Why Nature Chose Phosphates

The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme

Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684 · see citing works

Reduction of Ribonucleotides

Thelander, L., & Reichard, P. A. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.001025 · Cited by 1,177 · see citing works

Enzyme-Catalyzed Phosphoryl Transfer Reactions

Knowles, J. R. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.004305 · Cited by 1,145 · see citing works

Evolution of the genetic apparatus

Orgel, L. E. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90393-8 · Cited by 996 · see citing works

Pseudo-rotation in the hydrolysis of phosphate esters

Westheimer, F. H. (1968) · Accounts of Chemical Research · doi:10.1021/ar50003a002 · Cited by 772 · see citing works

Effective Molarities for Intramolecular Reactions

Kirby, A. J. (1980) · Advances in physical organic chemistry · doi:10.1016/s0065-3160(08)60129-x · Cited by 577 · see citing works

The Intervening Sequence RNA of Tetrahymena Is an Enzyme

Zaug, A. J., & Cech, T. R. (1986) · Science · doi:10.1126/science.3941911 · Cited by 507 · see citing works

Coenzymes as fossils of an earlier metabolic state

White, H. B. (1976) · Journal of Molecular Evolution · doi:10.1007/bf01732468 · Cited by 493 · see citing works

24 Bovine Pancreatic Ribonuclease

Richards, F. M., & Wyckoff, H. W. (1971) · The Enzymes · doi:10.1016/s1874-6047(08)60384-4 · Cited by 441 · see citing works

The Electrostatic Influence of Substituents on the Dissociation Constants of Organic Acids. I

Kirkwood, J. G., & Westheimer, F. H. (1938) · The Journal of Chemical Physics · doi:10.1063/1.1750302 · Cited by 414 · see citing works

Biosynthesis of Diphosphopyridine Nucleotide

Preiss, J., & Handler, P. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64790-8 · Cited by 408 · see citing works

When is an intermediate not an intermediate? Enforced mechanisms of general acid-base, catalyzed, carbocation, carbanion, and ligand exchange reaction

Jencks, W. P. (1980) · Accounts of Chemical Research · doi:10.1021/ar50150a001 · Cited by 387 · see citing works

Progress in understanding the LDL receptor and HMG-CoA reductase, two membrane proteins that regulate the plasma cholesterol

Goldstein, J. L., & Brown, M. S. (1984) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)34418-7 · Cited by 383 · see citing works

Hydrolysis of Ethyl Silicate*

Aelion, R., Loebel, A., & Eirich, F. R. (1950) · Journal of the American Chemical Society · doi:10.1021/ja01168a090 · Cited by 340 · see citing works

The Reactivity of Phosphate Esters. Monoester Hydrolysis

Kirby, A. J., & Varvoglis, A. G. (1967) · Journal of the American Chemical Society · doi:10.1021/ja00978a044 · Cited by 326 · see citing works

Mechanisms of Nucleophilic Substitution in Phosphate Esters

Cox, J. R., & Ramsay, O. B. (1964) · Chemical Reviews · doi:10.1021/cr60230a001 · Cited by 312 · see citing works

Catalytic Activity of an RNA Molecule Prepared by Transcription in Vitro

Guerrier-Takada, C., & Altman, S. (1984) · Science · doi:10.1126/science.6199841 · Cited by 279 · see citing works

Specific interaction between the self-splicing RNA of Tetrahymena and its guanosine substrate: implications for biological catalysis by RNA

Bass, B., & Cech, T. R. (1984) · Nature · doi:10.1038/308820a0 · Cited by 260 · see citing works

ENZYMATIC SYNTHESIS OF PURINE NUCLEOTIDES

Kornberg, A., Lieberman, I., & Simms, E. S. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66049-1 · Cited by 252 · see citing works

Monomeric metaphosphates

Westheimer, F. H. (1981) · Chemical Reviews · doi:10.1021/cr00044a001 · Cited by 190 · see citing works

The Lanthanum Hydroxide Gel Promoted Hydrolysis of Phosphate Esters

Butcher, W. W., & Westheimer, F. H. (1955) · Journal of the American Chemical Society · doi:10.1021/ja01614a018 · Cited by 184 · see citing works

The biochemistry of arsenic

Knowles, F. C., & Benson, A. A. (1983) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(83)90168-8 · Cited by 183 · see citing works

The thermal degradation of nucleic acids

Eigner, J., Boedtker, H., & Michaels, G. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)91028-9 · Cited by 181 · see citing works

The Electrostatic Influence of Substituents on the Dissociation Constants of Organic Acids. II

Westheimer, F. H., & Kirkwood, J. G. (1938) · The Journal of Chemical Physics · doi:10.1063/1.1750303 · Cited by 171 · see citing works

