Relevant bibliographies by topics / Guanylate cyclase, retinal dystrophy

Academic literature on the topic 'Guanylate cyclase, retinal dystrophy'

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Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Guanylate cyclase, retinal dystrophy"

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Downes, Susan M. "Autosomal Dominant Cone-Rod Dystrophy With Mutations in the Guanylate Cyclase 2D Gene Encoding Retinal Guanylate Cyclase-1." Archives of Ophthalmology 119, no. 11 (November 1, 2001): 1667. http://dx.doi.org/10.1001/archopht.119.11.1667.

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Marino, Valerio, Giuditta Dal Cortivo, Paolo Enrico Maltese, Giorgio Placidi, Elisa De Siena, Benedetto Falsini, Matteo Bertelli, and Daniele Dell’Orco. "Impaired Ca2+ Sensitivity of a Novel GCAP1 Variant Causes Cone Dystrophy and Leads to Abnormal Synaptic Transmission Between Photoreceptors and Bipolar Cells." International Journal of Molecular Sciences 22, no. 8 (April 14, 2021): 4030. http://dx.doi.org/10.3390/ijms22084030.

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Guanylate cyclase-activating protein 1 (GCAP1) is involved in the shutdown of the phototransduction cascade by regulating the enzymatic activity of retinal guanylate cyclase via a Ca2+/cGMP negative feedback. While the phototransduction-associated role of GCAP1 in the photoreceptor outer segment is widely established, its implication in synaptic transmission to downstream neurons remains to be clarified. Here, we present clinical and biochemical data on a novel isolate GCAP1 variant leading to a double amino acid substitution (p.N104K and p.G105R) and associated with cone dystrophy (COD) with an unusual phenotype. Severe alterations of the electroretinogram were observed under both scotopic and photopic conditions, with a negative pattern and abnormally attenuated b-wave component. The biochemical and biophysical analysis of the heterologously expressed N104K-G105R variant corroborated by molecular dynamics simulations highlighted a severely compromised Ca2+-sensitivity, accompanied by minor structural and stability alterations. Such differences reflected on the dysregulation of both guanylate cyclase isoforms (RetGC1 and RetGC2), resulting in the constitutive activation of both enzymes at physiological levels of Ca2+. As observed with other GCAP1-associated COD, perturbation of the homeostasis of Ca2+ and cGMP may lead to the toxic accumulation of second messengers, ultimately triggering cell death. However, the abnormal electroretinogram recorded in this patient also suggested that the dysregulation of the GCAP1–cyclase complex further propagates to the synaptic terminal, thereby altering the ON-pathway related to the b-wave generation. In conclusion, the pathological phenotype may rise from a combination of second messengers’ accumulation and dysfunctional synaptic communication with bipolar cells, whose molecular mechanisms remain to be clarified.
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Kelsell, R. E., K. Gregory-Evans, A. M. Payne, I. Perrault, J. Kaplan, R. B. Yang, D. L. Garbers, A. C. Bird, A. T. Moore, and D. M. Hunt. "Mutations in the Retinal Guanylate Cyclase (RETGC-1) Gene in Dominant Cone-Rod Dystrophy." Human Molecular Genetics 7, no. 7 (July 1, 1998): 1179–84. http://dx.doi.org/10.1093/hmg/7.7.1179.

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Mahroo, Omar A., Gavin Arno, Rola Ba-Abbad, Susan M. Downes, Alan Bird, and Andrew R. Webster. "Reanalysis of Association of Pro50Leu Substitution in Guanylate Cyclase Activating Protein-1 With Dominant Retinal Dystrophy." JAMA Ophthalmology 138, no. 2 (February 1, 2020): 200. http://dx.doi.org/10.1001/jamaophthalmol.2019.4959.

