last4=Kowalski |first4=Kasper |last5=Mackay |first5=Joel |last6=Crossley |first6=Merlin |date=1999-05-17 |title=Transcriptional cofactors of the FOG family interact with GATA proteins by means of multiple zinc fingers |url=https://link.springer.com/article/10.1093/emboj/18.10.2812 |journal=The EMBO Journal |volume=18 |issue=10 |pages=2812–2822 |doi=10.1093/emboj/18.10.2812 |pmid=10329627 |pmc=1171362 |issn=0261-4189}}</ref><ref>{{Cite journal |last1=Liew |first1=Chu Kong |last2=Simpson |first2=Raina J. Y. |last3=Kwan |first3=Ann H. Y. |last4=Crofts |first4=Linda A. |last5=Loughlin |first5=Fionna E. |last6=Matthews |first6=Jacqueline M. |last7=Crossley |first7=Merlin |last8=Mackay |first8=Joel P. |date=2005-01-18 |title=Zinc fingers as protein recognition motifs: Structural basis for the GATA-1/Friend of GATA interaction |journal=Proceedings of the National Academy of Sciences |language=en |volume=102 |issue=3 |pages=583–588 |doi=10.1073/pnas.0407511102 |doi-access=free |issn=0027-8424 |pmc=545545 |pmid=15644435 |bibcode=2005PNAS..102..583L }}</ref><ref>{{Cite journal |last1=Mackay |first1=Joel P. |last2=Crossley |first2=Merlin |date=1998-01-01 |title=Zinc fingers are sticking together |url=https://www.cell.com/trends/biochemical-sciences/abstract/S0968-0004(97)01168-7 |journal=Trends in Biochemical Sciences |language=English |volume=23 |issue=1 |pages=1–4 |doi=10.1016/S0968-0004(97)01168-7 |issn=0968-0004 |pmid=9478126|url-access=subscription }}</ref> He has been the advisor to the Human Genome Nomenclature Committee on the naming of the Kruppel-like Factor family and as well as identifying and cloning the genes for KLF3, KLF8, and KLF17, he discovered the cross-regulation between KLF1, KLF3, and KLF8, illustrating both redundancy and inter-dependency within this gene family.<ref>{{Cite journal |last1=Eaton |first1=Sally A. |last2=Funnell |first2=Alister P.W. |last3=Sue |first3=Nancy |last4=Nicholas |first4=Hannah |last5=Pearson |first5=Richard C.M. |last6=Crossley |first6=Merlin |date=October 2008 |title=A Network of Krüppel-like Factors (Klfs) |journal=Journal of Biological Chemistry |language=en |volume=283 |issue=40 |pages=26937–26947 |doi=10.1074/jbc.M804831200 |doi-access=free |pmid=18687676 |pmc=2556010 }}</ref>

==Other activities== He has contributed numerous articles on molecular genetics and education to newspapers and media outlets such as The Conversation (website)<ref>{{Cite web|url=http://theconversation.com/profiles/merlin-crossley-22601/articles | title=theconversation.com/profiles/merlin-crossley-22601/articles | date=15 December 2021 | publisher=theconversation.com}}</ref> and has promoted science communication, for instance as a member of the judging panel for the annual anthology, ''Best Australian Science Writing''.<ref>{{Cite web|url=http://www.newsouthpublishing.com/scienceprize | title=The Bragg UNSW Press Prize for Science Writing | publisher=newsouthpublishing.com}}</ref> He is Deputy Director of the Australian Science Media Centre (AusSMC),<ref>{{cite web|url=http://www.smc.org.au/about-us/our-people/board-members/|title=Board members - AusSMC - Australian Science Media Centre|website=www.smc.org.au}}</ref> has served on the Trust of the Australian Museum 2012-20<ref>{{Cite web|url=https://australianmuseum.net.au/australian-museum-trustees | title=Australian Museum Trustees | publisher=australianmuseum.net.au}}</ref> and the Board of the Sydney Institute of Marine Science 2010-15,<ref>{{Cite web|url=http://sims.org.au/about/people/ | title=SIMS is a collaboration which is stronger than its individual parts/articles | publisher=sims.org.au}}</ref> and is on the Board of, and Chair of the Editorial Board of The Conversation (website).