On the importance of being ionized

Davis, B. D. (1958) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(58)90374-6 · Cited by 162 · see citing works

RNA as an Enzyme

Cech, T. R. (1986) · Scientific American · doi:10.1038/scientificamerican1186-64 · Cited by 160 · see citing works

BIOSYNTHESIS OF THE PURINES

Flaks, J. G., Erwin, M. J., & Buchanan, J. M. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70703-5 · Cited by 149 · see citing works

Hydration and dehydration of phosphoric acid derivatives: free energies of formation of the pentacoordinate intermediates for phosphate ester hydrolysis and of monomeric metaphosphate

Guthrie, J. P. (1977) · Journal of the American Chemical Society · doi:10.1021/ja00454a018 · Cited by 134 · see citing works

In vitro splicing of the ribosomal RNA precursor in nuclei of tetrahymena

Zaug, A. J., & Cech, T. R. (1980) · Cell · doi:10.1016/0092-8674(80)90507-3 · Cited by 115 · see citing works

Biosynthesis of the Purines

Hartman, S. C., & Buchanan, J. M. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64782-9 · Cited by 91 · see citing works

The Hydrolysis of Some Cyclic Esters of Sulfuric Acid

Kaiser, E. T., Panar, M., & Westheimer, F. H. (1963) · Journal of the American Chemical Society · doi:10.1021/ja00888a028 · Cited by 83 · see citing works

Stereochemistry of nucleophilic displacement on two phosphoric monoesters and a phosphoguanidine: the role of metaphosphate

Buchwald, S. L., Friedman, J. M., & Knowles, J. R. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00329a047 · Cited by 77 · see citing works

Biochemistry: Polyribonucleic acids as enzymes

Westheimer, F. H. (1986) · Nature · doi:10.1038/319534a0 · Cited by 75 · see citing works

The Enzymic Synthesis of Chorismic and Prephenic Acids from 3-Enolpyruvylshikimic Acid 5-Phosphate

Morell, H., Clark, M. J., Knowles, P. F., et al. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96321-0 · Cited by 73 · see citing works

The Hydrolysis of Mono- and Dibenzyl Phosphates

Kumamoto, J., & Westheimer, F. H. (1955) · Journal of the American Chemical Society · doi:10.1021/ja01614a047 · Cited by 67 · see citing works

Biotin. Its place in evolution

Visser, C. M., & Kellogg, R. M. (1978) · Journal of Molecular Evolution · doi:10.1007/bf01733892 · Cited by 66 · see citing works

The Electrostatic Influence of Substituents on the Dissociation Constants of Organic Acids. III

Westheimer, F. H., & Shookhoff, M. W. (1939) · Journal of the American Chemical Society · doi:10.1021/ja01872a004 · Cited by 64 · see citing works

The hydrolysis and polycondensation of tetra alkoxysilanes

Aelion, R., Loebel, A., & Eirich, F. R. (1950) · Recueil des Travaux Chimiques des Pays-Bas · doi:10.1002/recl.19500690109 · Cited by 61 · see citing works

Thermodynamic and kinetic properties of the metaphosphate anion, PO3-, in the gas phase

Henchman, M. J., Viggiano, A. A., Paulson, J. F., et al. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00291a081 · Cited by 56 · see citing works

The Tetrahymena intervening sequence ribonucleic acid enzyme is a phosphotransferase and an acid phosphatase

Zaug, A. J., & Cech, T. R. (1986) · Biochemistry · doi:10.1021/bi00364a002 · Cited by 54 · see citing works

The reactivity of phosphate esters: reactions of monoesters with nucleophiles. Nucleophilicity independent of basicity in a bimolecular substitution reaction

Kirby, A. J., & Varvoglis, A. G. (1968) · Journal of the Chemical Society B Physical Organic · doi:10.1039/j29680000135 · Cited by 49 · see citing works

The Hydrolysis of γ-Phenylpropyl Di- and Triphosphates1

Miller, D. L., & Westheimer, F. H. (1966) · Journal of the American Chemical Society · doi:10.1021/ja00959a034 · Cited by 49 · see citing works

Mechanism of inactivation of Escherichia coli ribonucleotide reductase by 2'-chloro-2'-deoxyuridine 5'-diphosphate: evidence for generation of a 2'-deoxy-3'-ketonucleotide via a net 1,2 hydrogen shift

Ator, M. A., & Stubbe, J. (1985) · Biochemistry · doi:10.1021/bi00346a029 · Cited by 43 · see citing works

[16] Chiral [16O, 17O, 18O] phosphoric monoesters as stereochemical probes of phosphotransferases

