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Latest revision as of 02:27, 17 February 2020

Editor-In-Chief: Henry A. Hoff

Overview

Inside a cell, phosphate may be structural to a nucleic acid such as DNA and RNA or phospholipid. Outside the cell, phosphate may be dissolved in extracellular fluid (ECF) or form structures such as bone and teeth. Bringing phosphate in any form into the cell from a phosphate containing structure or for such a structure and when needed transporting phosphate out of the cell perhaps to a structure is a necessary activity of phosphate homeostasis for that cell.

Introduction

Inorganic phosphate (P_i) (structural phosphate) behaves as a serine phosphate and is not the same as the enzyme-bound phosphate (catalytic phosphate) derived from ATP during a catalytic reaction.^[1] The catalytic phosphate in a nucleotide is usually the phosphate farthest from the nucleoside. The structural phosphate becomes the hydrolyzed nucleotide after the catalysis that associates with the binding of the polymer. The structural phosphate is a part of each polymer whether it is a microfilament, microtubule, phospholipid, or nucleic acid. Inorganic phosphates such as P_i and PP_i can be precipitated with divalent cations like Ca²⁺, Mg²⁺, or others, e.g. Mn²⁺, to form a variety of tissue and mineral composites: cartilage, teeth, and bone. These in turn eventually become localized to the natural environment and form phosphorites.

Catalytic phosphate

Inorganic phosphate (P_i) (structural phosphate) behaves as a serine phosphate and is not the same as the enzyme-bound phosphate (catalytic phosphate) derived from ATP during a lyase reaction of EC 4.1.3.8.^[1] Evidence indicates that EC 4.1.3.8 contains one structural phosphate for each catalytic phosphate, which does not affect its catalytic activity.^[1] The γ phosphate of ATP is the catalytic phosphate. EC 4.1.3.8 ATP citrate lyase contains acid-labile, catalytic phosphate after the enzyme is reacted with ATP and Mg²⁺, whereas the structural phosphate is acid-stable, base-labile.^[2] There are 2 mol of acid-labile catalytic phosphate and 2 mol of base-labile structural phosphate per tetramer. A pH 7.5 buffer associated with EC 4.1.3.8 contains concentrations of ADP, P_i, and free Mg²⁺ similar to those found in vivo.^[2] Glucagon induces an incorporation of acid-stable phosphate into ATP citrate lyase without a concomitant change in enzyme activity.^[2]

Intracellular structural phosphate

In the mathematical modeling of cell growth and phosphatase biosynthesis it is necessary to determine the intracellular concentration of structural phosphate.^[3]

Nucleotides

Analysis of the phosphate moiety present in mononucleotides (NMP) can allow the identification of structural phosphate binding motifs.^[4]

When nucleotide hydrolysis is coupled to the polymerization process, the two ends of the polymer behave differently, and the critical concentration required for assembly at one end is different from that required for the opposite end. However, NTP hydrolysis is usually associated but not directly coupled with polymerization. When there are NTP-bound subunits at the ends, the polymer is stable and continues to grow slowly. When at the polymer ends there are subunits containing NDP, the polymer is in a shrinking phase, depolymerizes rapidly and completely, and much faster at lower mer concentrations.

Microfilaments

During the assembly of actin into microfilaments, actin-ATP becomes actin ADP upon polymerization.

Microtubules

P_i, BeF₃ or AIF₄, structural phosphate analogs, have a stabilizing effect on microtubules containing GDP tubulin.^[5] The structural phosphate of microtubules is the GDP in the interior of the polymer.

Phospholipid

Phospholipids are a major component of the plasma membrane and organelle membranes. In normal cell plasma membranes, phospholipids are asymmetrically distributed: phosphatidylcholine (PC) and sphingomyelin (SM) predominantly in the exoplasmic leaflet and phosphatidylserine (PS) and phosphatidylethanolamine (PE) in the cytoplasmic leaflet. All phospholipids in eukaryotic plasma membranes undergo a slow passive transbilayer movement.^[6] Half-times of redistribution are 3.6 min for PS.^[6] Both PC and SM have higher diffusion rates probably indicative of endocytosis.

