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Leucine Rich Repeat Proteins: Sequences, Mutations, Structures and Diseases

Matsushima, Norio, Takatsuka, Shintaro, Miyashita, Hiroki, Kretsinger, Robert H.·2019·Protein & Peptide Letters
DOI 10.2174/0929866526666181208170027
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Abstract

Mutations in the genes encoding Leucine Rich Repeat (LRR) containing proteins are associated with over sixty human diseases; these include high myopia, mitochondrial encephalomyopathy, and Crohn’s disease. These mutations occur frequently within the LRR domains and within the regions that shield the hydrophobic core of the LRR domain. The amino acid sequences of fifty-five LRR proteins have been published. They include Nod-Like Receptors (NLRs) such as NLRP1, NLRP3, NLRP14, and Nod-2, Small Leucine Rich Repeat Proteoglycans (SLRPs) such as keratocan, lumican, fibromodulin, PRELP, biglycan, and nyctalopin, and F-box/LRR-repeat proteins such as FBXL2, FBXL4, and FBXL12. For example, 363 missense mutations have been identified. Replacement of arginine, proline, or cysteine by another amino acid, or the reverse, is frequently observed. The diverse effects of the mutations are discussed based on the known structures of LRR proteins. These mutations influence protein folding, aggregation, oligomerization, stability, protein-ligand interactions, disulfide bond formation, and glycosylation. Most of the mutations cause loss of function and a few, gain of function.

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  1. Kobe B, Deisenhofer J. The leucine-rich repeat: A versatile binding motif. · DOI
  2. Miyashita H, Kuroki Y, Matsushima N. Novel leucine rich repeat domains in proteins from unicellular eukaryotes and bacteria. · DOI
  3. Kobe B, Kajava AV. The leucine-rich repeat as a protein recognition motif. · DOI
  4. Matsushima N, Miyashita H, Mikami T, Kuroki Y. A nested leucine rich repeat (LRR) domain: The precursor of LRRs is a ten or eleven residue motif. · DOI
  5. Enkhbayar P, Miyashita H, Kretsinger R, Matsushima N. Helical parameters and correlations of tandem leucine rich repeats in proteins. · DOI
  6. Bella J, Hindle KL, McEwan PA, Lovell SC. The leucine-rich repeat structure. · DOI
  7. Ng AC, Eisenberg JM, Heath RJ, Huett A, Robinson CM, Nau GJ, Xavier RJ. Human leucine-rich repeat proteins: A genome-wide bioinformatic categorization and functional analysis in innate immunity. · DOI
  8. Matsushima N, Tachi N, Kuroki Y, Enkhbayar P, Osaki M, Kamiya M, Kretsinger RH. Structural analysis of leucine-rich-repeat variants in proteins associated with human diseases. · DOI
  9. Desai SS, Roy BS, Mahale SD. Mutations and polymorphisms in FSH receptor: Functional implications in human reproduction. · DOI
  10. Kleinau G, Worth CL, Kreuchwig A, Biebermann H, Marcinkowski P, Scheerer P, Krause G. Structural-functional features of the thyrotropin receptor: A class A G-protein-coupled receptor at work. · DOI
  11. Li R, Emsley J. The organizing principle of the platelet glycoprotein Ib-IX-V complex. · DOI
  12. Domene HM, Hwa V, Jasper HG, Rosenfeld RG. Acid-labile subunit (ALS) deficiency. · DOI
  13. Fritz JH, Ferrero RL, Philpott DJ, Girardin SE. Nod-like proteins in immunity, inflammation and disease. · DOI
  14. Steimle V, Otten LA, Zufferey M, Mach B. Complementation cloning of an MHC class II transactivator mutated in hereditary MHC class II deficiency (or bare lymphocyte syndrome). · DOI