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Martínez-Velázquez, Luis A., and Niels Ringstad. "Antagonistic regulation of trafficking to Caenorhabditis elegans sensory cilia by a Retinal Degeneration 3 homolog and retromer." Proceedings of the National Academy of Sciences 115, no. 3 (December 27, 2017): E438—E447. http://dx.doi.org/10.1073/pnas.1712302115.

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Sensory neurons often possess cilia with elaborate membrane structures that are adapted to the sensory modality of the host cell. Mechanisms that target sensory transduction proteins to these specialized membrane domains remain poorly understood. Here, we show that a homolog of the human retinal dystrophy gene Retinal Degeneration 3 (RD3) is a Golgi-associated protein required for efficient trafficking of a sensory receptor, the receptor-type guanylate cyclase GCY-9, to cilia in chemosensory neurons of the nematode Caenorhabditis elegans. The trafficking defect caused by mutation of the nematode RD3 homolog is suppressed in vivo by mutation of key components of the retromer complex, which mediates recycling of cargo from endosomes to the Golgi. Our data show that there exists a critical balance in sensory neurons between the rates of anterograde and retrograde trafficking of cargo destined for the sensory cilium and this balance requires molecular specialization at an early stage of the secretory pathway.
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Payne, Annette M., Susan M. Downes, David A. R. Bessant, Catherine Plant, Tony Moore, Alan C. Bird, and Shomi S. Bhattacharya. "Genetic analysis of the guanylate cyclase activator 1B (GUCA1B) gene in patients with autosomal dominant retinal dystrophies: Table 1." Journal of Medical Genetics 36, no. 9 (September 1, 1999): 691–93. http://dx.doi.org/10.1136/jmg.36.9.691.

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The guanylate cyclase activator proteins (GCAP1 and GCAP2) are calcium binding proteins which by activating Ret-GC1 play a key role in the recovery phase of phototransduction. Recently a mutation in theGUCA1A gene (coding for GCAP1) mapping to the 6p21.1 region was described as causing cone dystrophy in a British family. In addition mutations in Ret-GC1have been shown to cause Leber congenital amaurosis and cone-rod dystrophy. To determine whether GCAP2 is involved in dominant retinal degenerative diseases, the GCAP2 gene was screened in 400 unrelated subjects with autosomal dominant central and peripheral retinal dystrophies.A number of changes involving the intronic as well as the coding sequence were observed. In exon 1 a T to C nucleotide change was observed leaving the tyrosine residue 57 unchanged. In exon 3 a 1 bp intronic insertion, a single nucleotide substitution G to A in the intron 3′ of this exon, and a GAG to GAT change at codon 155 were observed. This latter change results in a conservative change of glutamic acid to aspartic acid. In exon 4 a 7 bp intronic insertion, a single nucleotide A to G substitution in the intron 5′ of this exon, and a single base pair change C to G in the intron 3′ of exon 4 were seen. None of these changes would be expected to affect correct splicing of this gene. All these changes were observed in controls. The results of this study do not show any evidence so far that GCAP2 is involved in the pathogenesis of autosomal dominant retinal degeneration in this group of patients. All the changes detected were found to be sequence variations or polymorphisms and not disease causing.
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Biasi, Amedeo, Valerio Marino, Giuditta Dal Cortivo, Paolo Enrico Maltese, Antonio Mattia Modarelli, Matteo Bertelli, Leonardo Colombo, and Daniele Dell’Orco. "A Novel GUCA1A Variant Associated with Cone Dystrophy Alters cGMP Signaling in Photoreceptors by Strongly Interacting with and Hyperactivating Retinal Guanylate Cyclase." International Journal of Molecular Sciences 22, no. 19 (October 6, 2021): 10809. http://dx.doi.org/10.3390/ijms221910809.

