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Dilute to 1X with dH 2 O. Nonfat Dry Milk : Wash Buffer : 1X TBST. Bovine Serum Albumin BSA : Biotinylated Protein Ladder Detection Pack : Blue Prestained Protein Marker, Broad Range kDa : Blotting Membrane and Paper : This protocol has been optimized for nitrocellulose membranes.

Pore size 0. Secondary Antibody Conjugated to HRP : Anti-rabbit IgG, HRP-linked Antibody Protein Blotting A general protocol for sample preparation. Treat cells by adding fresh media containing regulator for desired time.

Aspirate media from cultures; wash cells with 1X PBS; aspirate. Lyse cells by adding 1X SDS sample buffer µl per well of 6-well plate or µl for a 10 cm diameter plate. Immediately scrape the cells off the plate and transfer the extract to a microcentrifuge tube.

Keep on ice. Sonicate for 10—15 sec to complete cell lysis and shear DNA to reduce sample viscosity. Heat a 20 µl sample to 95—°C for 5 min; cool on ice. Microcentrifuge for 5 min.

The cellular demise pathway mediated by PARylation in oxidatively stressed cells has been described almost thirty years ago. However, the underlying molecular mechanisms have only begun to emerge relatively recently.

PARylation has been implicated in necroptosis, autophagic cell death but its role in extrinsic and intrinsic apoptosis appears to be less predominant and depends largely on the cellular model used. Google Scholar Articles by Luo, X. Articles by Kraus, W. Search for related content. Related Content Signal Transduction Molecular Physiology and Metabolism.

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In closed ring riboses, the observed flexibility mentioned above is not observed because the ring cycle imposes a limit on the number of torsion angles possible in the structure.

If a carbon is facing towards the base, then the ribose is labeled as endo. If a carbon is facing away from the base, then the ribose is labeled as exo.

If there is an oxygen molecule attached to the 2' carbon of a closed cycle ribose, then the exo confirmation is more stable because it decreases the interactions of the oxygen with the base. A ribose molecule is typically represented as a planar molecule on paper. Despite this, it is typically non-planar in nature.

Even between hydrogen atoms, the many constituents on a ribose molecule cause steric hindrance and strain between them. To relieve this crowding and ring strain , the ring puckers, i. becomes non-planar. The pseudo-rotation angle can be described as either "north N " or "south S " range.

While both ranges are found in double helices, the north range is commonly associated with RNA and the A form of DNA. In contrast, the south range is associated with B form DNA. Z-DNA contains sugars in both the north and south ranges. When two atoms are displaced, it is referred to as a "twist" pucker, in reference to the zigzag orientation.

In an "exo" pucker, the major displacement of atoms is on the α-face, on the opposite side of the ring. The major forms of ribose are the 3'-endo pucker commonly adopted by RNA and A-form DNA and 2'-endo pucker commonly adopted by B-form DNA.

ATP is derived from ribose; it contains one ribose, three phosphate groups, and an adenine base. ATP is created during cellular respiration from adenosine diphosphate ATP with one less phosphate group.

Ribose is a building block in secondary signaling molecules such as cyclic adenosine monophosphate cAMP which is derived from ATP. One specific case in which cAMP is used is in cAMP-dependent signaling pathways.

In cAMP signaling pathways, either a stimulative or inhibitory hormone receptor is activated by a signal molecule. These receptors are linked to a stimulative or inhibitory regulative G-protein.

cAMP, a secondary messenger, then goes on to activate protein kinase A , which is an enzyme that regulates cell metabolism. Protein kinase A regulates metabolic enzymes by phosphorylation which causes a change in the cell depending on the original signal molecule.

The opposite occurs when an inhibitory G-protein is activated; the G-protein inhibits adenylyl cyclase and ATP is not converted to cAMP. Ribose is referred to as the "molecular currency" because of its involvement in intracellular energy transfers.

They can each be derived from d -ribose after it is converted to d -ribose 5-phosphate by the enzyme ribokinase. Nucleotides are synthesized through salvage or de novo synthesis. In de novo, amino acids, carbon dioxide, folate derivatives, and phosphoribosyl pyrophosphate PRPP are used to synthesize nucleotides.

Ribokinase catalyzes the conversion of d -ribose to d -ribose 5-phosphate. Once converted, d -ribosephosphate is available for the manufacturing of the amino acids tryptophan and histidine , or for use in the pentose phosphate pathway. One important modification occurs at the C2' position of the ribose molecule.

