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Functional Overlap between Retinitis Pigmentosa 2 Protein and the Tubulin-specific Chaperone Cofactor C
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/cm.970230306openalex-snapshot
Tubulin dimer formation via the release of α‐ and β‐tubulin monomers from multimolecular complexes
inferredcites →https://doi.org/10.1007/978-1-4419-8632-0_41openalex-snapshot
Activation of Toxin ADP-Ribosyltransferases by the Family of ADP-Ribosylation Factors
inferredcites →https://doi.org/10.1016/0092-8674(86)90283-7openalex-snapshot
Sites of microtubule assembly and disassembly in the mitotic spindle
inferredcites →https://doi.org/10.1016/0092-8674(86)90318-1openalex-snapshot
Beyond self-assembly: From microtubules to morphogenesis
inferredcites →https://doi.org/10.1016/0092-8674(92)90622-jopenalex-snapshot
A cytoplasmic chaperonin that catalyzes β-actin folding
inferredcites →https://doi.org/10.1016/0378-1119(95)00037-7openalex-snapshot
Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
inferredcites →https://doi.org/10.1016/s0014-5793(00)01202-3openalex-snapshot
A conserved small GTP‐binding protein Alp41 is essential for the cofactor‐dependent biogenesis of microtubules in fission yeast
inferredcites →https://doi.org/10.1016/s0014-5793(99)00759-0openalex-snapshot
ADP‐ribosylation factor (ARF)‐like 4, 6, and 7 represent a subgroup of the ARF family characterized by rapid nucleotide exchange and a nuclear localization signal
inferredcites →https://doi.org/10.1016/s0014-5793(99)01117-5openalex-snapshot
The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE δ, interacts with the Arf‐like protein Arl3 in a GTP specific manner
inferredcites →https://doi.org/10.1016/s0021-9258(17)32257-3openalex-snapshot
ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of GTP-binding proteins cloned from human and rat tissues.
inferredcites →https://doi.org/10.1016/s0092-8674(00)80100-2openalex-snapshot
Pathway Leading to Correctly Folded β-Tubulin
inferredcites →https://doi.org/10.1016/s0171-9335(99)80011-9openalex-snapshot
Mutations in the PILZ group genes disrupt the microtubule cytoskeleton and uncouple cell cycle progression from cell division in Arabidopsis embryo and endosperm
inferredcites →https://doi.org/10.1016/s0962-8924(97)01168-9openalex-snapshot
The α- and β-tubulin folding pathways
inferredcites →https://doi.org/10.1016/s0968-0004(98)01224-9openalex-snapshot
GTPase-activating proteins: helping hands to complement an active site
inferredcites →https://doi.org/10.1021/bi00086a034openalex-snapshot
Treatment of T cells with 2-hydroxymyristic acid inhibits the myristoylation and alters the stability of p56lck
inferredcites →https://doi.org/10.1038/1214openalex-snapshot
Positional cloning of the gene for X-linked retinitis pigmentosa 2
inferredcites →https://doi.org/10.1038/348125a0openalex-snapshot
The GTPase superfamily: a conserved switch for diverse cell functions
inferredcites →https://doi.org/10.1038/366643a0openalex-snapshot
Proteins regulating Ras and its relatives
inferredcites →https://doi.org/10.1038/ng0596-35openalex-snapshot
A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X–linked retinitis pigmentosa (RP3)
inferredcites →https://doi.org/10.1038/nsb0698-451openalex-snapshot
Tubulin and FtsZ form a distinct family of GTPases
inferredcites →https://doi.org/10.1073/pnas.70.3.765openalex-snapshot
Microtubule Assembly in the Absence of Added Nucleotides
inferredcites →https://doi.org/10.1073/pnas.88.8.3120openalex-snapshot
The arflike gene encodes an essential GTP-binding protein in Drosophila.
inferredcites →https://doi.org/10.1073/pnas.90.19.8952openalex-snapshot
Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes.