Buchwald, S. L., Hansen, D. E., Hassett, A., et al. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(82)87018-3 · Cited by 42 · see citing works

Aspects of biochemical catalysis

Altman, S. (1984) · Cell · doi:10.1016/0092-8674(84)90216-2 · Cited by 41 · see citing works

Direct observation of the monomeric metaphosphate anion

Harvan, D. J., Hass, J. R., Busch, K. L., et al. (1979) · Journal of the American Chemical Society · doi:10.1021/ja00518a050 · Cited by 32 · see citing works

Kinetics of the hydrolysis of arsenate(V) triesters

Baer, C. D., Edwards, J. O., & Rieger, P. H. (1981) · Inorganic Chemistry · doi:10.1021/ic50217a052 · Cited by 31 · see citing works

Bioorganic Chemistry and the Origin of Life

Visser, C. M., & Kellogg, R. M. (1978) · Journal of Molecular Evolution · doi:10.1007/bf01733891 · Cited by 28 · see citing works

The quest for free metaphosphate in solution: racemization at phosphorus in the transfer of the phospho group from phenyl phosphate to tert-butyl alcohol in acetonitrile

Friedman, J. M., & Knowles, J. R. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00307a061 · Cited by 28 · see citing works

Sterol Structure and Membrane Function

Bloch, K. (1981) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152818-8.50022-0 · Cited by 25 · see citing works

Stereoelectronic effects in the hydrolysis of methyl ethylene phosphate

Taira, K., Fanni, T., & Gorenstein, D. G. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00317a077 · Cited by 24 · see citing works

Three-phase test for reaction intermediates. Metaphosphates

REBEK, J. J., & Gaviña, F. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00839a062 · Cited by 22 · see citing works

Enthalpy of hydrolysis of simple phosphate diesters

Sturtevan, J. M., Gerlt, J. A., & Westheimer, F. H. (1973) · Journal of the American Chemical Society · doi:10.1021/ja00805a036 · Cited by 20 · see citing works

Amine catalysis in phosphoryl transfer from 2,4-dinitrophenyl phosphate in aprotic and protic solvents

Ramírez, F., & Marecek, J. F. (1979) · Tetrahedron · doi:10.1016/0040-4020(79)80019-8 · Cited by 19 · see citing works

Conant-Swan fragmentation reaction: stereochemistry of phosphate ester formation

Calvo, K. C. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00298a045 · Cited by 18 · see citing works

Monomeric metaphosphate anion: reaction with carbonyl groups

Satterthwait, A. C., & Westheimer, F. H. (1981) · Journal of the American Chemical Society · doi:10.1021/ja00395a030 · Cited by 15 · see citing works

Mechanism of the Conant-Swan fragmentation and the formation of monomeric metaphosphate ion

Calvo, K. C., & Westheimer, F. H. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00327a024 · Cited by 14 · see citing works

852. The existence of the P 1 P 1-diethyl pyrophosphate ion

Samuel, D., & Silver, B. L. (1961) · Journal of the Chemical Society (Resumed) · doi:10.1039/jr9610004321 · Cited by 8 · see citing works

Stereochemistry of the Conant-Swan fragmentation: the absence of a phenonium ion intermediate

Calvo, K. C., & Berg, J. M. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00327a023 · Cited by 8 · see citing works

Enol phosphates from the action of monomeric metaphosphate ion on ketones

Calvo, K. C., & Westheimer, F. H. (1983) · Journal of the American Chemical Society · doi:10.1021/ja00347a051 · Cited by 6 · see citing works

Calcium Signaling

Clapham, D. E. (2007) · Cell · doi:10.1016/j.cell.2007.11.028 · Cited by 4,175 · see citing works

P HOSPHORUS IN THE E NVIRONMENT : Natural Flows and Human Interferences

Smil, V. (2000) · Annual Review of Energy and the Environment · doi:10.1146/annurev.energy.25.1.53 · Cited by 1,165 · see citing works

Evidence for life on Earth before 3,800 million years ago

Mojzsis, S. J., Arrhenius, G., McKeegan, K. D., Harrison, T. M., Nutman, A. P., & Friend, C. R. L. (1996) · Nature · doi:10.1038/384055a0 · Cited by 1,370 · see citing works

Chemical space and biology

Dobson, C. M. (2004) · Nature · doi:10.1038/nature03192 · Cited by 1,003 · see citing works

Why Nature Chose Selenium

Reich, H. J., & Hondal, R. J. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00031 · Cited by 923 · see citing works

Anomeric-Oxygen Activation for Glycoside Synthesis: The Trichloroacetimidate Method