  15. Bontron S, Steimle V, Ucla C, Eibl MM, Mach B. Two novel mutations in the MHC class II transactivator CIITA in a second patient from MHC class II deficiency complementation group A. · DOI
  16. Dziembowska M, Fondaneche MC, Vedrenne J, Barbieri G, Wiszniewski W, Picard C, Cant AJ, Steimle V, Charron D, Alca-Loridan C, Fischer A, Lisowska-Grospierre B. Three novel mutations of the CIITA gene in MHC class II-deficient patients with a severe immunodeficiency. · DOI
  17. Peijnenburg A, Van den Berg R, Van Eggermond MJ, Sanal O, Vossen JM, Lennon AM, Alcaide-Loridan C, Van den Elsen PJ. Defective MHC class II expression in an MHC class II deficiency patient is caused by a novel deletion of a splice donor site in the MHC class II transactivator gene. · DOI
  18. Grandemange S, Sanchez E, Louis-Plence P, Tran Mau-Them F, Bessis D, Coubes C, Frouin E, Seyger M, Girard M, Puechberty J, Costes V, Rodière M, Carbasse A, Jeziorski E, Portales P, Sarrabay G, Mondain M, Jorgensen C, Apparailly F, Hoppenreijs E, Touitou I, Geneviève D. A new autoinflammatory and autoimmune syndrome associated with NLRP1 mutations: NAIAD (NLRP1-associated autoinflammation with arthritis and dyskeratosis). · DOI
  19. Levandowski CB, Mailloux CM, Ferrara TM, Gowan K, Ben S, Jin Y, McFann KK, Holland PJ, Fain PR, Dinarello CA, Spritz RA. NLRP1 haplotypes associated with vitiligo and autoimmunity increase interleukin-1beta processing the NLRP1 inflammasome. · DOI
  20. Zhong FL, Mamai O, Sborgi L, Boussofara L, Hopkins R, Robinson K, Szeverenyi I, Takeichi T, Balaji R, Lau A, Tye H, Roy K, Bonnard C, Ahl PJ, Jones LA, Baker PJ, Lacina L, Otsuka A, Fournie PR, Malecaze F, Lane EB, Akiyama M, Kabashima K, Connolly JE, Masters SL, Soler VJ, Omar SS, McGrath JA, Nedelcu R, Gribaa M, Denguezli M, Saad A, Hiller S, Reversade B. Germline NLRP1 mutations cause skin inflammatory and cancer susceptibility syndromes inflammasome activation. · DOI · Paper page
  21. Frenkel J, van Kempen MJ, Kuis W, van Amstel HK. Variant chronic infantile neurologic, cutaneous, articular syndrome due to a mutation within the leucine-rich repeat domain of CIAS1. · DOI
  22. Kubota K, Ohnishi H, Teramoto T, Matsui E, Murase K, Kanoh H, Kato Z, Kaneko H, Seishima M, Kondo N. analysis of the functional effects of an NLRP3 G809S variant with the co-existence of MEFV haplotype variants in atypical autoinflammatory syndrome. · DOI
  23. Wang CM, Dixon PH, Decordova S, Hodges MD, Sebire NJ, Ozalp S, Fallahian M, Sensi A, Ashrafi F, Repiska V, Zhao J, Xiang Y, Savage PM, Seckl MJ, Fisher RA. Identification of 13 novel NLRP7 mutations in 20 families with recurrent hydatidiform mole; missense mutations cluster in the leucine-rich region. · DOI
  24. Murdoch S, Djuric U, Mazhar B, Seoud M, Khan R, Kuick R, Bagga R, Kircheisen R, Ao A, Ratti B, Hanash S, Rouleau GA, Slim R. Mutations in NALP7 cause recurrent hydatidiform moles and reproductive wastage in humans. · DOI
  25. Nguyen NM, Slim R. Genetics and epigenetics of recurrent hydatidiform moles: Basic science and genetic counselling. · DOI
  26. Westerveld GH, Korver CM, van Pelt AM, Leschot NJ, van der Veen F, Repping S, Lombardi MP. Mutations in the testis-specific NALP14 gene in men suffering from spermatogenic failure. · DOI
  27. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N. Szabo, S.; Buckhaults, P.; Farrell, C.; Meeh, P.; Markowitz, S.D.; Willis, J.; Dawson, D.; Willson, J.K.; Gazdar, A.F.; Hartigan, J.; Wu, L.; Liu, C.; Parmigiani, G.; Park, B.H.; Bachman, K.E.; Papadopoulos, N.; Vogelstein, B.; Kinzler, K.W.; Velculescu, V.E. The consensus coding sequences of human breast and colorectal cancers. · DOI