A typical molecule of PC, SM, PS, or PE contains one monophosphate group. The entire PC molecule contains glycerol, P_i, choline and fatty acids for 760 Da^[7] with an average diameter of ~2.16 nm. However, the fatty acids extend between the bilayers of the cell membrane. The head of a PC molecule is 314 Da^[8], with an average diameter of ~1.62 nm. The head contains the structural monophosphate. For an cell of 10 µm diameter, there may be up to ~7.6 x 10⁷ molecules of PC in the exoplasmic leaflet, if the leaflet were entirely composed of PC.

The sphingomyelins (SMs) are found largely in the brain and other nervous tissue. They contain phosphocholine or phosphoethanolamine as their polar head group. The head group containing phosphocholine is 285 Da^[9], with an average diameter of ~1.56 nm. SMs can have fatty acid tails, such as in sphingosine phosphorylcholine 465 Da^[10] (one tail) or TNPAL-sphingomyelin 874 Da^[11] (two tails). Although the head size of the SMs is comparable to that of PC, the number of phosphates in the exoplasmic leaflet would be at ~8.2 x 10⁷, if composed entirely of SM.

In the cytoplasmic leaflet are PS and PE. The head of PS is 385 Da^[12], with an average diameter of ~1.72 nm. As the cell membrane averages about 7 nm in thickness, the cytoplasmic leaflet can have ~6.7 x 10⁷ molecules of PS, if totally composed of PS. The head of PE is 271 Da^[13], with an average diameter of ~1.54 nm. The cytoplasmic leaflet would have ~8.4 x 10⁷ molecules of PE, if totally composed of PE.

If half and half, the number of phosphates in the cytoplasmic leaflet would be ~7.6 x 10⁷. Half and half in the exoplasmic leaflet would yield ~7.9 x 10⁷ molecules of phosphate. The entire cell membrane could have up to ~1.6 x 10⁸ molecules of phosphate.

Nucleic acid

Phosphate is a component of DNA and RNA. Most of the structural phosphate in nucleic acids is in the phospho-diester linkage.^[14]

Ribonucleic acid (RNA)

The variety and type of RNA is extensive. Each has to be transcribed from the applicable portion of DNA in the euchromatin. The unfolded structure of euchromatin allows gene regulatory proteins and RNA polymerase (RNAP) complexes to bind to the DNA sequence, which can then initiate the transcription process. Control of the process of gene transcription affects patterns of gene expression and thereby allows a cell to adapt to a changing environment, perform specialized roles within an organism, and maintain basic metabolic processes necessary for survival. RNAP can initiate transcription at specific DNA sequences known as promoters. It then produces an RNA chain which is complementary to the template DNA strand. The process of adding nucleotides to the RNA strand is known as elongation.

RNAs involved in protein synthesis
Type	Abbr.	Function	Distribution	Ref.
Messenger RNA	mRNA	Codes for protein	All cells
Ribosomal RNA	rRNA	Translation	All cells
Signal recognition particle RNA	7SL RNA or SRP RNA	Membrane integration / mRNA tagging for export	All organisms	^[15]
Transfer RNA	tRNA	Translation	All cells
Transfer-messenger RNA	tmRNA	Rescuing stalled ribosomes Terminating translation	Bacteria	^[16]

RNAs involved in post-transcriptional modification or DNA replication
Type	Abbr.	Function	Distribution	Ref.
Small nuclear RNA	snRNA	Splicing and other functions	Eukaryotes and archaea	^[17]
Small nucleolar RNA	snoRNA	Nucleotide modification of RNAs RNA editing	Eukaryotes and archaea	^[18]
SmY RNA	SmY	mRNA trans-splicing	Nematodes	^[19]
Small Cajal body-specific RNA	scaRNA	Type of snoRNA; Nucleotide modification of RNAs
Guide RNA	gRNA	mRNA nucleotide modification / RNA editing	Kinetoplastid mitochondria	^[20]
Ribonuclease P	RNase P	tRNA maturation	All organisms	^[21]
Ribonuclease MRP	RNase MRP	rRNA maturation, DNA replication	Eukaryotes	^[22]
Y RNA		RNA processing, DNA replication	Animals	^[23]
Telomerase RNA		Telomere synthesis	Most eukaryotes	^[24]
Ribozyme		Catalysis	All cells
Transposon		Self-propagating	All cells