Schmidt, R. R., & Kinzy, W. (1994) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/s0065-2318(08)60150-x · Cited by 810 · see citing works

Global Phosphorus Scarcity and Full-Scale P-Recovery Techniques: A Review

Desmidt, E., Ghyselbrecht, K., Zhang, Y., Pinoy, L., der Bruggen, B. V., Verstraete, W., Rabaey, K., & Meesschaert, B. D. (2014) · Critical Reviews in Environmental Science and Technology · doi:10.1080/10643389.2013.866531 · Cited by 741 · see citing works

Template-directed synthesis of a genetic polymer in a model protocell

Mansy, S. S., Schrum, J. P., Krishnamurthy, M., Tobé, S., Treco, D. A., & Szostak, J. W. (2008) · Nature · doi:10.1038/nature07018 · Cited by 684 · see citing works

Synthesis of Phosphorus and Sulfur Heterocycles via Ring-Closing Olefin Metathesis

McReynolds, M. D., Dougherty, J. M., & Hanson, P. R. (2004) · Chemical Reviews · doi:10.1021/cr020109k · Cited by 631 · see citing works

Chemical etiology of nucleic acid structure

Eschenmoser, A. (1999) · Science · doi:10.1126/science.284.5423.2118 · Cited by 611 · see citing works

The mechanism of proton conduction in phosphoric acid

Vilčiauskas, L., Tuckerman, M. E., Bester, G., Paddison, S. J., & Kreuer, K. (2012) · Nature Chemistry · doi:10.1038/nchem.1329 · Cited by 585 · see citing works

Groundworks for an evolutionary biochemistry: The iron-sulphur world

Wächtershäuser, G. (1992) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(92)90022-x · Cited by 677 · see citing works

Toward the development of metal-based synthetic nucleases and peptidases: a rationale and progress report in applying the principles of coordination chemistry

Hegg, E. L., & Burstyn, J. N. (1998) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(98)00157-x · Cited by 565 · see citing works

GTPase mechanism of Gproteins from the 1.7-Å crystal structure of transducin α - GDP AIF−4

Sondek, J., Lambright, D. G., Noel, J. P., Hamm, H. E., & Sigler, P. B. (1994) · Nature · doi:10.1038/372276a0 · Cited by 559 · see citing works

Structure and Nuclease Activity of Simple Dinuclear Metal Complexes: Quantitative Dissection of the Role of Metal Ions

Williams, N. H., Takasaki, B. K., Wall, M., & Chin, J. (1999) · Accounts of Chemical Research · doi:10.1021/ar9500877 · Cited by 550 · see citing works

The Global Phosphorus Cycle

Ruttenberg, K. C. (2003) · Treatise on Geochemistry · doi:10.1016/b0-08-043751-6/08153-6 · Cited by 541 · see citing works

The Global Phosphorus Cycle: Past, Present, and Future

Filippelli, G. M. (2008) · Elements · doi:10.2113/gselements.4.2.89 · Cited by 591 · see citing works

Advances in theE → ZIsomerization of Alkenes Using Small Molecule Photocatalysts

Neveselý, T., Wienhold, M., Molloy, J. J., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00324 · Cited by 509 · see citing works

A Unidirectional DNA Walker That Moves Autonomously along a Track

Yin, P., Yan, H., Daniell, X. G., Turberfield, A. J., & Reif, J. H. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200460522 · Cited by 489 · see citing works

Developing artificial hydrolytic metalloenzymes by a unified mechanistic approach

Chin, J. (1991) · Accounts of Chemical Research · doi:10.1021/ar00005a004 · Cited by 471 · see citing works

Roles of Phosphate Solubilizing Microorganisms from Managing Soil Phosphorus Deficiency to Mediating Biogeochemical P Cycle

Tian, J., Ge, F., Zhang, D., et al. (2021) · Biology · doi:10.3390/biology10020158 · Cited by 450 · see citing works

DNA hydrolysis promoted by di- and multi-nuclear metal complexes

Liu, C., Wang, M., Zhang, T., & Sun, H. (2004) · Coordination Chemistry Reviews · doi:10.1016/j.cct.2003.11.002 · Cited by 442 · see citing works

Phosphinate Chemistry in the 21st Century: A Viable Alternative to the Use of Phosphorus Trichloride in Organophosphorus Synthesis.