By adding an O-alkyl group, the nuclear resistance of the RNA is increased because of additional stabilizing forces. These forces are stabilizing because of the increase of intramolecular hydrogen bonding and an increase in the glycosidic bond stability.

Along with phosphorylation, ribofuranose molecules can exchange their oxygen with selenium and sulfur to produce similar sugars that only vary at the 4' position.

These derivatives are more lipophilic than the original molecule. Increased lipophilicity makes these species more suitable for use in techniques such as PCR , RNA aptamer post-modification, antisense technology , and for phasing X-ray crystallographic data. Similar to the 2' modifications in nature, a synthetic modification of ribose includes the addition of fluorine at the 2' position.

This fluorinated ribose acts similar to the methylated ribose because it is capable of suppressing immune stimulation depending on the location of the ribose in the DNA strand.

The addition of fluorine leads to an increase in the stabilization of the glycosidic bond and an increase of intramolecular hydrogen bonds.

d -ribose has been suggested for use in management of congestive heart failure [29] as well as other forms of heart disease and for chronic fatigue syndrome CFS , also called myalgic encephalomyelitis ME in an open-label non-blinded, non-randomized, and non-crossover subjective study.

Supplemental d -ribose can bypass part of the pentose phosphate pathway , an energy-producing pathway, to produce d -ribosephosphate. The enzyme glucosephosphate-dehydrogenase GPDH is often in short supply in cells, but more so in diseased tissue, such as in myocardial cells in patients with cardiac disease.

The supply of d -ribose in the mitochondria is directly correlated with ATP production; decreased d -ribose supply reduces the amount of ATP being produced.

Studies suggest that supplementing d -ribose following tissue ischemia e. myocardial ischemia increases myocardial ATP production, and therefore mitochondrial function.

Essentially, administering supplemental d -ribose bypasses an enzymatic step in the pentose phosphate pathway by providing an alternate source of 5-phospho- d -ribose 1- pyrophosphate for ATP production.

Supplemental d -ribose enhances recovery of ATP levels while also reducing cellular injury in humans and other animals. One study suggested that the use of supplemental d -ribose reduces the instance of angina in men with diagnosed coronary artery disease.

It is also used to reduce symptoms of cramping, pain, stiffness, etc. after exercise and to improve athletic performance [ citation needed ].

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d -Ribose. CAS Number. ChEMBL N. DB N. PubChem CID. Chemical formula. Solubility in water. Chiral rotation [α] D. In brief, 0. Increase in the resorufin fluorescence with excitation at nm and emission at nm was measured using a Hitachi F fluorometer. The results shown are means ± se from at least three independent measurements.

Human myometrial cells and myometrium extracts were incubated in lysis buffer containing 0. After 7. SC ; Santa Cruz Biotechnology for 4 h. The immunoreactive bands were detected using a , dilution of horseradish peroxidase-conjugated antigoat IgG SC ; Santa Cruz Biotechnology as secondary antibody and an enhanced chemiluminescence detection system.

mRNA was isolated using an Invitrogen kit FastTrack 2. cDNA was synthesized at 42 C for 50 min using 0. For PCR, a 2 μl-aliquot of each cDNA solution was added to a reaction medium containing 0.

Reactions were performed in a DNA thermal cycler, with 40 cycles at 94 C for 45 sec, at 55 C for 60 sec, and at 72 C for 90 sec. As housekeeping mRNA, glyceraldehydephosphate dehydrogenase GAPDH primers were used under the same conditions as described for CD Flow cytometric analysis was performed by incubating intact myometrial cells with fluorescein isothiocyanate FITC -labeled monoclonal antibody against CD38 SCFITC; Santa Cruz Biotechnology in a dilution and further analyzed in a FACScan fluorescence cytometer Becton Dickinson, Lincoln Park, NJ.

For immunocytochemistry, cells plated on coverslips were permeabilized with 0. In summary, uterine smooth muscle strips were dissected, 0. Signals were recorded via a data acquisition board AT-MIOL9; National Instruments Corp.

After stabilization and testing with oxytocin, the strips were incubated with 5 m m nicotinamide for 1 h before further addition of 1 μ m oxytocin. Each strip was its own control. The human myometrium used in all experiments was obtained from healthy premenopausal women undergoing elective hysterectomy.