Regulatory RNAs
Type	Abbr.	Function	Distribution	Ref.
Antisense RNA	aRNA	Transcriptional attenuation / mRNA degradation / mRNA stabilisation / Translation block Gene regulation	All organisms	^[25]^[26]
Cis-natural antisense transcript		Gene regulation
CRISPR RNA	crRNA	Resistance to parasites, probably by targeting their DNA	Bacteria and archaea	^[27]
Long noncoding RNA	Long ncRNA	Various	Eukaryotes
MicroRNA	miRNA	Gene regulation	Most eukaryotes	^[28]
Piwi-interacting RNA	piRNA	Transposon defense Gene regulation	Animal germline cells	^[29]^[30]
Small interfering RNA	siRNA	Gene regulation	Most eukaryotes	^[31]
Trans-acting siRNA	tasiRNA	Gene regulation	Land plants	^[32]
Repeat associated siRNA	rasiRNA	Type of piRNA; transposon defense	Drosophila	^[33]

Enstructuring P_i into any RNA is usually not accomplished by reacting directly with ribose for RNA, deoxyribose present in DNA, purines, or pyrimidines. Although DNA records the sequence of nucleobases that are connected by ribose to P_i, the transcription process chosen by probably all life on Earth requires triphosphate nucleotides (NTPs).

For example, consider making a mRNA for a particular protein from the point of view of phosphate enstructuring. As of 2008 dystrophin has the longest gene known, at locus Xp21.2. The primary transcript measures 2.4 megabases (thus the gene comprises 0.008% of the human genome), and takes 16 hours to transcribe. The 79 exons^[34] code for a protein of over 3500 amino acid (aa) residues. It is human GeneID: 1756.^[35] Isoform Dp427c has 3677 aa^[36] which are specified by 3677 codons of 3 nucleotides each. That's 11,031 NMPs with one P_i each.

But the gene portion that is transcribed also contains a 5' cap requiring one GTP, a 5' UTR, 78 introns, and a 3' UTR or as mentioned 2.4 Mb of one P_i each. In this excess generation of RNA dystrophin is not unique. More than 95% of the enstructured phosphate for RNA synthesized by RNA polymerase II never reaches the cytoplasm. The main reason for this is due to the removal of introns which account for 80% of the total bases.^[37]

Per the apparently available phosphate reserve in a cell or intracellular phosphate of about 10^-3 P_i (1 molecule of P_i per 1000 other molecules, such as water) at any particular location and a rate of about 42 NTPs per second to transcribe this mRNA, some form of intranuclear transport other than diffusion is needed. While the number of transcription units varies at any given moment, should per transcription factories there be ~64,000 polymerase II active transcription units operating at about 42 NTPs per second, there would need to be a way to supply a total phosphate of ~2,700,000 NTPs per second to all transcription units in parallel.

With respect to phosphate reserves each ATP is recycled about once every minute on average. This may also be true for CTP, GTP, and UTP. That is ~0.07 recycled NTPs per second are available to transcribe on average.

Using the information derived regarding signal transduction for a water molecule of speed 15 µms^-1, if a nucleus of 5 µm diameter contains ~64,000 transcription units uniformly distributed throughout (a volume with ~120 nm diameter for each unit), it would take about 40 seconds for a GTP molecule to interact with one unit with ten molecules in each unit volume. The GTP molecule would have a speed of ~2800 nms^-1. But to get to 24 ms between interactions would take ~17,000 NTP molecules in a volume of ~120 nm diameter. That is ~68 µg/ml GTP. As the total number of normally available intracellular phosphate molecules, if uniformly distributed throughout the cell, would be ~33,000 molecules of all phosphate compunds within each ~120 nm diameter volume, diffusion may be sufficient. Pulling in additional phosphate from extracellular fluid would help to increase the amount of available phosphate, probably enough to make 42 NTPs per second reasonable.

Subtracting the estimated number of phosphates in the genome DNA yields ~21,000 phosphate molecules for all other purposes. The amount of phosphate in the cell membrane would reduce the available phosphate to ~20,000 molecules. But, if half the available phosphate is already tied up in RNA or other structures, then transport across the cell membrane and diffusion throughout the cell is mandatory.

Alternatively, if the actual translational speed of a water molecule is closer to 75 µms^-1, the needed phosphate is in ~3,400 NTPs. However, for transcription of a mRNA roughly equal amounts of ATP, CTP, GTP, and UTP need to be present in each ~120 nm diameter volume. That's ~13,600 NTPs with 3 phosphates each for ~41,000 phosphates. To have the needed concentration in the nucleus, the entire cell needs to be at the same level of phosphate in the cytosol. The total phosphate uniformly distributed by diffusion throughout the cytosol is ~24 x 10⁹: ~6.0 x 10⁹ each of ATP, CTP, GTP, and UTP.