inferredcites →https://doi.org/10.1073/pnas.96.4.1315openalex-snapshot
The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase
inferredcites →https://doi.org/10.1074/jbc.270.41.23910openalex-snapshot
Quasi-native Chaperonin-bound Intermediates in Facilitated Protein Folding
inferredcites →https://doi.org/10.1074/jbc.273.25.15872openalex-snapshot
Phospholipid- and GTP-dependent Activation of Cholera Toxin and Phospholipase D by Human ADP-ribosylation Factor-like Protein 1 (HARL1)
inferredcites →https://doi.org/10.1074/jbc.274.34.24054openalex-snapshot
Tubulin Folding Cofactors as GTPase-activating Proteins
inferredcites →https://doi.org/10.1074/jbc.274.39.27553openalex-snapshot
The ARF-like 2 (ARL2)-binding Protein, BART
inferredcites →https://doi.org/10.1074/jbc.m102359200openalex-snapshot
ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) Have Both Specific and Shared Effectors
inferredcites →https://doi.org/10.1074/jbc.m106660200openalex-snapshot
Structures of Yeast ARF2 and ARL1
inferredcites →https://doi.org/10.1083/jcb.124.5.769openalex-snapshot
Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
inferredcites →https://doi.org/10.1083/jcb.138.4.821openalex-snapshot
Tubulin Subunits Exist in an Activated Conformational State Generated and Maintained by Protein Cofactors
inferredcites →https://doi.org/10.1083/jcb.149.5.1087openalex-snapshot
Adp Ribosylation Factor-like Protein 2 (Arl2) Regulates the Interaction of Tubulin-Folding Cofactor D with Native Tubulin
inferredcites →https://doi.org/10.1093/genetics/124.2.251openalex-snapshot
Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function.
inferredcites →https://doi.org/10.1093/genetics/146.3.849openalex-snapshot
Saccharomyces cerevisiae PAC2 Functions With CIN1, 2 and 4 in a Pathway Leading to Normal Microtubule Stability
inferredcites →https://doi.org/10.1093/genetics/156.1.69openalex-snapshot
Function of Tubulin Binding Proteins in Vivo
inferredcites →https://doi.org/10.1093/genetics/156.1.93openalex-snapshot
The Cofactor-Dependent Pathways for α- and β-Tubulins in Microtubule Biogenesis Are Functionally Different in Fission Yeast
inferredcites →https://doi.org/10.1093/hmg/10.11.1177openalex-snapshot
Mutations in the X-linked RP2 gene cause intracellular misrouting and loss of the protein
inferredcites →https://doi.org/10.1093/hmg/5.7.1035openalex-snapshot
Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1
inferredcites →https://doi.org/10.1093/hmg/9.13.1919openalex-snapshot
Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane
inferredcites →https://doi.org/10.1098/rstb.1992.0048openalex-snapshot
Nucleotide hydrolysis regulates the dynamics of actin filaments and microtubules
inferredcites →https://doi.org/10.1105/tpc.12.8.1379openalex-snapshot
The TITAN5 Gene of Arabidopsis Encodes a Protein Related to the ADP Ribosylation Factor Family of GTP Binding Proteins
inferredcites →https://doi.org/10.1128/mcb.10.1.223openalex-snapshot
Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes.
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/9780470015902.a0026333openalex-snapshot
Tubulin Folding and Degradation
inferred← citeshttps://doi.org/10.1002/cm.21255openalex-snapshot
Loss of retinitis pigmentosa 2 ( RP 2) protein affects cone photoreceptor sensory cilium elongation in mice
inferred← citeshttps://doi.org/10.1002/humu.20417openalex-snapshot
Comprehensive survey of mutations in RP2 and RPGR in patients affected with distinct retinal dystrophies: genotype–phenotype correlations and impact on genetic counseling
inferred← citeshttps://doi.org/10.1007/978-0-387-49310-7_11openalex-snapshot
The Role of Hsp70 and Its Co-Chaperones in Protein Misfolding, Aggregation and Disease
inferred← citeshttps://doi.org/10.1007/978-1-4020-8231-3_5openalex-snapshot
The Role of Chaperones and Co-Chaperones in Retinal Degenerative Diseases