Montchamp, J. (2013) · Accounts of Chemical Research · doi:10.1021/ar400071v · Cited by 439 · see citing works

Toxic metals and metalloids: Uptake, transport, detoxification, phytoremediation, and crop improvement for safer food

Zhao, F. J., Tang, Z., Song, J.-J., Huang, X., & Wang, P. (2021) · Molecular Plant · doi:10.1016/j.molp.2021.09.016 · Cited by 441 · see citing works

Why nature chose phosphate to modify proteins

Hunter, T. R. (2012) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2012.0013 · Cited by 430 · see citing works

The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate

Jurica, M. S., Mesecar, A., Heath, P. J., Shi, W., Nowak, T., & Stoddard, B. L. (1998) · Structure · doi:10.1016/s0969-2126(98)00021-5 · Cited by 426 · see citing works

Biological Phosphoryl-Transfer Reactions: Understanding Mechanism and Catalysis

Lassila, J. K., Zalatan, J. G., & Herschlag, D. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060409-092741 · Cited by 406 · see citing works

Why nature really chose phosphate

Kamerlin, S. C. L., Sharma, P. K., Prasad, R. B., & Warshel, A. (2013) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583512000157 · Cited by 403 · see citing works

M Stars as Targets for Terrestrial Exoplanet Searches And Biosignature Detection

Scalo, J., Kaltenegger, L., Segura, A., Fridlund, M. C., Ribas, I., Kulikov, Y. N., Grenfell, J. L., Rauer, H., Odert, P., Leitzinger, M., et al. (2007) · Astrobiology · doi:10.1089/ast.2006.0125 · Cited by 385 · see citing works

RAFT Aqueous Dispersion Polymerization Yields Poly(ethylene glycol)-Based Diblock Copolymer Nano-Objects with Predictable Single Phase Morphologies

Warren, N. J., Mykhaylyk, O. O., Mahmood, D., Ryan, A. J., & Armes, S. P. (2013) · Journal of the American Chemical Society · doi:10.1021/ja410593n · Cited by 384 · see citing works

Phosphorus: a limiting nutrient for humanity?

Elser, J. J. (2012) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2012.03.001 · Cited by 381 · see citing works

Parameterization of DFTB3/3OB for Sulfur and Phosphorus for Chemical and Biological Applications

Gaus, M., Lu, X., Elstner, M., & Cui, Q. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct401002w · Cited by 380 · see citing works

phoD Alkaline Phosphatase Gene Diversity in Soil

Ragot, S. A., Kertesz, M. A., & Bünemann, E. K. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.01823-15 · Cited by 371 · see citing works

Fluorinated Phosphonates: Synthesis and Biomedical Application

Romanenko, V. D., & Kukhar, V. P. (2006) · Chemical Reviews · doi:10.1021/cr051000q · Cited by 366 · see citing works

Phosphate sensing in higher plants

Abel, S., Ticconi, C. A., & Delatorre, C. A. (2002) · Physiologia Plantarum · doi:10.1034/j.1399-3054.2002.1150101.x · Cited by 364 · see citing works

Is there a common chemical model for life in the universe?

Benner, S. A., Ricardo, A., & Carrigan, M. A. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.10.003 · Cited by 363 · see citing works

Understanding the rates of certain enzyme-catalyzed reactions: Proton abstraction from carbon acids, acyl transfer reactions, and displacement reactions of phosphodiesters

Gerlt, J. A., & Gassman, P. G. (1993) · Biochemistry · doi:10.1021/bi00096a001 · Cited by 354 · see citing works

Mineral surfaces, geochemical complexities, and the origins of life

Hazen, R. M., & Sverjensky, D. A. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a002162 · Cited by 344 · see citing works

DNA And RNA Cleavage by Metal Complexes

Pratviel, G., Bernadou, J., & Meunier, B. (1998) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60027-6 · Cited by 349 · see citing works

The Origin and Early Evolution of Life: Prebiotic Chemistry, the Pre-RNA World, and Time

Lazcano, A., & Miller, S. L. (1996) · Cell · doi:10.1016/s0092-8674(00)81263-5 · Cited by 347 · see citing works

Assessment of gross and net mineralization rates of soil organic phosphorus – A review

Bünemann, E. K. (2015) · Soil Biology and Biochemistry · doi:10.1016/j.soilbio.2015.06.026 · Cited by 346 · see citing works

Human Perturbation of the Global Phosphorus Cycle: Changes and Consequences

Yuan, Z., Jiang, S., Hu, S., Liu, X., Hua, H., Liu, X., & Zhang, Y. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.7b03910 · Cited by 340 · see citing works

Root developmental responses to phosphorus nutrition

Liu, D. (2021) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13090 · Cited by 315 · see citing works

Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism

Walsh, C. T., Tu, B. P., & Tang, Y. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00510 · Cited by 302 · see citing works

Nature‐Inspired Environmental “Phosphorylation” Boosts Photocatalytic H2 Production over Carbon Nitride Nanosheets under Visible‐Light Irradiation