Average phosphate content of human RNAs
Abbr.	GeneID	Number of basepairs	Accumulative average phosphates
mRNA	1	1488	1488
mRNA	2	4425	2956.5
mRNA	9	873	2262
mRNA	10	873	1914.8
mRNA	12	1272	1786.2
ncRNA	245	2768	2768
ncRNA	303	1343	2055.5
ncRNA	305	1350	1820.3
ncRNA	1057	985	1611.5
ncRNA	1197	1812	1651.6
ncRNA	1587 variant 1	2642	1816.7
ncRNA	1587 variant 2	2396	1988.4
ncRNA	1587 variant 3	2491	1973.4
miscRNA (ncRNA)	711	2264	2264
miscRNA (ncRNA)	3262	1198	1731
miscRNA (ncRNA)	5820	1918	1793.3
miscRNA (Long? ncRNA)	7503	19271	6162.8
miscRNA (ncRNA)	8123	3373	5604.8
miscRNA (ncRNA)	8420	939	4827.2
rRNA	4549	953	953
rRNA	4550	1558	1255.5
rRNA (ribosome component)	6052	---	---
rRNA (ribosome component)	6053	---	---
rRNA (ribosome component)	6054	---	---
rRNA (ribosome component)	6055	---	---
rRNA (ribosome component)	6056	---	---
rRNA	100008587	156	889
rRNA	100008588	1869	1134
rRNA	100008589	5070	1921.2
SRP RNA (miscRNA)	6029	299	299
SRP RNA (scRNA)	378706	299	299
tRNA	4511 (mitochondrial)	65	65
tRNA	4553 (mitochondrial)	68	66.5
tRNA	4555 (mitochondrial)	67	66.7
tRNA	4556 (mitochondrial)	68	67
tRNA	4558 (mitochondrial)	70	67.6
snRNA (spliceosome)	6060	164	164
snRNA (spliceosome)	6066	188	176
snRNA (ncRNA)	125050	332	228
snRNA (spliceosome)	100151683	130	203.5
snRNA (spliceosome)	100151684	125	187.8
snoRNA (ncRNA)	6043	135	135
snoRNA (ncRNA)	6044	154	144.5
snoRNA (ncRNA)	6079	148	145.7
snoRNA (ncRNA)	6080	207	161
snoRNA (ncRNA)	6081	205	169.8
RNase P (miscRNA)	85495	341	341
RNase MRP (miscRNA)	6023	265	265
Y RNA (scRNA)	6084	113	113
Y RNA (scRNA)	6085	102	107.5
Y RNA (scRNA)	6086	96	103.7
Y RNA (scRNA)	6090	84	98.8
Telomerase RNA (miscRNA)	7012	451	451
Ribozyme (ncRNA	54677	1264	1264
Alu sequence (Transposon)	?	~300	~300
aRNA (miscRNA)	6315	1472	1472
aRNA (miscRNA)	8475	1286	1379
aRNA (miscRNA)	9383	37027	13261.7
aRNA (miscRNA)	10108	---	13261.7
aRNA (miscRNA)	10737 variant 1	1357	13261.7
aRNA (miscRNA)	10737 variant 2	1115	8451.4
aRNA (miscRNA)	10740	5125	7897
Long ncRNA	7503	19271	19271
Long ncRNA	9383	37027	28149
Long ncRNA	10984	59461	38586.3
miRNA	406991	71	71
miRNA	406952	83	77
miRNA	406902	109	87.7
miRNA	407043	109	93
miRNA	407006	109	96.2
piRNA	?	29-30	29-30
siRNA	?	20-25	20-25

In the table above those RNAs with a GeneID less than 30000 are found by searching among the human GeneIDs up to 30000. A total of 230 RNA genes, including variants, occur prior to GeneID 30000. There are as of July 22, 2009, 15827 human genes of all types, including variants and pseudogenes, at and before GeneID: 30000. Of the pseudogenes, 521 are inactive. Many of the active pseudogenes are RNA transcribing genes. Some 611 of these GeneIDs are also not transcribed genes. Some 14,695 are active and transcribed.