Lytechinus pictus and Aplysia californica were obtained from Marinus, Inc. Long Beach, CA. BODIPY-TR-ryanodine and Fluo-3 were purchased from Molecular Probes.

All other reagents of the highest available purity grade were supplied by Sigma Chemical Co. Louis, MO. The reported experiments were repeated at least three to six times, as appropriate. Data are expressed as means ± sd. We used bodipy ryanodine to determine the presence of RyR in human myometrial cells.

As shown in Fig. Perinuclear distribution of bodipy ryanodine is consistent with the location of the RyR in the sarcoplasmic reticulum of the myometrial cells.

Ryanodine binding sites are also present in human myometrial microsomes. Binding of radioactive ryanodine to microsomes was determined and can be blocked by cold ryanodine, cADPR, and ruthenium red Fig. In addition, the effect of cADPR on ryanodine binding can be blocked by the cADPR inhibitor 8-Br-cADPR Fig.

These experiments confirmed the presence of RyR in myometrial cells 8 — 11 , 23 and indicate that cADPR interacts with the RyR in human myometrial cells and may play a role as the endogenous regulator of the RyR.

Characterization of RyR channel in human myometrial cells. A, Immunofluorescence of a myometrial cell stained with bodipy-labeled antibody raised against the RyR channel.

Notice the enhanced perinuclear distribution of fluorescence, consistent with the endoplasmic reticulum localization of the receptor. The arrows show the cell borders. B, Ryanodine binding in human myometrium microsomes. Shown are the average and se of four different experiments. The results of the present study support and extend those observations.

Agonists such as oxytocin play critical roles in the coordination of uterine contraction during labor. The intracellular signaling pathway that regulates the RyR channel in response to uterotonic agonists in human myometrium is not yet known. A, Human myometrial cells were perfused for 5 min with HBSS with or without 2 m m CaCl 2 , and calcium release was initiated by addition of 1 μ m oxytocin, as described in Materials and Methods.

B, Myometrial cells were exposed to the IP 3 receptor antagonist Xestospongin C 10 μ m or the cADPR antagonist 8-Br-cADPR μ m for 60 min. Release of calcium in response to 1 μ m oxytocin was then compared with untreated controls. Shown are the average and sd of four different experiments.

A member of our group has previously shown that TNFα induces cellular expression of CD38 and increases synthesis of cADPR Time dependence of the TNFα stimulation of cyclase indicates that its effect is mediated byincreased expression of the enzyme Fig.

Furthermore, TNFα was more potent then other cytokines tested Fig. CD38 cyclase activity and cADPR accumulation in human myometrial cells. A, Dose-dependent curve of TNFα in human myometrial cells.

Cells were cultured in six-well plates and incubated with varying concentrations of TNFα for 24 h, after which culture medium was replaced with sucrose buffer containing 20 m m Tris-HCl pH 7. C, Effect of the different cytokines on CD38 cyclase activity in human myometrial cells.

D, cADPR levels in human myometrial cells. Nucleotide levels were measured as described in Materials and Methods. First, the effect of TNFα on CD38 cyclase activity was inhibited by the DNA synthesis inhibitor actinomycin D and cycloheximide, an inhibitor of protein synthesis Fig.

Furthermore, we observed an increased expression of immunoreactive CD38 in cells treated with TNFα. Immunoprecipitation and Western blot analysis showed a 3-fold increase of CD38 enzyme in TNFα-treated cells when compared with nontreated cells Fig.

Cycloheximide and actinomycin D inhibited the effect of TNFα on the activity of the ADP-ribosyl cyclase Fig. These data were confirmed by immunostaining the cultured human myometrial cells with FITC-labeled monoclonal antibody for CD38 Fig.

TNFα stimulates de novo synthesis of CD A, Cyclase activity in the presence of protein and transcription inhibitors. C, Densitometry of the Western blot bands.

See Materials and Methods for details. D and E, Immunocytochemistry of human myometrial cells stained with an FITC-labeled monoclonal antibody against human CD Magnification: top , ×20 × oil lens; bottom , × D, Control cells.

Arrows indicate the location of the cells. F, RT-PCR for CD38 and GAPDH mRNAs. In lane 1, HL cells were incubated with 1 μ m all-trans-retinoic acid atRA for 24 h and used as positive control.

