• Judson H.F.
• Gratzer W.

The eighth day of creation.

Nature. 1997; 386: 344

• Avery O.
• et al.

Studies on the chemical nature of the substance causing transformation of the pneumococcal types. Induction by a desoxyribonucleic acid fraction isolated from pneumococcus type III.

J. Exp. Med. 1944; 79: 137-158

• Franklin R.E.
• Gosling R.G.

Evidence for 2-chain helix in crystalline structure of sodium deoxyribonucleate.

Nature. 1953; 172: 156-157

• Watson J.D.
• Crick F.H.

Molecular structure of nucleic acids: A structure for deoxyribose nucleic acid.

Nature. 1953; 171: 737-738

• Brenner S.
• et al.

An unstable intermediate carrying information from genes to ribosomes for protein synthesis.

Nature. 1961; 190: 576-581

• Gros F.
• et al.

Unstable ribonucleic acid revealed by pulse labelling of Escherichia coli.

Nature. 1961; 190: 581-585

• Lohrmann R.
• et al.

Studies on polynucleotides. LI. Syntheses of the 64 possible ribotrinucleotides derived from the four major ribomononucleotides.

J. Am. Chem. Soc. 1966; 88: 819-829

• Brenner S.
• et al.

UGA: A third nonsense triplet in the genetic code.

Nature. 1967; 213: 449-450

Central dogma of molecular biology.

Nature. 1970; 227: 561-563

• Grunberg-Manago M.

Enzymatic synthesis of nucleic acids.

Prog. Biophys. Mol. Biol. 1963; 13: 175-239

• Cramer P.
• et al.

Structural basis of transcription: RNA polymerase II at 2.8 Ångstrom resolution.

Science. 2001; 292: 1863-1876

• Nissen P.
• et al.

The structural basis of ribosome activity in peptide bond synthesis.

Science. 2000; 289: 920-930

• Jacob F.
• Monod J.

Genetic regulatory mechanisms in the synthesis of proteins.

J. Mol. Biol. 1961; 3: 318-356

• Luria S.E.
• Delbrück M.

Mutations of bacteria from virus sensitivity to virus resistance.

Genetics. 1943; 28: 491

• Arber W.
• Linn S.

DNA modification and restriction.

Annu. Rev. Biochem. 1969; 38: 467-500

Lysogeny.

Bacteriol. Rev. 1953; 17: 269-337

• Nathans D.
• Smith H.O.

Restriction endonucleases in the analysis and restructuring of DNA molecules.

Annu. Rev. Biochem. 1975; 44: 273-293

• Mertz J.E.
• Davis R.W.

Cleavage of DNA by R1 restriction endonuclease generates cohesive ends.

Proc. Natl. Acad. Sci. U. S. A. 1972; 69: 3370-3374

• Jackson D.A.
• et al.

Biochemical method for inserting new genetic information into DNA of simian virus 40: Circular SV40 DNA molecules containing lambda phage genes and the galactose operon of Escherichia coli.

Proc. Natl. Acad. Sci. U. S. A. 1972; 69: 2904-2909

• Chang A.C.
• Cohen S.N.

Genome construction between bacterial species in vitro: Replication and expression of Staphylococcus plasmid genes in Escherichia coli.

Proc. Natl. Acad. Sci. U. S. A. 1974; 71: 1030-1034

• Morrow J.F.
• et al.

Replication and transcription of eukaryotic DNA in Escherichia coli.

Proc. Natl. Acad. Sci. U. S. A. 1974; 71: 1743-1747

• Hutchison C.A.
• et al.

Mutagenesis at a specific position in a DNA sequence.

J. Biol. Chem. 1978; 253: 6551-6560

• Maxam A.M.
• Gilbert W.

A new method for sequencing DNA.

Proc. Natl. Acad. Sci. U. S. A. 1977; 74: 560-564

• Sanger F.
• et al.

DNA sequencing with chain-terminating inhibitors.

Proc. Natl. Acad. Sci. U. S. A. 1977; 74: 5463-5467

• Itakura K.
• et al.

Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin.

Science. 1977; 198: 1056-1063

• Riggs A.
• Itakura K.

Synthetic DNA and medicine.

Am. J. Hum. Genet. 1979; 31: 531

• Saiki R.K.
• et al.

Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia.

Science. 1985; 230: 1350-1354

• van Kasteren P.B.
• et al.

Comparison of seven commercial RT-PCR diagnostic kits for COVID-19.

J. Clin. Virol. 2020; 128104412

• Stemmer W.P.