Using a likely cellular phosphate budget in a human adult as a guide, an average cell could be operating ~28,800 transcription units. For a lateral speed of 37 µms^-1 of a water molecule, an average cell could operate ~14,400 transcription units by diffusion.

For an average cell of "default" cell type running the 14,695 active and transcribeable genes including variants, 14,464 mRNAs and 230 other assorted RNAs are being transcribed. As the above table lists the number of phosphates per RNA on average, an RNA transcription budget can be estimated, assuming each is halfway through transcription.

Estimated phosphate budget for RNAs
Abbr.	Number of RNAs	Number of structural phosphates	Accumulative phosphates
mRNA	14,464	~12.9 x 10⁶	~12.9 x 10⁶
snoRNA	77	~6500	~12.9 x 10⁶
tRNA	59	~2000	~12.9 x 10⁶
miscRNA	39	~94,000	~13.0 x 10⁶
ncRNA	21	~21,000	~13.0 x 10⁶
RNA	11	~10,000	~13.1 x 10⁶
aRNA	7	~28,000	~13.1 x 10⁶
rRNA	6	~5800	~13.1 x 10⁶
Y RNA	4	~200	~13.1 x 10⁶
SRP	2	~300	~13.1 x 10⁶
snRNA	2	~200	~13.1 x 10⁶
Long ncRNA	2	~39,000	~13.1 x 10⁶

Deoxyribonucleic acid (DNA)

The entire human genome has ~3.4 Gb in its DNA, with one P_i each. That is ~3.4 x 10⁹ P_i tied up in DNA per strand, ~6.8 x 10⁹ P_i total structural phosphate in each nucleus. With ~19 x 10⁹ P_i per cell in some form, that leaves ~12 x 10⁹ P_i per cell for all other functions and forms.

Mitochondria have their own genetic material, and the machinery to manufacture their own RNAs and proteins. A published human mitochondrial DNA sequence revealed 16,569 base pairs encoding 37 total genes, 24 tRNA and rRNA genes and 13 peptide genes.^[38] The mitochondrial matrix contains several (2-10) copies of the mitochondrial DNA genome. Up to ~2000 mitochondria can occur per cell. This can enstructure up to ~3.3 x 10⁸ phosphates.

Cartilage

Mineralization in the extracellular matrix starting with hydroxyapatite deposition into a collagenous scaffolding of cartilage, cementum, dentin and bone is initially regulated locally by calcium, orthophosphate, and pyrophosphate ion concentrations.

Although cuboid calcium phosphate crystals are absent in young articular cartilage, they are sometimes present in old normal articular cartilage occasionally adjacent to larger areas of pyrophosphate crystals.^[39]

Endochondrial ossification of cartilage development ultimately leads to mineralization of the extracellular matrix.^[40] Metabolism of Ca²⁺ and P_i by cartilage growth plate chondrocytes, involved in matrix vesicle formation, clearly are integral features of endochondrial calcification.^[40] This calcification is apparently due to the diffusion barrier and avascularity progressing from the zone of proliferation to the zone of hypertrophy of the cartilage growth plate chondrocytes environment.^[40]

Teeth

Hydroxyapatite, which is a crystalline calcium phosphate is the primary mineral of enamel.^[41]

By weight, seventy percent of dentin consists of the mineral, hydroxylapatite, twenty percent is organic material, and ten percent is water.^[42]

Cementum is a specialized bony substance covering the root of a tooth, composed of approximately 45% inorganic material (mainly hydroxyapatite), 33% organic material (mainly collagen) and 22% water.

Bone

During bone resorption high levels of phosphate are released into the ECF as osteoclasts tunnel into mineralized bone, breaking it down and releasing phosphate, that results in a transfer of phosphate from bone fluid to the blood. During childhood, bone formation exceeds resorption, but as the aging process occurs, resorption exceeds formation.

Transphosphorylation between nucleotides and hydroxyapatite (HA) results in a pyrophosphate on HA that is distinctive from pyrophosphate absorbed onto HA from solution. This may be due to a different orientation of the pyrophosphate on the surface depending on the origin of the pyrophosphate.^[43]

Sedimentary phosphorites

Phosphogenesis under palaeoceanographic conditions that were different from modern phosphorite depositional systems occurred across a broad range of palaeoenvironments in the shallow and broad epicontinental Phosphoria Sea.^[44] These conditions were revealed by oxygen isotope analyses of the structural phosphate in sedimentary phosphorites of the Upper Permian Phosphoria Formation.^[44]

Acknowledgements

The content on this page was first contributed by: Henry A. Hoff.