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Guanylate cyclase-activating protein 1 (GCAP1), encoded by the GUCA1A gene, is a neuronal calcium sensor protein involved in shaping the photoresponse kinetics in cones and rods. GCAP1 accelerates or slows the cGMP synthesis operated by retinal guanylate cyclase (GC) based on the light-dependent levels of intracellular Ca2+, thereby ensuring a timely regulation of the phototransduction cascade. We found a novel variant of GUCA1A in a patient affected by autosomal dominant cone dystrophy (adCOD), leading to the Asn104His (N104H) amino acid substitution at the protein level. While biochemical analysis of the recombinant protein showed impaired Ca2+ sensitivity of the variant, structural properties investigated by circular dichroism and limited proteolysis excluded major structural rearrangements induced by the mutation. Analytical gel filtration profiles and dynamic light scattering were compatible with a dimeric protein both in the presence of Mg2+ alone and Mg2+ and Ca2+. Enzymatic assays showed that N104H-GCAP1 strongly interacts with the GC, with an affinity that doubles that of the WT. The doubled IC50 value of the novel variant (520 nM for N104H vs. 260 nM for the WT) is compatible with a constitutive activity of GC at physiological levels of Ca2+. The structural region at the interface with the GC may acquire enhanced flexibility under high Ca2+ conditions, as suggested by 2 μs molecular dynamics simulations. The altered interaction with GC would cause hyper-activity of the enzyme at both low and high Ca2+ levels, which would ultimately lead to toxic accumulation of cGMP and Ca2+ in the photoreceptor outer segment, thus triggering cell death.
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Avesani, Anna, Valerio Marino, Serena Zanzoni, Karl-Wilhelm Koch, and Daniele Dell'Orco. "Molecular properties of human guanylate cyclase–activating protein 2 (GCAP2) and its retinal dystrophy–associated variant G157R." Journal of Biological Chemistry 296 (January 2021): 100619. http://dx.doi.org/10.1016/j.jbc.2021.100619.

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Marino, Valerio, Alexander Scholten, Karl-Wilhelm Koch, and Daniele Dell'Orco. "Two retinal dystrophy-associated missense mutations inGUCA1Awith distinct molecular properties result in a similar aberrant regulation of the retinal guanylate cyclase." Human Molecular Genetics 24, no. 23 (September 10, 2015): 6653–66. http://dx.doi.org/10.1093/hmg/ddv370.

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Abbas, Seher, Valerio Marino, Laura Bielefeld, Karl-Wilhelm Koch, and Daniele Dell’Orco. "Constitutive Activation of Guanylate Cyclase by the G86R GCAP1 Variant Is Due to “Locking” Cation-π Interactions that Impair the Activator-to-Inhibitor Structural Transition." International Journal of Molecular Sciences 21, no. 3 (January 23, 2020): 752. http://dx.doi.org/10.3390/ijms21030752.

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Guanylate Cyclase activating protein 1 (GCAP1) mediates the Ca2+-dependent regulation of the retinal Guanylate Cyclase (GC) in photoreceptors, acting as a target inhibitor at high [Ca2+] and as an activator at low [Ca2+]. Recently, a novel missense mutation (G86R) was found in GUCA1A, the gene encoding for GCAP1, in patients diagnosed with cone-rod dystrophy. The G86R substitution was found to affect the flexibility of the hinge region connecting the N- and C-domains of GCAP1, resulting in decreased Ca2+-sensitivity and abnormally enhanced affinity for GC. Based on a structural model of GCAP1, here, we tested the hypothesis of a cation-π interaction between the positively charged R86 and the aromatic W94 as the main mechanism underlying the impaired activator-to-inhibitor conformational change. W94 was mutated to F or L, thus, resulting in the double mutants G86R+W94L/F. The double mutants showed minor structural and stability changes with respect to the single G86R mutant, as well as lower affinity for both Mg2+ and Ca2+, moreover, substitutions of W94 abolished “phase II” in Ca2+-titrations followed by intrinsic fluorescence. Interestingly, the presence of an aromatic residue in position 94 significantly increased the aggregation propensity of Ca2+-loaded GCAP1 variants. Finally, atomistic simulations of all GCAP1 variants in the presence of Ca2+ supported the presence of two cation-π interactions involving R86, which was found to act as a bridge between W94 and W21, thus, locking the hinge region in an activator-like conformation and resulting in the constitutive activation of the target under physiological conditions.
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Dissertations / Theses on the topic "Guanylate cyclase, retinal dystrophy"