Liu, G., Wang, T., Zhang, H., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201505802 · Cited by 303 · see citing works

PKA: Lessons learned after twenty years

Taylor, S. S., Zhang, P., Steichen, J. M., Keshwani, M. M., & Kornev, A. P. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.007 · Cited by 298 · see citing works

Ring Strain Energies from ab Initio Calculations

Dudev, T., & Lim, C. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973895x · Cited by 288 · see citing works

The terpenoid theory of the origin of cellular life: the evolution of terpenoids to cholesterol

Ourisson, G., & Nakatani, Y. (1994) · Chemistry & Biology · doi:10.1016/1074-5521(94)90036-1 · Cited by 289 · see citing works

Inorganic Mimics of Ribonucleases and Ribozymes: From Random Cleavage to Sequence-Specific Chemistry to Catalytic Antisense Drugs

Trawick, B. N., Daniher, A. T., & Bashkin, J. K. (1998) · Chemical Reviews · doi:10.1021/cr960422k · Cited by 280 · see citing works

Mechanism and Catalysis of Nucleophilic Substitution in Phosphate Esters

Thatcher, R. J., & Kluger, R. (1989) · Advances in physical organic chemistry · doi:10.1016/s0065-3160(08)60019-2 · Cited by 277 · see citing works

Rethinking early Earth phosphorus geochemistry

Pasek, M. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708205105 · Cited by 275 · see citing works

Greenhouse gases emission from agricultural soil: A review

Chataut, G., Bhatta, B., Joshi, D., Subedi, K., & Kafle, K. (2023) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2023.100533 · Cited by 277 · see citing works

The first living systems: a bioenergetic perspective

Deamer, D. W. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.2.239-261.1997 · Cited by 305 · see citing works

The search for the chemistry of life's origin

Eschenmoser, A. (2007) · Tetrahedron · doi:10.1016/j.tet.2007.10.012 · Cited by 292 · see citing works

Abiotic production of sugar phosphates and uridine ribonucleoside in aqueous microdroplets

Nam, I., Lee, J. K., Nam, H. G., & Zare, R. N. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714896114 · Cited by 262 · see citing works

Protein-Tyrosine Phosphatases: Biological Function, Structural Characteristics, and Mechanism of Catalysis

Zhang, Z. (1998) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409239891204161 · Cited by 260 · see citing works

Rethinking glycolysis: on the biochemical logic of metabolic pathways

Bar‐Even, A., Flamholz, A. I., Noor, Ε., & Milo, R. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.971 · Cited by 258 · see citing works

Aqueous Corrosion of Phosphide Minerals from Iron Meteorites: A Highly Reactive Source of Prebiotic Phosphorus on the Surface of the Early Earth

Pasek, M. A., & Lauretta, D. S. (2005) · Astrobiology · doi:10.1089/ast.2005.5.515 · Cited by 251 · see citing works

Stewardship to tackle global phosphorus inefficiency: The case of Europe

Withers, P. J. A., van Dijk, K. C., Neset, T., Nesme, T., Oenema, O., Rubæk, G. H., Schoumans, O. F., Smit, A. B., & Pellerin, S. (2015) · AMBIO · doi:10.1007/s13280-014-0614-8 · Cited by 252 · see citing works

The pH of Enceladus’ ocean

Glein, C. R., Baross, J. A., & Waite, J. H. (2015) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2015.04.017 · Cited by 276 · see citing works

Chemistry of potentially prebiological natural products

Eschenmoser, A., & Loewenthal, E. (1992) · Chemical Society Reviews · doi:10.1039/cs9922100001 · Cited by 245 · see citing works

The chemical logic of a minimum protocell

Morowitz, H. J., Heinz, B., & Deamer, D. W. (1988) · Origins of life and evolution of the biosphere · doi:10.1007/bf01804674 · Cited by 239 · see citing works

Metabolite Concentration Changes in Humans After a Bout of Exercise: a Systematic Review of Exercise Metabolomics Studies

Schranner, D., Kastenmüller, G., Schönfelder, M., Römisch‐Margl, W., & Wackerhage, H. (2020) · Sports Medicine - Open · doi:10.1186/s40798-020-0238-4 · Cited by 250 · see citing works

DNA and RNA Sequence Determination Based on Phosphorothioate Chemistry

Gish, G. D., & Eckstein, F. (1988) · Science · doi:10.1126/science.2453926 · Cited by 232 · see citing works

Efficient Inorganic Deoxyribonucleases. Greater than 50-Million-Fold Rate Enhancement in Enzyme-Like DNA Cleavage

Sreedhara, A., Freed, J. D., & Cowan, J. A. (2000) · Journal of the American Chemical Society · doi:10.1021/ja994411v · Cited by 225 · see citing works