  28. Ogura Y, Bonen DK, Inohara N, Nicolae DL, Chen FF, Ramos R, Britton H, Moran T, Karaliuskas R, Duerr RH, Achkar JP, Brant SR, Bayless TM, Kirschner BS, Hanauer SB, Nuñez G, Cho JH. A frameshift mutation in NOD2 associated with susceptibility to Crohn’s disease. · DOI · Paper page
  29. Hugot JP, Chamaillard M, Zouali H, Lesage S, Cezard JP, Belaiche J, Almer S, Tysk C, O’Morain CA, Gassull M, Binder V, Finkel Y, Cortot A, Modigliani R, Laurent-Puig P, Gower-Rousseau C, Macry J, Colombel JF, Sahbatou M, Thomas G. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn’s disease. · DOI · Paper page
  30. Hampe J. Cuthbert. A.; Croucher. P.J.; Mirza. M.M.; Mascheretti, S.; Fisher, S.; Frenzel, H.; King, K.; Hasselmeyer, A.; MacPherson, A.J.; Bridger, S.; van Deventer, S.; Forbes, A.; Nikolaus, S.; Lennard-Jones, J.E.; Foelsch, U.R.; Krawczak, M.; Lewis, C.; Schreiber, S.; Mathew, C.G. Association between insertion mutation in NOD2 gene and Crohn’s disease in German and British populations. · DOI
  31. Lakatos PL, Lakatos L, Szalay F, Willheim-Polli C, Osterreicher C, Tulassay Z, Molnar T, Reinisch W. Papp, J/; Mozsik, G.; Ferenci. P.; Hungarian IBD Study Group. Toll-like receptor 4 and NOD2/CARD15 mutations in Hungarian patients with Crohn’s disease: phenotype-genotype correlations. · DOI
  32. Girardelli M, Vuch J, Tommasini A, Crovella S, Bianco AM. Novel missense mutation in the NOD2 gene in a patient with early onset ulcerative colitis: Causal or chance association? · DOI
  33. Motta V, Soares F, Sun T, Philpott DJ. NOD-like receptors: Versatile cytosolic sentinels. · DOI
  34. Gai X, Ghezzi D, Johnson MA, Biagosch CA, Shamseldin HE, Haack TB, Reyes A, Tsukikawa M, Sheldon CA, Srinivasan S, Gorza M, Kremer LS, Wieland T, Strom TM, Polyak E, Place E, Consugar M, Ostrovsky J, Vidoni S, Robinson AJ, Wong LJ, Sondheimer N, Salih MA, Al-Jishi E, Raab CP, Bean C, Furlan F, Parini R, Lamperti C, Mayr JA, Konstantopoulou V, Huemer M, Pierce EA, Meitinger T, Freisinger P, Sperl W, Prokisch H, Alkuraya FS, Falk MJ, Zeviani M. Mutations in FBXL4, encoding a mitochondrial protein, cause early-onset mitochondrial encephalomyopathy. · DOI
  35. Huemer M, Karall D, Schossig A, Abdenur JE, Al Jasmi F, Biagosch C, Distelmaier F, Freisinger P, Graham BH, Haack TB. Hauser. N.; Hertecant, J.; Ebrahimi-Fakhari, D.; Konstantopoulou, V.; Leydiker, K.; Lourenco, C.M.; Scholl-Bürgi, S.; Wilichowski, E.; Wolf, N.I.; Wortmann, S.B.; Taylor, R.W.; Mayr, J.A.; Bonnen, P.E.; Sperl, W.; Prokisch, H.; McFarland, R. Clinical, morphological, biochemical, imaging and outcome parameters in 21 individuals with mitochondrial maintenance defect related to FBXL4 mutations. · DOI
  36. Baroy T, Pedurupillay CR, Bliksrud YT, Rasmussen M, Holmgren A, Vigeland MD, Hughes T, Brink M. Rodenburg, R.; Nedregaard, B.; Strømme, P.; Frengen, E.; Misceo, D. A novel mutation in FBXL4 in a Norwegian child with encephalomyopathic mitochondrial DNA depletion syndrome 13. · DOI
  37. van Rij MC, Jansen FA, Hellebrekers DM, Onkenhout W, Smeets HJ, Hendrickx AT, Gottschalk RW, Steggerda SJ, Peeters-Scholte CM, Haak MC, Hilhorst-Hofstee Y. Polyhydramnios and cerebellar atrophy: A prenatal presentation of mitochondrial encephalomyopathy caused by mutations in the FBXL4 gene. · DOI
  38. Bonnen PE, Yarham JW, Besse A, Wu P, Faqeih EA, Al-Asmari AM, Saleh MA, Eyaid W, Hadeel A, He L, Smith F, Yau S, Simcox EM, Miwa S, Donti T, Abu-Amero KK, Wong LJ, Craigen WJ, Graham BH, Scott KL, McFarland R, Taylor RW. Mutations in FBXL4 cause mitochondrial encephalopathy and a disorder of mitochondrial DNA maintenance. · DOI