inferred← citeshttps://doi.org/10.1007/978-1-4419-1399-9_13openalex-snapshot
Multiprotein Complexes of Retinitis Pigmentosa GTPase Regulator (RPGR), a Ciliary Protein Mutated in X-Linked Retinitis Pigmentosa (XLRP)
inferred← citeshttps://doi.org/10.1007/978-1-4614-0631-0_101openalex-snapshot
Potential Cellular Functions of N-Ethylmaleimide Sensitive Factor in the Photoreceptor
inferred← citeshttps://doi.org/10.1007/978-1-4614-0631-0_66openalex-snapshot
The Role of the X-linked Retinitis Pigmentosa Protein RP2 in Vesicle Traffic and Cilia Function
inferred← citeshttps://doi.org/10.1007/978-1-59745-186-4_14openalex-snapshot
X-Linked Retinal Dystrophies and Microtubular Functions Within the Retina
inferred← citeshttps://doi.org/10.1007/978-3-030-44496-9_3openalex-snapshot
Chaperonin: Protein Folding Machinery in Cells
inferred← citeshttps://doi.org/10.1007/978-3-319-11731-7_12openalex-snapshot
The Role of HSP70 and Its Co-chaperones in Protein Misfolding, Aggregation and Disease
inferred← citeshttps://doi.org/10.1007/s00418-020-01905-6openalex-snapshot
Spatio-temporal distribution of tubulin-binding cofactors and posttranslational modifications of tubulin in the cochlea of mice
inferred← citeshttps://doi.org/10.1007/s12041-009-0061-7openalex-snapshot
RPGR-containing protein complexes in syndromic and non-syndromic retinal degeneration due to ciliary dysfunction
inferred← citeshttps://doi.org/10.1007/s13238-011-1030-5openalex-snapshot
Erratum to: Small GTPases and cilia
inferred← citeshttps://doi.org/10.1016/b978-0-12-370873-1.00052-6openalex-snapshot
The Chlamydomonas Flagellum as a Model for Human Ciliary Disease
inferred← citeshttps://doi.org/10.1016/j.brainresbull.2022.12.005openalex-snapshot
Maintaining essential microtubule bundles in meter-long axons: a role for local tubulin biogenesis?
inferred← citeshttps://doi.org/10.1016/j.cell.2006.12.017openalex-snapshot
Mutations in α-Tubulin Cause Abnormal Neuronal Migration in Mice and Lissencephaly in Humans
inferred← citeshttps://doi.org/10.1016/j.cis.2017.03.004openalex-snapshot
How to gather useful and valuable information from protein binding measurements using Langmuir lipid monolayers
inferred← citeshttps://doi.org/10.1016/j.cub.2009.05.071openalex-snapshot
ASQ2 Encodes a TBCC-like Protein Required for Mother-Daughter Centriole Linkage and Mitotic Spindle Orientation
inferred← citeshttps://doi.org/10.1016/j.exer.2005.10.023openalex-snapshot
Focus on Molecules: X‐linked Retinitis Pigmentosa 2 protein, RP2
inferred← citeshttps://doi.org/10.1016/j.jmb.2005.05.036openalex-snapshot
Properties of the Interaction of Arf-like Protein 2 with PDEδ
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2015.05.003openalex-snapshot
Crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major
inferred← citeshttps://doi.org/10.1016/j.preteyeres.2008.03.001openalex-snapshot
Molecular chaperones and photoreceptor function
inferred← citeshttps://doi.org/10.1016/j.preteyeres.2020.100898openalex-snapshot
The X-linked retinopathies: Physiological insights, pathogenic mechanisms, phenotypic features and novel therapies
inferred← citeshttps://doi.org/10.1016/j.semcdb.2003.12.010openalex-snapshot
Roles of molecular chaperones in protein misfolding diseases
inferred← citeshttps://doi.org/10.1016/j.str.2005.11.008openalex-snapshot
Crystal Structure of the Human Retinitis Pigmentosa 2 Protein and Its Interaction with Arl3
inferred← citeshttps://doi.org/10.1016/j.tcb.2004.10.004openalex-snapshot
Arf-like GTPases: not so Arf-like after all
inferred← citeshttps://doi.org/10.1016/j.tibs.2009.12.007openalex-snapshot
Quality control of cytoskeletal proteins and human disease
inferred← citeshttps://doi.org/10.1016/j.ydbio.2007.08.049openalex-snapshot
The Drosophila Dead end Arf-like3 GTPase controls vesicle trafficking during tracheal fusion cell morphogenesis