For details see Materials and Methods. Finally, we found an increase in CD38 mRNA levels in ΤNFα-treated human myometrial cells Fig. In contrast, TNFα had no effect on the mRNA levels of the constitutive enzyme GAPDH. These data clearly indicate that TNFα treatment leads to increased expression of CD38 and increased intracellular cADPR levels in human myometrial cells.

The cADPR inhibitor 8-Br-cADPR blocked this increase Fig. Previous studies have shown that the activity of CD38 cyclase can be inhibited by nicotinamide and its analogs Our study confirms these findings data not shown.

Cells were then treated with medium with or without 5 m m nicotinamide for 60 min, and release of intracellular calcium was initiated with 1 μ m oxytocin. Results are the means of three or four experiments. C, Uterine muscle strips were obtained, and the force change induced by oxytocin was determined as described in Materials and Methods.

Strips were incubated with nicotinamide for 1 h before the addition of 1 μ m oxytocin. The data shown are the result of three different strips. Maximum force for controls was 5. We also demonstrated that TNFα and interleukins can affect ADP-ribosyl cyclase activity and CD38 expression in human myometrial cells, thus increasing levels of cADPR.

During human pregnancy the myometrium is relatively quiescent until close to term 1 , 28 , The precise sequence of events preceding the initiation of intense contractile activity in human labor is still unknown and is likely due to an orchestration of many pathways.

It is possible that cytokines may modulate the expression of components of the cADPR pathway in vivo and, in this way, increase contractility. During pregnancy, the myometrium undergoes various structural and biochemical changes 1 , 28 , During the first two stages of pregnancy, hyperplasia and hypertrophy occur.

It is during the third stage of pregnancy, however, that the balance in the myometrium starts to shift from relaxant to contracting pathways. Mounting evidence indicates that the parturition process represents an inflammatory response 30 — When term labor approaches, leukocytes, macrophages, neutrophils, and T-lymphocytes infiltrate the myometrium.

Moreover, it has been shown that proinflammatory cytokines are expressed in myometrium in association with labor 30 , Recent studies have demonstrated that the onset of term labor induces elevated production of IL-1β, IL-6, IL-8, and TNFα by placental endothelial cells and increases their concentrations in the amniotic fluid Development of new therapeutic strategies that target the cADPR system may be key to the generation of new specific therapies for dysfunctional uterine contractions.

This work was supported by Mayo Foundation Clinical Research protocol to E. and NIH Grant GM Bernal, AL Uterine contractility symposium: overview of current research in parturition. Exp Physiol 86 : — Slattery MM , Morrison J Preterm delivery.

Lancet : — Google Scholar. Tribe RM Regulation of human myometrial contraction during pregnancy and labour: are calcium homeostatic pathways important? Phillippe M , Chien EK Intracellular signaling and phasic myometrial contractions.

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Supporting Data Related Products Product Usage Protocols Background Pathways Citations On Page Menu. Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

What is a Recombinant Antibody? Superior Lot-to-Lot Consistency Because recombinant antibody production involves sequencing the antibody light and heavy chains, it is a highly controlled and reliable process.

Scalability In vitro methods for producing antibodies are amenable to large-scale production, meaning antibody availability is unlikely to become a limiting factor.

Animal-free Manufacturing Unlike traditional methods for antibody production, recombinant approaches avoid the need to use animals. SARS-CoV-2 2'-O-ribose Methyltransferase E6N2C Rabbit mAb Citations 0. Filter: WB. Image Gallery Learn more about how we get our images.

To Purchase Size Qty. ADD TO BASKET Carrier Free and Custom Formulation. Your Local Representative Your Local Purchase Information Antibody Guarantee FAQ Tech Support -- Datasheet -- Without Images With Images SDS: Choose Your Region America - English China - Chinese China - English Europe - Dutch Europe - English Europe - French Europe - German Europe - Italian Europe - Portuguese Europe - Spanish Europe - Swedish Japan - English Japan - Japanese Korea - English Korea - Korean Certificate of Analysis.

Supporting Data Related Products Product Usage Protocols Background Pathways Citations. melanogaster X -Xenopus Z -Zebrafish B -Bovine Dg -Dog Pg -Pig Sc -S. cerevisiae Ce -C. elegans Hr -Horse GP -Guinea Pig Rab -Rabbit All -All Species Expected.

Related Products. Product Information Product Usage Information Application Dilution Western Blotting Storage Supplied in 10 mM sodium HEPES pH 7.