Peptide nucleic acids rather than RNA may have been the first genetic molecule

Nelson, K. E., Levy, M., & Miller, S. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.3868 · Cited by 269 · see citing works

Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective

Chowdhury, D. (2013) · Physics Reports · doi:10.1016/j.physrep.2013.03.005 · Cited by 218 · see citing works

The molecular basis of phosphate discrimination in arsenate-rich environments

Elias, M. H., Wellner, A., Goldin-Azulay, K., et al. (2012) · Nature · doi:10.1038/nature11517 · Cited by 219 · see citing works

The Origin and Nature of Life on Earth: The Emergence of the Fourth Geosphere

Smith, E., & Morowitz, H. J. (2016) · doi:10.1017/cbo9781316348772 · Cited by 215 · see citing works

Poly(phosphoester)s: A new platform for degradable polymers

Steinbach, T., & Wurm, F. R. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201500147 · Cited by 219 · see citing works

Ribozyme speed limits

EMILSSON, G. M., NAKAMURA, S., ROTH, A., & BREAKER, R. R. (2003) · RNA · doi:10.1261/rna.5680603 · Cited by 216 · see citing works

Genetics first or metabolism first? The formamide clue

Saladino, R., Botta, G., Pino, S., Costanzo, G., & Di Mauro, E. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35066a · Cited by 215 · see citing works

Recent Trends in Nucleotide Synthesis

Roy, B., Depaix, A., Périgaud, C., et al. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00174 · Cited by 212 · see citing works

The Origin of RNA and “My Grandfather’s Axe”

Hud, N. V., Cafferty, B. J., Krishnamurthy, R., & Williams, L. D. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.03.012 · Cited by 210 · see citing works

Emerging Enzymes for ATP Regeneration in Biocatalytic Processes

Andexer, J. N., & Richter, M. (2015) · ChemBioChem · doi:10.1002/cbic.201402550 · Cited by 205 · see citing works

The Importance of Water for Life

Westall, F., & Brack, A. (2018) · Space Science Reviews · doi:10.1007/s11214-018-0476-7 · Cited by 208 · see citing works

From OCR and ECAR to energy: Perspectives on the design and interpretation of bioenergetics studies

Schmidt, C. A., Fisher‐Wellman, K. H., & Neufer, P. D. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101140 · Cited by 197 · see citing works

Arsenic uptake and toxicity in plants: integrating mycorrhizal influences

Smith, S. E., Christophersen, H. M., Pope, S., & SMITH, F. A. (2009) · Plant and Soil · doi:10.1007/s11104-009-0089-8 · Cited by 198 · see citing works

Silicon increases the phosphorus availability of Arctic soils

Schaller, J., Faucherre, S., Joß, H., Obst, M., Goeckede, M., Planer‐Friedrich, B., Peiffer, S., Gilfedder, B. S., & Elberling, B. (2019) · Scientific Reports · doi:10.1038/s41598-018-37104-6 · Cited by 201 · see citing works

Protein kinases and protein phosphatases in prokaryotes: a genomic perspective

Kennelly, P. J. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb10978.x · Cited by 197 · see citing works

DNA-Cation Interactions

Egli, M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00116-3 · Cited by 196 · see citing works

The use of phosphate bioisosteres in medicinal chemistry and chemical biology

Elliott, T. S., Slowey, A., Ye, Y., & Conway, S. J. (2012) · MedChemComm · doi:10.1039/c2md20079a · Cited by 196 · see citing works

Bacterial metabolism of environmental arsenic—mechanisms and biotechnological applications

Kruger, M. C., Bertin, P. N., Heipieper, H. J., & Arsène‐Ploetze, F. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-4838-5 · Cited by 193 · see citing works

Chemie von a‐Aminonitrilen. Aldomerisierung von Glycolaldehyd‐phosphat zu racemischen Hexose‐2,4,6‐triphosphaten und (in Gegenwart von Formaldehyd) racemischen Pentose‐2,4‐diphosphaten: <i>rac</i>‐Allose‐2,4,6‐triphosphat und <i>rac</i>‐Ribose‐2,4‐diphosphat sind die Reaktionshauptprodukte

Müller, D., Pitsch, S., Kittaka, A., Wagner, E., Wintner, C. E., Eschenmoser, A., & Ohlofjgewidmet, G. (1990) · Helvetica Chimica Acta · doi:10.1002/hlca.19900730526 · Cited by 216 · see citing works

A carbonate-rich lake solution to the phosphate problem of the origin of life

Toner, J. D., & Catling, D. C. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1916109117 · Cited by 201 · see citing works