inferred← citeshttps://doi.org/10.1016/j.yexcr.2005.12.026openalex-snapshot
The retinitis pigmentosa-mutated RP2 protein exhibits exonuclease activity and translocates to the nucleus in response to DNA damage
inferred← citeshttps://doi.org/10.1016/s0014-5793(02)03766-3openalex-snapshot
Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain
inferred← citeshttps://doi.org/10.1016/s0070-2153(08)00804-1openalex-snapshot
Chapter 4 Ciliary Tubulin and Its Post-Translational Modifications
inferred← citeshttps://doi.org/10.1016/s0076-6879(05)04041-3openalex-snapshot
Assay and Functional Analysis of the ARL3 Effector RP2 Involved in X‐Linked Retinitis Pigmentosa
inferred← citeshttps://doi.org/10.1021/bi049071ropenalex-snapshot
Crystal Structure of the Actin Binding Domain of the Cyclase-Associated Protein
inferred← citeshttps://doi.org/10.1021/bi1005249openalex-snapshot
Interaction and Localization of the Retinitis Pigmentosa Protein RP2 and NSF in Retinal Photoreceptor Cells
inferred← citeshttps://doi.org/10.1021/bi501517ropenalex-snapshot
Lipid Selectivity, Orientation, and Extent of Membrane Binding of Nonacylated RP2
inferred← citeshttps://doi.org/10.1038/embor.2010.5openalex-snapshot
TBCCD1, a new centrosomal protein, is required for centrosome and Golgi apparatus positioning
inferred← citeshttps://doi.org/10.1038/ng1012openalex-snapshot
Mutation of TBCE causes hypoparathyroidism– retardation–dysmorphism and autosomal recessive Kenny–Caffey syndrome
inferred← citeshttps://doi.org/10.1038/nrmicro2009openalex-snapshot
Swimming with protists: perception, motility and flagellum assembly
inferred← citeshttps://doi.org/10.1038/nsmb.1396openalex-snapshot
The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3
inferred← citeshttps://doi.org/10.1038/s41598-023-35950-7openalex-snapshot
Investigation of enzalutamide, docetaxel, and cabazitaxel resistance in the castration resistant prostate cancer cell line C4 using genome-wide CRISPR/Cas9 screening
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Cytokinetic abscission in Toxoplasma gondii is governed by protein phosphatase 2A and the daughter cell scaffold complex
inferred← citeshttps://doi.org/10.1038/srep44465openalex-snapshot
Analysis of RP2 and RPGR Mutations in Five X-Linked Chinese Families with Retinitis Pigmentosa
inferred← citeshttps://doi.org/10.1042/bj20021475openalex-snapshot
Organization on the plasma membrane of the retinitis pigmentosa protein RP2: investigation of association with detergent-resistant membranes and polarized sorting
inferred← citeshttps://doi.org/10.1042/bst20160148openalex-snapshot
Disease mechanisms of X-linked retinitis pigmentosa due to RP2 and RPGR mutations
inferred← citeshttps://doi.org/10.1046/j.1462-5822.2003.00316.xopenalex-snapshot
Abortive infection of Lutzomyia longipalpis insect vectors by aflagellated LdARL-3A-Q70L overexpressing Leishmania amazonensis parasites
inferred← citeshttps://doi.org/10.1074/jbc.m113.509521openalex-snapshot
An Alternative Model for the Role of RP2 Protein in Flagellum Assembly in the African Trypanosome
inferred← citeshttps://doi.org/10.1074/jbc.m116.760314openalex-snapshot
Pathogenic mutations in retinitis pigmentosa 2 predominantly result in loss of RP2 protein stability in humans and zebrafish
inferred← citeshttps://doi.org/10.1074/jbc.m308678200openalex-snapshot
Cytosolic Arl2 Is Complexed with Cofactor D and Protein Phosphatase 2A
inferred← citeshttps://doi.org/10.1080/10253890400019706openalex-snapshot
The Pathology of Cellular Anti-stress Mechanisms: A New Frontier
inferred← citeshttps://doi.org/10.1089/zeb.2012.0761openalex-snapshot
Zebrafish Model for the Genetic Basis of X-Linked Retinitis Pigmentosa
inferred← citeshttps://doi.org/10.1091/mbc.e05-10-0929openalex-snapshot
Arl2 and Arl3 Regulate Different Microtubule-dependent Processes