BODIPY-TR-ryanodine and Fluo-3 were purchased from Molecular Probes. All other reagents of the highest available purity grade were supplied by Sigma Chemical Co. Louis, MO. The reported experiments were repeated at least three to six times, as appropriate. Data are expressed as means ± sd.

We used bodipy ryanodine to determine the presence of RyR in human myometrial cells. As shown in Fig. Perinuclear distribution of bodipy ryanodine is consistent with the location of the RyR in the sarcoplasmic reticulum of the myometrial cells.

Ryanodine binding sites are also present in human myometrial microsomes. Binding of radioactive ryanodine to microsomes was determined and can be blocked by cold ryanodine, cADPR, and ruthenium red Fig.

In addition, the effect of cADPR on ryanodine binding can be blocked by the cADPR inhibitor 8-Br-cADPR Fig. These experiments confirmed the presence of RyR in myometrial cells 8 — 11 , 23 and indicate that cADPR interacts with the RyR in human myometrial cells and may play a role as the endogenous regulator of the RyR.

Characterization of RyR channel in human myometrial cells. A, Immunofluorescence of a myometrial cell stained with bodipy-labeled antibody raised against the RyR channel.

Notice the enhanced perinuclear distribution of fluorescence, consistent with the endoplasmic reticulum localization of the receptor. The arrows show the cell borders. B, Ryanodine binding in human myometrium microsomes.

Shown are the average and se of four different experiments. The results of the present study support and extend those observations. Agonists such as oxytocin play critical roles in the coordination of uterine contraction during labor.

The intracellular signaling pathway that regulates the RyR channel in response to uterotonic agonists in human myometrium is not yet known. A, Human myometrial cells were perfused for 5 min with HBSS with or without 2 m m CaCl 2 , and calcium release was initiated by addition of 1 μ m oxytocin, as described in Materials and Methods.

B, Myometrial cells were exposed to the IP 3 receptor antagonist Xestospongin C 10 μ m or the cADPR antagonist 8-Br-cADPR μ m for 60 min. Release of calcium in response to 1 μ m oxytocin was then compared with untreated controls. Shown are the average and sd of four different experiments.

A member of our group has previously shown that TNFα induces cellular expression of CD38 and increases synthesis of cADPR Time dependence of the TNFα stimulation of cyclase indicates that its effect is mediated byincreased expression of the enzyme Fig.

Furthermore, TNFα was more potent then other cytokines tested Fig. CD38 cyclase activity and cADPR accumulation in human myometrial cells. A, Dose-dependent curve of TNFα in human myometrial cells.

Cells were cultured in six-well plates and incubated with varying concentrations of TNFα for 24 h, after which culture medium was replaced with sucrose buffer containing 20 m m Tris-HCl pH 7.

C, Effect of the different cytokines on CD38 cyclase activity in human myometrial cells. D, cADPR levels in human myometrial cells. Nucleotide levels were measured as described in Materials and Methods. First, the effect of TNFα on CD38 cyclase activity was inhibited by the DNA synthesis inhibitor actinomycin D and cycloheximide, an inhibitor of protein synthesis Fig.

Furthermore, we observed an increased expression of immunoreactive CD38 in cells treated with TNFα. Immunoprecipitation and Western blot analysis showed a 3-fold increase of CD38 enzyme in TNFα-treated cells when compared with nontreated cells Fig.

Cycloheximide and actinomycin D inhibited the effect of TNFα on the activity of the ADP-ribosyl cyclase Fig. These data were confirmed by immunostaining the cultured human myometrial cells with FITC-labeled monoclonal antibody for CD38 Fig. TNFα stimulates de novo synthesis of CD A, Cyclase activity in the presence of protein and transcription inhibitors.

C, Densitometry of the Western blot bands. See Materials and Methods for details. D and E, Immunocytochemistry of human myometrial cells stained with an FITC-labeled monoclonal antibody against human CD Magnification: top , ×20 × oil lens; bottom , × D, Control cells.

Arrows indicate the location of the cells. F, RT-PCR for CD38 and GAPDH mRNAs. In lane 1, HL cells were incubated with 1 μ m all-trans-retinoic acid atRA for 24 h and used as positive control. For details see Materials and Methods.