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BONI', FRANCESCO. "GUANYLATE CYCLASE ACTIVATING PROTEIN 1 MONOMER-DIMER EQUILIBRIUM CONTROLLED BY CA2+ OR MG2+ BINDING: HINTS TO UNDERSTAND RETINAL GUANYLATE CYCLASE REGULATION." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/839565.

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Neuronal calcium sensors play a crucial role in different pathways of Ca2+-mediated neurotransmission. Among them guanylate cyclase-activating protein 1 (GCAP1) is expressed only in photoreceptors and activates or inhibits retinal guanylate cyclase 1 (retGC1) depending on cellular Ca2+ concentrations during phototransduction. To date, 22 pathogenic mutations responsible for retinal dystrophy have been associated to GCAP1, but a complete picture of the molecular determinants of the disease is still missing. The only crystal structure available so far is the wt Ca2+-bound monomeric homologue from chicken and no cure exists for retinal dystrophy. In this work I report for the first time that the recombinant human GCAP1 is characterized by a highly dynamic monomer-dimer equilibrium, whose dissociation constant is influenced by salt concentration and by the nature of the divalent ion bound. Surprisingly, I discovered that also the chicken protein shows a similar mechanism, suggesting that this property could be potentially functional for GCAP1 activity and conserved among different species. Despite the large number of crystallization trials, no diffracting crystal of the human GCAP1 was obtained, probably due to the flexible C-terminal tail and the intrinsic dynamicity of the protein. To overcome this issue, I produced a construct lacking the 12 C-term residues and stabilized by a disulfide bridge between the N- and C-term domains which was successfully crystallized. We showed that such engineered construct is able to regulate retGC1 as well as the wt protein. By combining SAXS, protein-protein docking and molecular dynamics simulation we propose two novel three-dimensional models of Ca2+-bound GCAP1 dimer which are stabilized by some of the residues involved in the interaction with the retGC1. We used a biophysical and biochemical approach to thoroughly investigate three pathogenic variants (D100G, E155A and E155G) characterized by mutations in residues directly involved in Ca2+-coordination. All the three variants were able to form oligomers in solutions, showing a decreased affinity for Ca2+ and constitutively activating retGC1 at physiological calcium concentrations. Besides local structural effects, the mutations perturb also the oligomeric state of GCAP1 suggesting that the multimeric assembly of the protein could affect its proper biological function. A recombinant baculovirus for the expression of the cytoplasmic domain of retGC1 in insect cells was produced with the aim to get atomic structural information on the GCAP1/retGC1 complex. This will facilitate the identification of drug candidates able to recognize the binding region of the pathogenic GCAP1 mutants with the cyclase and to competitively inhibit the constitutive retGC1 activation, restoring the homeostasis of second messengers which is impaired in retinal degenerative diseases. A preliminary molecular docking based on the crystal structure of the chicken protein was performed and I identified four molecules able to bind the wt human GCAP1 in the millimolar/micromolar range. Together these results shed new light on the quaternary assembly of the wt human GCAP1, showing how the structural changes related to the presence of Ca2+ or Mg2+ are reflected in the different measured dimerization constant. Such conformational changes are in turn likely related to the regulatory mechanism of GCAP1 in the modulation of the retGC1 activity. The differences between the oligomerization state of D100G, E155G and E155A variants suggest a correlation between the altered quaternary assembly of GCAP1 and the aberrant activity of the mutants, representing a step forward to dissect the structural bases of the altered regulatory mechanism of GCAP1 in retinal dystrophies.
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Tucker, Chandra Lenore. "Structural and functional studies of retinal guanylyl cyclase /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/9272.