  39. El-Hattab AW, Dai H, Almannai M, Wang J, Faqeih EA, Al Asmari A, Saleh MAM, Elamin MAO, Alfadhel M, Alkuraya FS. Hashem. M.; Aldosary, M.S.; Almass, R.; Almutairi, F.B.; Alsagob, M.; Al-Owain, M.; Al-Sharfa, S.; Al-Hassnan, Z.N.; Rahbeeni, Z.; Al-Muhaizea, M.A.; Makhseed, N.; Foskett, G.K.; Stevenson, D.A.; Gomez-Ospina, N.; Lee, C.; Boles, R.G.; Schrier Vergano, S.A.; Wortmann, S.B.; Sperl, W.; Opladen, T.; Hoffmann, G.F.; Hempel, M.; Prokisch, H.; Alhaddad, B.; Mayr, J.A.; Chan, W.; Kaya, N.; Wong, L.C. Molecular and clinical spectra of FBXL4 deficiency. · DOI
  40. Varela I, Tarpey P, Raine K, Huang D, Ong CK, Stephens P, Davies H, Jones D, Lin ML, Teague J, Bignell G, Butler A, Cho J, Dalgliesh GL, Galappaththige D, Greenman C, Hardy C, Jia M, Latimer C, Lau KW, Marshall J, McLaren S, Menzies A, Mudie L, Stebbings L, Largaespada DA, Wessels LF, Richard S, Kahnoski RJ, Anema J, Tuveson DA, Perez-Mancera PA, Mustonen V, Fischer A, Adams DJ, Rust A, Chan-on W, Subimerb C, Dykema K, Furge K, Campbell PJ, The BT, Stratton MR, Futreal PA. Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma. · DOI
  41. Kuchay S, Duan S, Schenkein E, Peschiaroli A, Saraf A, Florens L, Washburn MP, Pagano M. FBXL2- and PTPL1-mediated degradation of p110-free p85beta regulatory subunit controls the PI(3)K signalling cascade. · DOI
  42. Chen BB, Glasser JR, Coon TA, Mallampalli RK. F-box protein FBXL2 exerts human lung tumor suppressor-like activity by ubiquitin-mediated degradation of cyclin D3 resulting in cell cycle arrest. · DOI
  43. Chen BB, Glasser JR, Coon TA, Zou C, Miller HL, Fenton M, McDyer JF, Boyiadzis M, Mallampalli RK. F-box protein FBXL2 targets cyclin D2 for ubiquitination and degradation to inhibit leukemic cell proliferation. · DOI
  44. Xing W, Busino L, Hinds TR, Marionni ST, Saifee NH, Bush MF, Pagano M, Zheng N. SCF(FBXL3) ubiquitin ligase targets cryptochromes at their cofactor pocket. · DOI · Paper page
  45. Sinibaldi L, De Luca A, Bellacchio E, Conti E, Pasini A, Paloscia C, Spalletta G, Caltagirone C, Pizzuti A, Dallapiccola B. Mutations of the Nogo-66 receptor (RTN4R) gene in schizophrenia. · DOI
  46. Hsu R, Woodroffe A, Lai WS, Cook MN, Mukai J, Dunning JP, Swanson DJ, Roos JL, Abecasis GR, Karayiorgou M, Gogos JA. Nogo Receptor 1 (RTN4R) as a candidate gene for schizophrenia: Analysis using human and mouse genetic approaches. · DOI
  47. Budel S, Padukkavidana T, Liu BP, Feng Z, Hu F, Johnson S, Lauren J, Park JH, McGee AW, Liao J, Stillman A, Kim JE, Yang BZ, Sodi S, Gelernter J, Zhao H, Hisama F, Arnsten AF, Strittmatter SM. Genetic variants of Nogo-66 receptor with possible association to schizophrenia block myelin inhibition of axon growth. · DOI · Paper page
  48. Kimura H, Fujita Y, Kawabata T, Ishizuka K, Wang C, Iwayama Y, Okahisa Y, Kushima I, Morikawa M, Uno Y, Okada T, Ikeda M, Inada T, Branko A, Mori D, Yoshikawa T, Iwata N, Nakamura H, Yamashita T, Ozaki N. A novel rare variant R292H in RTN4R affects growth cone formation and possibly contributes to schizophrenia susceptibility. · DOI
  49. Lazar NL, Singh S, Paton T, Clapcote SJ, Gondo Y, Fukumura R, Roder JC, Cain DP. Missense mutation of the reticulon-4 receptor alters spatial memory and social interaction in mice. · DOI
  50. Thomas RA, Ambalavanan A, Rouleau GA, Barker PA. Identification of genetic variants of LGI1 and RTN4R (NgR1) linked to schizophrenia that are defective in NgR1-LGI1 signaling. · DOI
  51. Nobile C, Michelucci R, Andreazza S, Pasini E, Tosatto SC, Striano P. LGI1 mutations in autosomal dominant and sporadic lateral temporal epilepsy. · DOI