inferred← citeshttps://doi.org/10.1091/mbc.e12-11-0792openalex-snapshot
The dual role of fission yeast Tbc1/cofactor C orchestrates microtubule homeostasis in tubulin folding and acts as a GAP for GTPase Alp41/Arl2
inferred← citeshttps://doi.org/10.1093/hmg/11.24.3065openalex-snapshot
Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3
inferred← citeshttps://doi.org/10.1093/hmg/ddq012openalex-snapshot
The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium
inferred← citeshttps://doi.org/10.1093/hmg/ddr520openalex-snapshot
The X-linked retinitis pigmentosa protein RP2 facilitates G protein traffic
inferred← citeshttps://doi.org/10.1093/hmg/ddv197openalex-snapshot
Knockout ofRP2decreases GRK1 and rod transducin subunits and leads to photoreceptor degeneration in zebrafish
inferred← citeshttps://doi.org/10.1093/hmg/ddw077openalex-snapshot
ARL3 regulates trafficking of prenylated phototransduction proteins to the rod outer segment
inferred← citeshttps://doi.org/10.1095/biolreprod.115.130575openalex-snapshot
X-Linked Retinitis Pigmentosa 2 Is a Novel Maternal-Effect Gene Required for Left-Right Asymmetry in Zebrafish1
inferred← citeshttps://doi.org/10.1096/fj.14-257915openalex-snapshot
Mistrafficking of prenylated proteins causes retinitis pigmentosa 2
inferred← citeshttps://doi.org/10.1097/01.gim.0000151351.11876.c3openalex-snapshot
Genetic disorders involving molecular-chaperone genes: A perspective
inferred← citeshttps://doi.org/10.1104/pp.16.01240openalex-snapshot
Membrane Proteomic Insights into the Physiology and Taxonomy of an Oleaginous Green Microalga
inferred← citeshttps://doi.org/10.1105/tpc.17.00440openalex-snapshot
DISTAG/TBCCd1 Is Required for Basal Cell Fate Determination in Ectocarpus
inferred← citeshttps://doi.org/10.1111/j.1600-0854.2007.00611.xopenalex-snapshot
An Essential Quality Control Mechanism at the Eukaryotic Basal Body Prior to Intraflagellar Transport
inferred← citeshttps://doi.org/10.1111/tra.12072openalex-snapshot
Rab and Arf Proteins in Genetic Diseases
inferred← citeshttps://doi.org/10.1126/science.ady2708openalex-snapshot
Structural dissection of αβ-tubulin heterodimer assembly and disassembly by human tubulin–specific chaperones
inferred← citeshttps://doi.org/10.1136/bjo.2003.027979openalex-snapshot
An atypical phenotype of macular and peripapillary retinal atrophy caused by a mutation in the RP2 gene
inferred← citeshttps://doi.org/10.1142/s0219720015500286openalex-snapshot
HPMV: Human protein mutation viewer — relating sequence mutations to protein sequence architecture and function changes
inferred← citeshttps://doi.org/10.1146/annurev.cellbio.23.090506.123209openalex-snapshot
The Small G Proteins of the Arf Family and Their Regulators
inferred← citeshttps://doi.org/10.1152/ajpcell.00188.2020openalex-snapshot
ARF family GTPases with links to cilia
inferred← citeshttps://doi.org/10.1167/iovs.02-0882openalex-snapshot
Spectrum and Range of Oxidative Stress Responses of Human Lens Epithelial Cells to H2O2 Insult
inferred← citeshttps://doi.org/10.1167/iovs.07-0071openalex-snapshot
A Population-Based Epidemiological and Genetic Study of X-Linked Retinitis Pigmentosa
inferred← citeshttps://doi.org/10.1167/iovs.13-12140openalex-snapshot
Ablation of the X-Linked Retinitis Pigmentosa 2 ( Rp2 ) Gene in Mice Results in Opsin Mislocalization and Photoreceptor Degeneration
inferred← citeshttps://doi.org/10.1167/iovs.14-16066openalex-snapshot
Membrane Protein Transport in Photoreceptors: The Function of PDE
inferred← citeshttps://doi.org/10.1186/1471-2105-4-46openalex-snapshot
Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization
inferred← citeshttps://doi.org/10.1186/1471-2407-10-135openalex-snapshot
Tubulin binding cofactor C (TBCC) suppresses tumor growth and enhances chemosensitivity in human breast cancer cells