Rapid evolution of a protein in vitro by DNA shuffling.

Nature. 1994; 370: 389-391

• Arnold F.H.

Directed evolution: Bringing new chemistry to life.

Angew. Chem. Int. Ed. Engl. 2018; 57: 4143-4148

• Bouzetos E.
• et al.

(R) evolution-on-a-chip.

Trends Biotechnol. 2022; 40: 60-76

• van Dijk E.L.
• et al.

Ten years of next-generation sequencing technology.

Trends Genet. 2014; 30: 418-426

• Sanger F.
• et al.

Nucleotide sequence of bacteriophage φX174 DNA.

Nature. 1977; 265: 687-695

• Fleischmann R.D.
• et al.

Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.

Science. 1995; 269: 496-512

• Goffeau A.
• et al.

Life with 6000 genes.

Science. 1996; 274: 546-567

• Arabidopsis Genome Initiative

Analysis of the genome sequence of the flowering plant Arabidopsis thaliana.

Nature. 2000; 408: 796-815

• Venter J.C.
• et al.

The sequence of the human genome.

Science. 2001; 291: 1304-1351

• Nurk S.
• et al.

The complete sequence of a human genome.

Science. 2022; 376: 44-53

• Lander E.S.
• et al.

Initial sequencing and analysis of the human genome.

Nature. 2001; 409: 860-921

• Merryman C.
• Gibson D.G.

Methods and applications for assembling large DNA constructs.

Metab. Eng. 2012; 14: 196-204

• Murphy K.C.

λ recombination and recombineering.

EcoSal Plus. 2016; 7

• Lesterlin C.
• et al.

RecA bundles mediate homology pairing between distant sisters during DNA break repair.

Nature. 2014; 506: 249-253

• Patinios C.
• et al.

Streamlined CRISPR genome engineering in wild-type bacteria using SIBR-Cas.

Nucleic Acids Res. 2021;

• Reece-Hoyes J.S.
• Walhout A.J.

Gateway recombinational cloning.

Cold Spring Harbor Protoc. 2018; 2018 ()

• Tuntufye H.N.
• Goddeeris B.M.

Use of lambda Red-mediated recombineering and Cre/lox for generation of markerless chromosomal deletions in avian pathogenic Escherichia coli.

FEMS Microbiol. Lett. 2011; 325: 140-147

• Zhang Y.
• et al.

A new logic for DNA engineering using recombination in Escherichia coli.

Nat. Genet. 1998; 20: 123-128

• Murphy K.C.

Use of bacteriophage λ recombination functions to promote gene replacement in Escherichia coli.

J. Bacteriol. 1998; 180: 2063-2071

• Zhang Y.
• et al.

DNA cloning by homologous recombination in Escherichia coli.

Nat. Biotechnol. 2000; 18: 1314-1317

• Wannier T.M.
• et al.

Recombineering and MAGE.

Nat. Rev. Methods Prim. 2021; 1: 7

• Yilmaz S.
• et al.

Towards next-generation cell factories by rational genome-scale engineering.

Nat. Catal. 2022; 5: 751-765

• Jiang W.
• et al.

RNA-guided editing of bacterial genomes using CRISPR-Cas systems.

Nat. Biotechnol. 2013; 31: 233-239

• Bubnov D.M.
• et al.

Robust counterselection and advanced λRed recombineering enable markerless chromosomal integration of large heterologous constructs.

Nucleic Acids Res. 2022; 50: 8947-8960

• Stoddard B.L.

Homing endonucleases: From microbial genetic invaders to reagents for targeted DNA modification.

Structure. 2011; 19: 7-15

• Kim Y.-G.
• et al.

Hybrid restriction enzymes: zinc finger fusions to Fok I cleavage domain.

Proc. Natl. Acad. Sci. 1996; 93: 1156-1160

• Urnov F.D.
• et al.

Genome editing with engineered zinc finger nucleases.

Nat. Rev. Genet. 2010; 11: 636-646

• Boch J.
• et al.

Breaking the code of DNA binding specificity of TAL-type III effectors.

Science. 2009; 326: 1509-1512

• Christian M.
• et al.

Targeting DNA double-strand breaks with TAL effector nucleases.

Genetics. 2010; 186: 757-761

• Li Y.
• et al.

Assembly and validation of versatile transcription activator-like effector libraries.

Sci. Rep. 2014; 4: 1-7

• Feng R.
• et al.

RNA Therapeutics – research and clinical advancements.