Etiology of Potentially Primordial Biomolecular Structures: From Vitamin B12to the Nucleic Acids and an Inquiry into the Chemistry of Life’s Origin: A Retrospective

Eschenmoser, A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201103672 · Cited by 192 · see citing works

Main-chain poly(phosphoester)s: History, syntheses, degradation, bio-and flame-retardant applications

Bauer, K. N., Tee, H. T., Velencoso, M. M., & Wurm, F. R. (2017) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2017.05.004 · Cited by 189 · see citing works

The energy landscape of adenylate kinase during catalysis

Kerns, S. J., Agafonov, R. V., Cho, Y.-J., Pontiggia, F., Otten, R., Pachov, D. V., Kutter, S., Phung, L. A., Murphy, P. N., Thai, V., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2941 · Cited by 190 · see citing works

Phosphorus in prebiotic chemistry

Schwartz, A. W. (2006) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2006.1901 · Cited by 207 · see citing works

Arsenate Replacing Phosphate: Alternative Life Chemistries and Ion Promiscuity

Tawfik, D. S., & Viola, R. E. (2011) · Biochemistry · doi:10.1021/bi200002a · Cited by 184 · see citing works

Adenosine-Phosphate-Fueled, Temporally Programmed Supramolecular Polymers with Multiple Transient States

Dhiman, S., Jain, A., Kumar, M., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b07469 · Cited by 184 · see citing works

Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation

Kennelly, P. J., & Potts, M. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.16.4759-4764.1996 · Cited by 183 · see citing works

Progress in artificial metallonucleases

Mancin, F., Scrimin, P., & Tecilla, P. (2012) · Chemical Communications · doi:10.1039/c2cc30952a · Cited by 181 · see citing works

Prodrugs of Phosphonates and Phosphates: Crossing the Membrane Barrier

Wiemer, A. J., & Wiemer, D. F. (2014) · Topics in current chemistry · doi:10.1007/128_2014_561 · Cited by 183 · see citing works

Why did Nature select phosphate for its dominant roles in biology?

Bowler, M. W., Cliff, M. J., Waltho, J. P., & Blackburn, G. M. (2010) · New Journal of Chemistry · doi:10.1039/b9nj00718k · Cited by 178 · see citing works

Vesicular-Arbuscular Mycorrhizae as Modifiers of Soil Fertility

Barea, J. M. (1991) · Advances in soil science · doi:10.1007/978-1-4612-3030-4_1 · Cited by 178 · see citing works

Biogeochemistry

Schlesinger, W. H. (2013) · Oxford Bibliographies in Ecology · doi:10.1093/obo/9780199830060-0111 · Cited by 175 · see citing works

Stimulus-cleavable chemistry in the field of controlled drug delivery

Xue, Y., Bai, H., Peng, B., Fang, B., Baell, J. B., Li, L., Huang, W., & Voelcker, N. H. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01061h · Cited by 176 · see citing works

Bioenergetics and Life’s Origins

Deamer, D., & Weber, A. L. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004929 · Cited by 165 · see citing works

Are polyphosphates or phosphate esters prebiotic reagents?

Keefe, A., & Miller, S. (1995) · Journal of Molecular Evolution · doi:10.1007/bf00173147 · Cited by 168 · see citing works

Influence of Varying Calcium Levels on the Utilization of Calcium Meta- and Pyrophosphate in Chick Diets

Damron, B. L., & Harms, R. H. (1971) · Poultry Science · doi:10.3382/ps.0501423 · Cited by 2 · see citing works

Structure of pyrophosphate 2ZnO·P2O5–2Na2O·P2O5 glasses according to molecular dynamics simulation

Boiko, G. G., Andreev, N. S., & Parkachev, A. V. (1998) · Journal of Non-Crystalline Solids · doi:10.1016/s0022-3093(98)00693-0 · Cited by 30 · see citing works

Studies on the Curd Tension and Salt Balance in Abnormal Milk (Part II)

MIYABE, T., & 大平, 伸. (1964) · Eiyo to shokuryo/Eiyo To Shokuryo · doi:10.4327/jsnfs1949.17.225

Mechanism of polyphosphate gel formation in the Na2OAl2O3P2O5 system

Montagne, L., Palavit, G., & Draoui, M. (1993) · Journal of Non-Crystalline Solids · doi:10.1016/0022-3093(93)91315-t · Cited by 32 · see citing works

Polyphosphate Formation from Pyrophosphate in Intact Cells of a Photosynthetic Bacterium, Rhodospirillum rubrum

Oh, D.-C., & Lee, H.-S. (1987) · Plant and Cell Physiology · doi:10.1093/oxfordjournals.pcp.a077320 · Cited by 4 · see citing works