Initial content for this page in some instances came from Wikipedia.

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↑ "Entrez Protein - dystrophin Dp427c isoform [Homo spiens]".
↑ Jackson DA, Pombo A, Iborra F (2000). "The balance sheet for transcription: an analysis of nuclear RNA metabolism in mammalian cells". FASEB J. 14 (2): 242–54. PMID 10657981.
↑ Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR; et al. (1981). "Sequence and organization of the human mitochondrial genome". Nature. 410 (5806): 141. doi:10.1038/290457a0. Unknown parameter |month= ignored (help)
↑ Ali SY, Griffiths S (1983). "Formation of calcium phosphate crystals in normal and osteoarthritic cartilage". Ann Rheum Dis. 42 (Suppl 1): 45–8. PMID 6615026. Unknown parameter |month= ignored (help)
↑ ^40.0 ^40.1 ^40.2 Wuthier RE (1993). "Involvement of cellular metabolism of calcium and phosphate in calcification of avian growth plate cartilage". J Nutr. 123 (2 Suppl): 301–9. PMID 8429379. Unknown parameter |month= ignored (help)
↑ Johnson, Clarke (1998). "Biology of the Human Dentition".
↑ Cate, A.R. Ten. (1998). Oral Histology: development, structure, and function (5th ed.). pp. 150–5. ISBN 0-8151-2952-1.
↑ Taves DR, Reedy RC (1969). "A structural basis for the transphosphorylation of nucleotides with hydroxyapatite". Calcified Tissue International. 3 (1): 284–92. doi:10.1007/BF02058670. Unknown parameter |month= ignored (help)
↑ ^44.0 ^44.1 Hiatt EE, Budd DA (2001). "Sedimentary phosphate formation in warm shallow waters: new insights into the palaeoceanography of the Permian Phosphoria Sea from analysis of phosphate oxygen isotopes". Sedimentary Geol. 145 (1–2): 119–33. doi:10.1016/S0037-0738(01)00127-0. Unknown parameter |month= ignored (help)

Template:WH Template:WS

[Linn-1] 1.0 ^1.1 ^1.2 Linn TC, Srere PA (1979). "Identification of ATP citrate lyase as a phosphoprotein". J Biol Chem. 254 (5): 1691–8. PMID 762167. Unknown parameter |month= ignored (help)

[Janski-2] 2.0 ^2.1 ^2.2 Janski AM, Srere PA, Cornell NW, Veech RL (1979). "Phosphorylation of ATP Citrate Lyase in Response to Glucagon". J Biol Chem. 254 (19): 9365–8. PMID 489538. Unknown parameter |month= ignored (help)

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[Babor-4] Babor M, Soboleva V, Edelman M (2002). "Conserved Positions for Ribose Recognition: Importance of Water Bridging Interactions Among ATP, ADP and FAD-protein Complexes". J Mol Biol. 323 (3): 523–32. doi:10.1016/S0022-2836(02)00975-0. Unknown parameter |month= ignored (help)

[Avila-5] Avila J (1990). "Microtubule dynamics". FASEB J. 4 (15): 3284–90. PMID 2253844. Unknown parameter |month= ignored (help)

[Pomorski-6] 6.0 ^6.1 Pomorski T, Muller P, Zimmermann B, Burger K, Devaux PF, Herrmann A (1996). "Transbilayer movement of fluorescent and spin-labeled phospholipids in the plasma membrane of human fibroblasts: a quantitative approach". J Cell Sci. 109 (Pt 3): 687–98. PMID 8907713. Unknown parameter |month= ignored (help)

[phosphacholine-7] "1-palmitoyl-2-oleoylphosphatidylcholine - PubChem Public Chemical Database".

[tidylcholine-8] "Phosphatidylcholines - PubChem Public Chemical Database".

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[phosphorylcholine-10] "sphingosine phosphorylcholine - PubChem Public Chemical Database".

[TNPAL-11] "TNPAL-Sphingomyelin - PubChem Public Chemical Database".

[tidylserine-12] "Phosphatidylserine - PubChem Public Chemical Database".