Front. Mol. Biosci. 2021; 913

• Swarts D.C.
• et al.

DNA-guided DNA interference by a prokaryotic Argonaute.

Nature. 2014; 507: 258-261

• Hegge J.W.
• et al.

Prokaryotic Argonaute proteins: Novel genome-editing tools?.

Nat. Rev. Microbiol. 2018; 16: 5-11

• Hegge J.W.
• et al.

DNA-guided DNA cleavage at moderate temperatures by Clostridium butyricum Argonaute.

Nucleic Acids Res. 2019; 47: 5809-5821

• Fu L.
• et al.

The prokaryotic Argonaute proteins enhance homology sequence-directed recombination in bacteria.

Nucleic Acids Res. 2019; 47: 3568-3579

• Huang S.
• et al.

Guide-directed DNA cleavage by a prokaryotic Argonaute protein induces chromosome recombination in Escherichia coli.

bioRxiv. 2022; ()

• Esyunina D.
• et al.

Specific targeting of plasmids with Argonaute enables genome editing.

bioRxiv. 2022; ()

• Song J.
• et al.

Highly specific enrichment of rare nucleic acid fractions using Thermus thermophilus argonaute with applications in cancer diagnostics.

Nucleic Acids Res. 2020; 48: e19

• Ishino Y.
• et al.

Nucleotide sequence of the iap gene, responsible for alkaline phosphatase isozyme conversion in Escherichia coli, and identification of the gene product.

J. Bacteriol. 1987; 169: 5429-5433

• Jansen R.
• et al.

Identification of genes that are associated with DNA repeats in prokaryotes.

Mol. Microbiol. 2002; 43: 1565-1575

• Makarova K.S.
• et al.

A DNA repair system specific for thermophilic Archaea and bacteria predicted by genomic context analysis.

Nucleic Acids Res. 2002; 30: 482-496

• Makarova K.S.
• et al.

Evolutionary classification of CRISPR–Cas systems: a burst of class 2 and derived variants.

Nat. Rev. Microbiol. 2020; 18: 67-83

• Wu W.Y.
• et al.

The miniature CRISPR-Cas12m effector binds DNA to block transcription.

Mol. Cell. 2022; 82: 4487-4502.e7

• Brouns S.J.
• et al.

Small CRISPR RNAs guide antiviral defense in prokaryotes.

Science. 2008; 321: 960-964

• Sinkunas T.
• et al.

Cas3 is a single-stranded DNA nuclease and ATP-dependent helicase in the CRISPR/Cas immune system.

EMBO J. 2011; 30: 1335-1342

• Garneau J.E.
• et al.

The CRISPR/Cas bacterial immune system cleaves bacteriophage and plasmid DNA.

Nature. 2010; 468: 67-71

• Zetsche B.
• et al.

Cpf1 is a single RNA-guided endonuclease of a class 2 CRISPR-Cas system.

Cell. 2015; 163: 759-771

• Hale C.R.
• et al.

RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.

Cell. 2009; 139: 945-956

• Abudayyeh O.O.
• et al.

C2c2 is a single-component programmable RNA-guided RNA-targeting CRISPR effector.

Science. 2016; 353aaf5573

• Strecker J.
• et al.

RNA-guided DNA insertion with CRISPR-associated transposases.

Science. 2019; 365: 48-53

• Huang C.J.
• et al.

A naturally DNase-free CRISPR-Cas12c enzyme silences gene expression.

Mol. Cell. 2022; 82: 2148-2160. e2144

• Barrangou R.
• et al.

CRISPR provides acquired resistance against viruses in prokaryotes.

Science. 2007; 315: 1709-1712

• Deltcheva E.
• et al.

CRISPR RNA maturation by trans-encoded small RNA and host factor RNase III.

Nature. 2011; 471: 602-607

• Deveau H.
• et al.

Phage response to CRISPR-encoded resistance in Streptococcus thermophilus.

J. Bacteriol. 2008; 190: 1390-1400

• Mojica F.J.
• et al.

Short motif sequences determine the targets of the prokaryotic CRISPR defence system.

Microbiology. 2009; 155: 733-740

• Wu W.Y.
• et al.

Genome editing by natural and engineered CRISPR-associated nucleases.

Nat. Chem. Biol. 2018; 14: 642-651

• Sapranauskas R.
• et al.

The Streptococcus thermophilus CRISPR/Cas system provides immunity in Escherichia coli.

Nucleic Acids Res. 2011; 39: 9275-9282

• Jinek M.
• et al.