==Honours and awards== * Member (AM) in the General Division of the Order of Australia - 2023<ref>{{cite web |url=https://www.gg.gov.au/kings-birthday-2023-honours-list |access-date=12 June 2023}}</ref> * Award for Research Excellence, Federation of Asian and Oceanian Biochemists and Molecular Biologists - 2023<ref>{{cite web|url=https://faobmb.com/2023/06/27/winner-of-2023-faobmb-award-for-research-excellence/ | title=Winner of 2023 FAOBMB Award for Research Excellence | access-date= 12 March 2023}}</ref> * Lemberg Medal, Australian Society of Biochemistry and Molecular Biology – 2021<ref>{{cite web|url=http://www.asbmb.org.au/merlin-crossley-2/ |title=HE 2021 Lemberg Medal: Merlin Crossley | access-date= 7 August 2021}}</ref> * NSW Premier's Prize for Excellence in Medical Biological Sciences - 2020<ref>{{cite web |url=https://www.chiefscientist.nsw.gov.au/events/nsw-premiers-prizes-for-science-and-engineering/2020-category-winners | title=2020 Category Winners | date=27 October 2020 | access-date = 7 August 2021}}</ref> * Fellow of the Royal Society of New South Wales - 2014<ref>{{cite web|url=http://royalsoc.org.au/about-us/fellows|title=Fellows - The Royal Society of NSW|website=royalsoc.org.au|date=18 November 2015 }}</ref> * Fellow of Queen's College (University of Melbourne) - 2013<ref>{{cite web|url=https://www.queens.unimelb.edu.au/about/fellows/|title=Fellows - Queen's College - The University of Melbourne - Queen's College - The University of Melbourne|first=Queen's|last=College|website=www.queens.unimelb.edu.au|date=22 November 2017 }}</ref> * Julian Wells Medal, Lorne Genome Conference - 2010<ref>http://www.lornegenome.asnevents.com.au/index84bb.html?option=com_content&view=article&id=38&Itemid=29{{dead link|date=January 2018 |bot=InternetArchiveBot |fix-attempted=yes }}</ref> * Australian Academy of Science Gottschalk Medal - 2002<ref>{{cite web |url=http://www.sciencearchive.org.au/awards/awards/gottschalk.html |title=Australian Academy of Science - Gottschalk medal |access-date=2014-12-11 |url-status=dead |archive-url=https://archive.today/20140826095815/http://www.sciencearchive.org.au/awards/awards/gottschalk.html |archive-date=26 August 2014 |df=dmy-all }}</ref> * Royal Society of New South Wales Sir Edgeworth David Medal - 2000<ref>{{Cite web |url=http://royalsoc.org.au/awards/edgeworth_david.htm |title=Edgeworth David Medal |access-date=26 August 2014 |archive-url=https://web.archive.org/web/20140720040618/http://royalsoc.org.au/awards/edgeworth_david.htm |archive-date=20 July 2014 |url-status=dead }}</ref> * Australian Society for Biochemistry and Molecular Biology Roche Medal - 1999<ref>{{cite web |url=https://www.asbmb.org.au/researchmedal.html |title=Medalists|website=asbmb.org.au}}</ref> * Rhodes Scholarship 1987 -1990<ref>{{cite web |url=http://www.rhodeshouse.ox.ac.uk/about/rhodes-scholars/rhodes-scholars-complete-list |archive-url=https://web.archive.org/web/20131106034818/http://www.rhodeshouse.ox.ac.uk/about/rhodes-scholars/rhodes-scholars-complete-list |url-status=dead |archive-date=2013-11-06 |df=dmy-all | title= Rhodes Scholars: Complete List, 1903-2013 | access-date = 7 August 2021 }}</ref>

== References == {{Reflist}}

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{{DEFAULTSORT:Crossley, Merlin}} Category:Living people Category:Year of birth missing (living people) Category:Scientists from Melbourne Category:Academic staff of the University of New South Wales Category:University of Melbourne alumni Category:Australian molecular biologists Category:Alumni of Magdalen College, Oxford Category:Australian Rhodes Scholars Category:Harvard University faculty Category:Academic staff of the University of Sydney Category:People educated at Melbourne Grammar School Category:Members of the Order of Australia