Finally, we found an increase in CD38 mRNA levels in ΤNFα-treated human myometrial cells Fig. In contrast, TNFα had no effect on the mRNA levels of the constitutive enzyme GAPDH. These data clearly indicate that TNFα treatment leads to increased expression of CD38 and increased intracellular cADPR levels in human myometrial cells.

The cADPR inhibitor 8-Br-cADPR blocked this increase Fig. Previous studies have shown that the activity of CD38 cyclase can be inhibited by nicotinamide and its analogs Our study confirms these findings data not shown. Cells were then treated with medium with or without 5 m m nicotinamide for 60 min, and release of intracellular calcium was initiated with 1 μ m oxytocin.

Results are the means of three or four experiments. C, Uterine muscle strips were obtained, and the force change induced by oxytocin was determined as described in Materials and Methods. Strips were incubated with nicotinamide for 1 h before the addition of 1 μ m oxytocin. The data shown are the result of three different strips.

Maximum force for controls was 5. We also demonstrated that TNFα and interleukins can affect ADP-ribosyl cyclase activity and CD38 expression in human myometrial cells, thus increasing levels of cADPR.

During human pregnancy the myometrium is relatively quiescent until close to term 1 , 28 , The precise sequence of events preceding the initiation of intense contractile activity in human labor is still unknown and is likely due to an orchestration of many pathways. It is possible that cytokines may modulate the expression of components of the cADPR pathway in vivo and, in this way, increase contractility.

During pregnancy, the myometrium undergoes various structural and biochemical changes 1 , 28 , During the first two stages of pregnancy, hyperplasia and hypertrophy occur. It is during the third stage of pregnancy, however, that the balance in the myometrium starts to shift from relaxant to contracting pathways.

Mounting evidence indicates that the parturition process represents an inflammatory response 30 — When term labor approaches, leukocytes, macrophages, neutrophils, and T-lymphocytes infiltrate the myometrium. Moreover, it has been shown that proinflammatory cytokines are expressed in myometrium in association with labor 30 , Recent studies have demonstrated that the onset of term labor induces elevated production of IL-1β, IL-6, IL-8, and TNFα by placental endothelial cells and increases their concentrations in the amniotic fluid Development of new therapeutic strategies that target the cADPR system may be key to the generation of new specific therapies for dysfunctional uterine contractions.

This work was supported by Mayo Foundation Clinical Research protocol to E. and NIH Grant GM Bernal, AL Uterine contractility symposium: overview of current research in parturition.

Exp Physiol 86 : — Slattery MM , Morrison J Preterm delivery. Lancet : — Google Scholar. Tribe RM Regulation of human myometrial contraction during pregnancy and labour: are calcium homeostatic pathways important?

Phillippe M , Chien EK Intracellular signaling and phasic myometrial contractions. J Soc Gynecol Invest 5 : — Ruttner Z , Inanics T , Slaaf DW , Reneman RS , Toth A , Ligeti L In vivo monitoring of intracellular free calcium changes during uterine activation by prostaglandin F-2α and oxytocin.

J Soc Gynecol Invest 9 : — Biol Reprod 60 : — Berridge MJ , Lipp P , Bootman MD The versatility and universality of calcium signalling. Nat Rev Mol Cell Biol 1 : 11 — Awad SS , Lamb HK , Morgan JM , Dunlop W , Gillespie JI Differential expression of ryanodine receptor RyR2 mRNA in the non-pregnant and pregnant human myometrium.

Biochem J : — Martin C , Hyvelin JM , Chapman KE , Marthan R , Ashley RH , Savineau JP Pregnant rat myometrial cells show heterogeneous ryanodine- and caffeine-sensitive calcium stores.

Am J Physiol 2 C — C Young RC , Mathur SP Focal sarcoplasmic reticulum calcium stores and diffuse inositol 1,4,5-trisphosphate and ryanodine receptors in human myometrium.

Cell Calcium 26 : 69 — Young RC , Zhang P The mechanism of propagation of intracellular calcium waves in cultured human uterine myocytes. Am J Obstet Gynecol : — Chini EN , De Toledo FGS The new calcium-mobilizing nucleotides cyclic ADP-ribose and NAADP. In: Pandalai SG , ed.

Recent research developments in biophysics and biochemistry. Trivandrum, India : Research Signpost ; 43 — Coronado R , Morrissette J , Sukhareva M , Vaughan DM Structure and function of ryanodine receptors. Am J Physiol : C — C Trends Cell Biol 4 : —