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Krylov, Dmitri M. "Guanylyl cyclase activating protein-1 and its regulation of retinal guanylyl cyclases : a study by molecular biological methods and a novel mass spectrometry based method /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/9259.

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López, del Hoyo Natalia. "Role of Guanylate Cyclase Activating Proteins in photoreceptor cells of the retina in health and disease." Doctoral thesis, Universitat de Barcelona, 2014. http://hdl.handle.net/10803/283566.

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In the last two decades, it has been done a thoroughly research about the role of Guanylate Cyclase Activating Proteins (GCAPs) in photoreceptor cells of the retina as activity regulators of Retinal Guanylate Cyclase (RetGC), which allow to restore cGMP levels to darkness ones when intracellular Ca2+ falls. However, little is known about: a) ¿What determines GCAPs distribution within the cell?, b) ¿Which other functions GCAP proteins, GCAP1 and GCAP2, carry out at other cellular compartments different from the sensory one? and c) ¿How they cause cell death when they are mutated? In this study we want address these questions. 1. First of all, we own a mouse model that expresses a GCAP2 mutated form unable to bind Ca2+ (bEF-GCAP2). Other mutations described for GCAP1 and present in some autosomic dominant Cone Rod Dystrophies (adCORD), prevent Ca2+ binding to some of its EF-hand domains which produces the constitutive activation of RetGC, and consequently, high cGMP levels that result in toxicity for the cell. However, we observe that our model causes the death by other mechanism, as RetGC is not activated by GCAP2, because GCAP2 is retained in the inner segment and does not translocate to the sensory compartment. We want to identify interactions that GCAP2 establish differentially in this compartment and could be retaining it. We find out 14-3-3 family of proteins by mass-spectrometry and liquid chromatography. Furthermore, bEF-GCAP2 is abnormally phosphorylated in vivo and GCAP2 phosphorylation promotes its binding to 14-3-3 binding. We demonstrate that GCAP2 phosphorylation in residue serine 201 is the cause of its retention in the inner segment, avoiding its translocation to the outer segment, and when we mutate serine 201 into a glycine, this retention is reverted in vivo. Finally, we propose that GCAP2 phosphorylation and its binding to 14-3-3 is what retains GCAP2 in the inner segment, and this happens in a balance way during dark/light day cycles. When this system overloads will cause retinal degeneration by the formation of aggregates. We believe that mutations in GCAP2 or light conditions promoting GCAP2 accumulation in its Ca2+-free form in the inner segment of the cell, bring to cell death by GCAP2 conformational instability. Most important, we propose that this will also apply for genetic scenarios mimicking the effects to constant light exposure, the so called “equivalent-light” scenarios. 2. Secondly, as a result of the identification of GCAP2 interaction to RIBEYE (Venkatesan et al. 2010) the major component of synaptic ribbons in the photoreceptor cell terminal, we developed an ultrastructural study of the role that GCAP2 may play in this compartment. Through confocal and electronic microscopy we have demonstrated the presence of GCAP1 and GCAP2 in rod synaptic ribbons. However, GCAP1 and GCAP2 are not necessary during synaptic ribbons assembling and basic maintenance. As GCAP2 overexpression in the wildtype background (which means a higher GCAP2:GCAP1 ratio) promotes ribbons disassembling, we propose that GCAP2 may play a role mediating the morphological changes that take place in the synaptic ribbons in response to variations in [Ca2+].
En las dos últimas décadas se ha investigado a fondo el papel que juegan las Proteínas Activadoras de Guanilato Ciclasa (GCAPs) en las células fotorreceptor de la retina como proteínas encargadas de regular la actividad de la Guanilato Ciclasa (GC). Sin embargo se sabe poco acerca de: a) ¿Qué determina la distribución de GCAPs en la célula?, b) ¿Qué otras funciones ejercen GCAP1 y GCAP2 en otros compartimentos celulares distintos al segmento sensorial? y c) ¿Cómo dan lugar a muerte celular cuando están mutadas? En este estudio hemos querido encarar estas preguntas. 1. En primer lugar, poseemos un modelo de ratón que expresa una forma mutante de GCAP2 que no une Ca2+ (bEF-GCAP2). A diferencia de otras mutaciones descritas para GCAP1, en que se ha observado que la muerte celular es producida por niveles tóxicos de cGMP, observamos que nuestro modelo produce la muerte celular por otro mecanismo en que GCAP2 se acumula en el segmento interno. Identificamos abundantemente las distintas isoformas de 14-3-3 como interactores diferenciales de bEF-GCAP2, que a su vez está anormalmente fosforilada in vivo. Tras una serie de experimentos para caracterizar esta interacción, proponemos que la fosforilación de GCAP2 y su unión a 14-3-3 retienen a GCAP2 en el segmento interno, y si este mecanismo se sobrecarga por a) mutaciones en GCAP2, b) condiciones de luz que promuevan la acumulación de GCAP2 en su forma libre de Ca2+ en el segmento interno o c) condiciones genéticas que mimeticen los efectos de exposición a luz prolongada, tendría lugar la degeneración de la retina por la formación de agregados debido a la inestabilidad conformacional de GCAP2. 2. En segundo lugar, tras la identificación de la interacción de GCAP2 con RIBEYE (Venkatesan et al. 2010), el componente mayoritario de las cintillas sinápticas de fotorreceptores, realizamos un estudio ultrastructural del papel que puede estar jugando GCAP2 en este compartimento mediante microscopia electrónica y confocal, demostrando la presencia de GCAP1 y GCAP2 en las cintillas sinápticas de bastones. GCAP1 y GCAP2 son prescindibles en el ensamblaje y mantenimiento básico de las cintillas sinápticas, pero la sobreexpresión de GCAP2 en el fenotipo salvaje, que incrementa el ratio GCAP2:GCAP1, promueve el desensamblaje de las cintillas. Proponemos que GCAP2 podría jugar un papel mediando cambios morfológicos en las cintillas sinápticas promovidas por cambios en [Ca2+].
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Book chapters on the topic "Guanylate cyclase, retinal dystrophy"