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[Battley-14] Battley EH (1992). "On the enthalpy of formation of Escherichia coli K-12 cells". Biotech Bioeng. 39 (1): 5–12. doi:10.1002/bit.260390103. Unknown parameter |month= ignored (help)

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[Ghildiyal-30] Ghildiyal M, Zamore PD (2009). "Small silencing RNAs: an expanding universe". Nat. Rev. Genet. 10 (2): 94–108. doi:10.1038/nrg2504. PMID 19148191. Unknown parameter |month= ignored (help)

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[dystrophin-35] "Entrez Gene: DMD dystrophin".

[Dp427c-36] "Entrez Protein - dystrophin Dp427c isoform [Homo spiens]".

[Jacjson-37] Jackson DA, Pombo A, Iborra F (2000). "The balance sheet for transcription: an analysis of nuclear RNA metabolism in mammalian cells". FASEB J. 14 (2): 242–54. PMID 10657981.

[Anderson-38] Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR; et al. (1981). "Sequence and organization of the human mitochondrial genome". Nature. 410 (5806): 141. doi:10.1038/290457a0. Unknown parameter |month= ignored (help)

[Ali-39] Ali SY, Griffiths S (1983). "Formation of calcium phosphate crystals in normal and osteoarthritic cartilage". Ann Rheum Dis. 42 (Suppl 1): 45–8. PMID 6615026. Unknown parameter |month= ignored (help)

[Wuthier-40] 40.0 ^40.1 ^40.2 Wuthier RE (1993). "Involvement of cellular metabolism of calcium and phosphate in calcification of avian growth plate cartilage". J Nutr. 123 (2 Suppl): 301–9. PMID 8429379. Unknown parameter |month= ignored (help)

[Johnson-41] Johnson, Clarke (1998). "Biology of the Human Dentition".

[Cate-42] Cate, A.R. Ten. (1998). Oral Histology: development, structure, and function (5th ed.). pp. 150–5. ISBN 0-8151-2952-1.

[Taves-43] Taves DR, Reedy RC (1969). "A structural basis for the transphosphorylation of nucleotides with hydroxyapatite". Calcified Tissue International. 3 (1): 284–92. doi:10.1007/BF02058670. Unknown parameter |month= ignored (help)

[Hiatt-44] 44.0 ^44.1 Hiatt EE, Budd DA (2001). "Sedimentary phosphate formation in warm shallow waters: new insights into the palaeoceanography of the Permian Phosphoria Sea from analysis of phosphate oxygen isotopes". Sedimentary Geol. 145 (1–2): 119–33. doi:10.1016/S0037-0738(01)00127-0. Unknown parameter |month= ignored (help)

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v t e Phosphate biochemistry
Activities	Phosphate budget laboratory
Articles	Dominant group/Archaeology Dominant group/Paleontology
Courses	Geology courses
History
Lectures	Adenosine triphosphates Antisense RNA Bioenergetics Bones Cartilages Cell junction Cell membrane Configuron Cytoskeletons Degenerate nucleotide gene transcriptions Diazinon Dynactin Elasticity of cell membranes Extracellular fluids Ferredoxins Filopodia Flavodoxins Gap junction Glucose-6-phosphate Haemotaphonomy Human ATP synthase Human bones Hydroxyapatites Hyperphosphatemia Hypophosphorous acid Inorganic pyrophosphatases Intercellular space Lamellipodia Macromolecular crowding Matrix extracellular phosphoglycoprotein Meiosis Membrane skeleton Metaphosphate Microfilaments Microtubules Nucleic acids Nucleohyaloplasm Nucleoplasm Nucleoside triphosphates Nucleoskeleton Nucleosol Organophosphates Organophosphorus Oxidative phosphorylation Parathyroid gland Perinuclear space Phosphatases Phosphate minerals Phosphates Phosphate homeostasis Phosphate reactions Phosphate reserves Phosphate transistasis Phosphate-transporting ATPase Phospholipids Phosphonic acid Phosphoramidates Phosphoric acids Phosphoric acids and phosphates Phosphorites Phosphorous acid Phosphorus Phosphorus oxoacids Phosphorylation Phosphorylation cascade Phosphoryl chloride Polyphosphates Pseudopseudohypoparathyroidism Pyrimidine metabolism Pyrophosphate Pyrophosphoric acid (RNA-polymerase)-subunit kinase Skeletons Structural phosphates Superphosphates Tight junction Transduction Transduction (biophysics) Uridine triphosphate
Lessons
Original research	Biosynthesis of a human protein Origin of life: polyphosphate
Portals	Mineralogy