A programmable dual-RNA–guided DNA endonuclease in adaptive bacterial immunity.

Science. 2012; 337: 816-821

• Gasiunas G.
• et al.

Cas9–crRNA ribonucleoprotein complex mediates specific DNA cleavage for adaptive immunity in bacteria.

Proc. Natl. Acad. Sci. 2012; 109: E2579-E2586

• Cho S.W.
• et al.

Targeted genome engineering in human cells with the Cas9 RNA-guided endonuclease.

Nat. Biotechnol. 2013; 31: 230-232

• Cong L.
• et al.

Multiplex genome engineering using CRISPR/Cas systems.

Science. 2013; 339: 819-823

• Jinek M.
• et al.

RNA-programmed genome editing in human cells.

eLife. 2013; 2e00471

• Mali P.
• et al.

RNA-guided human genome engineering via Cas9.

Science. 2013; 339: 823-826

• Makarova K.S.
• et al.

An updated evolutionary classification of CRISPR–Cas systems.

Nat. Rev. Microbiol. 2015; 13: 722-736

• Cameron P.
• et al.

Harnessing type I CRISPR–Cas systems for genome engineering in human cells.

Nat. Biotechnol. 2019; 37: 1471-1477

• Slaymaker I.M.
• Gaudelli N.M.

Engineering Cas9 for human genome editing.

Curr. Opin. Struct. Biol. 2021; 69: 86-98

• Anzalone A.V.
• et al.

Genome editing with CRISPR–Cas nucleases, base editors, transposases and prime editors.

Nat. Biotechnol. 2020; 38: 824-844

• Komor A.C.
• et al.

Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage.

Nature. 2016; 533: 420-424

• Anzalone A.V.
• et al.

Programmable deletion, replacement, integration and inversion of large DNA sequences with twin prime editing.

Nat. Biotechnol. 2022; 40: 731-740

• Yarnall M.T.
• et al.

Drag-and-drop genome insertion of large sequences without double-strand DNA cleavage using CRISPR-directed integrases.

Nat. Biotechnol. 2022; ()

• Gilbert L.A.
• et al.

Genome-scale CRISPR-mediated control of gene repression and activation.

Cell. 2014; 159: 647-661

• Bikard D.
• et al.

Programmable repression and activation of bacterial gene expression using an engineered CRISPR-Cas system.

Nucleic Acids Res. 2013; 41: 7429-7437

• Cox D.B.
• et al.

RNA editing with CRISPR-Cas13.

Science. 2017; 358: 1019-1027

• Xu C.
• et al.

Programmable RNA editing with compact CRISPR–Cas13 systems from uncultivated microbes.

Nat. Methods. 2021; 18: 499-506

• Marina R.J.
• et al.

Evaluation of engineered CRISPR-Cas-mediated systems for site-specific RNA editing.

Cell Rep. 2020; 33108350

• Shams A.
• et al.

Comprehensive deletion landscape of CRISPR-Cas9 identifies minimal RNA-guided DNA-binding modules.

Nat. Commun. 2021; 12: 5664

• Zhang L.
• et al.

AsCas12a ultra nuclease facilitates the rapid generation of therapeutic cell medicines.

Nat. Commun. 2021; 12: 3908

• Nguyen G.T.
• et al.

Miniature CRISPR-Cas12 endonucleases–Programmed DNA targeting in a smaller package.

Curr. Opin. Struct. Biol. 2022; 77102466

• Schmitz M.
• et al.

Structural basis for the assembly of the type V CRISPR-associated transposon complex.

Cell. 2022; 185: 4999-5010.e17

• Jiao C.
• et al.

Noncanonical crRNAs derived from host transcripts enable multiplexable RNA detection by Cas9.

Science. 2021; 372: 941-948

• Chen J.S.
• et al.

CRISPR-Cas12a target binding unleashes indiscriminate single-stranded DNase activity.

Science. 2018; 360: 436-439

• Gootenberg J.S.
• et al.

Nucleic acid detection with CRISPR-Cas13a/C2c2.

Science. 2017; 356: 438-442

• Santiago-Frangos A.
• et al.

Intrinsic signal amplification by type III CRISPR-Cas systems provides a sequence-specific SARS-CoV-2 diagnostic.

Cell Rep. Med. 2021; 2100319

• Steens J.A.
• et al.

SCOPE enables type III CRISPR-Cas diagnostics using flexible targeting and stringent CARF ribonuclease activation.

Nat. Commun. 2021; 12: 5033

• Donohoue P.D.
• et al.