inferred← citeshttps://doi.org/10.1186/1745-6150-5-66openalex-snapshot
Bayesian classification of residues associated with protein functional divergence: Arf and Arf-like GTPases
inferred← citeshttps://doi.org/10.1242/jcs.01719openalex-snapshot
Identification of a novel tubulin-destabilizing protein related to the chaperone cofactor E
inferred← citeshttps://doi.org/10.1242/jcs.070839openalex-snapshot
Localization of retinitis pigmentosa 2 to cilia is regulated by Importin β2
inferred← citeshttps://doi.org/10.1242/jcs.136515openalex-snapshot
Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation
inferred← citeshttps://doi.org/10.1371/journal.pone.0021379openalex-snapshot
Functional Analysis of Retinitis Pigmentosa 2 (RP2) Protein Reveals Variable Pathogenic Potential of Disease-Associated Missense Variants
inferred← citeshttps://doi.org/10.1371/journal.pone.0025912openalex-snapshot
The Solution Structure of the N-Terminal Domain of Human Tubulin Binding Cofactor C Reveals a Platform for Tubulin Interaction
inferred← citeshttps://doi.org/10.1515/bmc.2010.033openalex-snapshot
Revisiting the tubulin folding pathway: new roles in centrosomes and cilia
inferred← citeshttps://doi.org/10.1517/14728220903225016openalex-snapshot
RPGR and RP2: targets for the treatment of X-linked retinitis pigmentosa?
inferred← citeshttps://doi.org/10.21203/rs.3.rs-10732337/v1openalex-snapshot
TAOK3 marks an invasion‑competent epithelial subset in cervical cancer, and its inhibition restrains tumor growth, sensitizes to paclitaxel, and remodels the immune microenvironment
inferred← citeshttps://doi.org/10.2147/rrb.s57087openalex-snapshot
Role of small GTPases in polarized vesicle transport to primary cilium
inferred← citeshttps://doi.org/10.21561/jor.2024.9.1.81openalex-snapshot
Retinal Dystrophy Associated with a Novel RP2 Exon1 Deletion with Simultaneous TGFBI Point Mutation in Two Male Siblings: Case Report
inferred← citeshttps://doi.org/10.2174/1389203724666230915123217openalex-snapshot
ARL15 and its Multiple Disease Association: Emerging Functions and Potential Therapeutic Application
inferred← citeshttps://doi.org/10.32657/10356/73545openalex-snapshot
Amino acids stimulate the endosome-to-golgi trafficking through ragulator and small GTPase Arl5
inferred← citeshttps://doi.org/10.3389/fcell.2021.720782openalex-snapshot
A Novel ARL3 Gene Mutation Associated With Autosomal Dominant Retinal Degeneration
inferred← citeshttps://doi.org/10.3389/fgene.2019.00323openalex-snapshot
Structural but Not Functional Alterations in Cones in the Absence of the Retinal Disease Protein Retinitis Pigmentosa 2 (RP2) in a Cone-Only Retina
inferred← citeshttps://doi.org/10.3390/genes14010074openalex-snapshot
Genetic Diagnosis for 64 Patients with Inherited Retinal Disease
inferred← citeshttps://doi.org/10.3390/ijms252212301openalex-snapshot
TBCC Domain-Containing Protein Regulates Sporulation and Virulence of Phytophthora capsici via Nutrient-Responsive Signaling
inferred← citeshttps://doi.org/10.3390/jcm14030898openalex-snapshot
Pre-Clinical and Clinical Advances in Gene Therapy of X-Linked Retinitis Pigmentosa: Hope on the Horizon
inferred← citeshttps://doi.org/10.33915/etd.6979openalex-snapshot
Complex Regulation of Protein Trafficking and Photoreceptor Cell Development by Small GTPases
inferred← citeshttps://doi.org/10.5301/ejo.5000879openalex-snapshot
Novel Variants of RPGR in X-Linked Retinitis Pigmentosa Families and Genotype-Phenotype Correlation
inferred← citeshttps://doi.org/10.5772/48387openalex-snapshot
Photoreceptor Sensory Cilium and Associated Disorders
inferred← citeshttps://doi.org/10.64898/2026.07.04.736128openalex-snapshot
TAOK3 inhibition constrains invasion, potentiates paclitaxel, and reprograms the tumor microenvironment toward anti-tumor immunity in cervical cancer
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