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Duda, Teresa, and Karl-Wilhelm Koch. "Retinal diseases linked with photoreceptor guanylate cyclase." In Guanylate Cyclase, 129–38. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0927-1_11.

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Bondarenko, Vladimir A., Hao Yu, Russell K. Yamazaki, and Akio Yamazaki. "A novel role of RGS9: Inhibition of retinal guanylyl cyclase." In Guanylate Cyclase, 125–28. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0927-1_10.

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Olshevskaya, Elena V., Alexandre N. Ermilov, and Alexander M. Dizhoor. "Factors that affect regulation of cGMP synthesis in vertebrate photoreceptors and their genetic link to human retinal degeneration." In Guanylate Cyclase, 139–47. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0927-1_12.

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Pepe, I. M., I. Panfoli, and C. Cugnoli. "Guanylate Cyclase of Retinal Rod Outer Segment." In Sensory Transduction, 139–45. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5841-1_10.

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Bitensky, M. W., D. Torney, A. Yamazaki, M. M. Whalen, and J. S. George. "A Model of the Light Dependent Regulation of Retinal Rod Phosphodiesterase, Guanylate Cyclase and the Cation Flux." In Advances in Experimental Medicine and Biology, 107–21. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-7618-7_9.

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Johnston, Jeffrey P., Jennifer G. Aparicio, and Meredithe L. Applebury. "[44] Purification and autophosphorylation of retinal guanylate cyclase." In Methods in Enzymology, 673–89. Elsevier, 2000. http://dx.doi.org/10.1016/s0076-6879(00)15874-4.

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