Advances in industrial biotechnology using CRISPR-Cas systems.

Trends Biotechnol. 2018; 36: 134-146

GABA-enriched tomato is first CRISPR-edited food to enter market.

Nat. Biotechnol. 2022; 40: 9-11

• Zsögön A.
• et al.

De novo domestication of wild tomato using genome editing.

Nat. Biotechnol. 2018; 36: 1211-1216

• Zong Y.
• et al.

Precise base editing in rice, wheat and maize with a Cas9-cytidine deaminase fusion.

Nat. Biotechnol. 2017; 35: 438-440

• Rodríguez-Leal D.
• et al.

Engineering quantitative trait variation for crop improvement by genome editing.

Cell. 2017; 171: 470-480. e478

• Li C.
• et al.

Targeted, random mutagenesis of plant genes with dual cytosine and adenine base editors.

Nat. Biotechnol. 2020; 38: 875-882

Genome engineering for crop improvement and future agriculture.

Cell. 2021; 184: 1621-1635

• Barrangou R.
• Doudna J.A.

Applications of CRISPR technologies in research and beyond.

Nat. Biotechnol. 2016; 34: 933-941

• Huang C.-H.
• et al.

Applications of CRISPR-Cas enzymes in cancer therapeutics and detection.

Trends Cancer. 2018; 4: 499-512

• Riley R.S.
• et al.

Delivery technologies for cancer immunotherapy.

Nat. Rev. Drug Discov. 2019; 18: 175-196

• Doudna J.A.

The promise and challenge of therapeutic genome editing.

Nature. 2020; 578: 229-236

• Gallagher J.

Base editing: Revolutionary therapy clears girl’s incurable cancer.

• Kounang N.

Gene editing technology for treatment-resistant cancer could be a ‘scientific layup’ to treat other diseases.

• Ledford H.

CRISPR treatment inserted directly into the body for first time.

Nature. 2020; 579: 185-186

• Baek M.
• et al.

Accurate prediction of protein structures and interactions using a three-track neural network.

Science. 2021; 373: 871-876

• Jumper J.
• et al.

Highly accurate protein structure prediction with AlphaFold.

Nature. 2021; 596: 583-589

• Rives A.
• et al.

Biological structure and function emerge from scaling unsupervised learning to 250 million protein sequences.

Proc. Natl. Acad. Sci. 2021; 118e2016239118

60 years ago, Francis Crick changed the logic of biology.

PLoS Biol. 2017; 15e2003243

• Mans R.
• et al.

CRISPR/Cas9: A molecular Swiss army knife for simultaneous introduction of multiple genetic modifications in Saccharomyces cerevisiae.

FEMS Yeast Res. 2015; 15fov004

• Anzalone A.V.
• et al.

Search-and-replace genome editing without double-strand breaks or donor DNA.

Nature. 2019; 576: 149-157

• Mojica F.J.
• et al.

Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements.

J. Mol. Evol. 2005; 60: 174-182

• Pourcel C.
• et al.

CRISPR elements in Yersinia pestis acquire new repeats by preferential uptake of bacteriophage DNA, and provide additional tools for evolutionary studies.

Microbiology. 2005; 151: 653-663

• Bolotin A.
• et al.

Clustered regularly interspaced short palindrome repeats (CRISPRs) have spacers of extrachromosomal origin.

Microbiology. 2005; 151: 2551-2561

• Makarova K.S.
• et al.

Evolution and classification of the CRISPR–Cas systems.

Nat. Rev. Microbiol. 2011; 9: 467-477

• Wiedenheft B.
• et al.

Structures of the RNA-guided surveillance complex from a bacterial immune system.

Nature. 2011; 477: 486-489

• Nishimasu H.
• et al.

Crystal structure of Cas9 in complex with guide RNA and target DNA.

Cell. 2014; 156: 935-949

• Jinek M.
• et al.

Structures of Cas9 endonucleases reveal RNA-mediated conformational activation.

Science. 2014; 3431247997

• Niewoehner O.
• et al.

Type III CRISPR–Cas systems produce cyclic oligoadenylate second messengers.

Nature. 2017; 548: 543-548

• Kazlauskiene M.
• et al.

A cyclic oligonucleotide signaling pathway in type III CRISPR-Cas systems.

Science. 2017; 357: 605-609

• Klompe S.E.
• et al.

Transposon-encoded CRISPR–Cas systems direct RNA-guided DNA integration.

Nature. 2019; 571: 219-225