  52. Sirerol-Piquer MS, Ayerdi-Izquierdo A, Morante-Redolat JM, Herranz-Perez V, Favell K, Barker PA, Perez-Tur J. The epilepsy gene LGI1 encodes a secreted glycoprotein that binds to the cell surface. · DOI
  53. Chabrol E, Popescu C, Gourfinkel-An I, Trouillard O, Depienne C, Senechal K, Baulac M, LeGuern E, Baulac S. Two novel epilepsy-linked mutations leading to a loss of function of LGI1. · DOI
  54. Gu W, Brodtkorb E, Steinlein OK. LGI1 is mutated in familial temporal lobe epilepsy characterized by aphasic seizures. · DOI
  55. Pizzuti A, Flex E, Di Bonaventura C, Dottorini T, Egeo G, Manfredi M, Dallapiccola B, Giallonardo AT. Epilepsy with auditory features: A LGI1 gene mutation suggests a loss-of-function mechanism. · DOI
  56. Berkovic SF, Izzillo P, McMahon JM, Harkin LA, McIntosh AM, Phillips HA, Briellmann RS, Wallace RH, Mazarib A, Neufeld MY, Korczyn AD, Scheffer IE, Mulley JC. LGI1 mutations in temporal lobe epilepsies. · DOI
  57. Michelucci R, Mecarelli O, Bovo G, Bisulli F, Testoni S, Striano P, Striano S, Tinuper P, Nobile C. A de novo LGI1 mutation causing idiopathic partial epilepsy with telephone-induced seizures. · DOI
  58. Striano P, de Falco A, Diani E, Bovo G, Furlan S, Vitiello L, Pinardi F, Striano S, Michelucci R, de Falco FA, Nobile C. A novel loss-of-function LGI1 mutation linked to autosomal dominant lateral temporal epilepsy. · DOI
  59. de Bellescize J, Boutry N, Chabrol E, Andre-Obadia N, Arzimanoglou A, Leguern E, Baulac S, Calender A, Ryvlin P, Lesca G. A novel three base-pair LGI1 deletion leading to loss of function in a family with autosomal dominant lateral temporal epilepsy and migraine-like episodes. · DOI
  60. Di Bonaventura C, Carni M, Diani E, Fattouch J, Vaudano EA, Egeo G, Pantano P, Maraviglia B, Bozzao L, Manfredi M, Prencipe M, Giallonardo TA, Nobile C. Drug resistant ADLTE and recurrent partial status epilepticus with dysphasic features in a family with a novel LGI1mutation: Electroclinical, genetic, and EEG/fMRI findings. · DOI
  61. Kalachikov S, Evgrafov O, Ross B, Winawer M, Barker-Cummings C, Martinelli Boneschi F, Choi C, Morozov P, Das K, Teplitskaya E, Yu A, Cayanis E, Penchaszadeh G, Kottmann AH, Pedley TA, Hauser WA, Ottman R, Gilliam TC. Mutations in LGI1 cause autosomal-dominant partial epilepsy with auditory features. · DOI
  62. Ottman R, Winawer MR, Kalachikov S, Barker-Cummings C, Gilliam TC, Pedley TA, Hauser WA. LGI1 mutations in autosomal dominant partial epilepsy with auditory features. · DOI
  63. Sadleir LG, Agher D, Chabrol E, Elkouby L, Leguern E, Paterson SJ, Harty R, Bellows ST, Berkovic SF, Scheffer IE, Baulac S. Seizure semiology in autosomal dominant epilepsy with auditory features, due to novel LGI1 mutations. · DOI
  64. Di Bonaventura C, Operto FF, Busolin G, Egeo G, D’Aniello A, Vitello L, Smaniotto G, Furlan S, Diani E, Michelucci R, Giallonardo AT, Coppola G, Nobile C. Low penetrance and effect on protein secretion of LGI1 mutations causing autosomal dominant lateral temporal epilepsy. · DOI
  65. Hedera P, Abou-Khalil B, Crunk AE, Taylor KA, Haines JL, Sutcliffe JS. Autosomal dominant lateral temporal epilepsy: two families with novel mutations in the LGI1 gene. · DOI
  66. Pisano T, Marini C, Brovedani P, Brizzolara D, Pruna D, Mei D, Moro F, Cianchetti C, Guerrini R. Abnormal phonologic processing in familial lateral temporal lobe epilepsy due to a new LGI1 mutation. · DOI
  67. Michelucci R, Poza JJ, Sofia V, de Feo MR, Binelli S, Bisulli F, Scudellaro E, Simionati B, Zimbello R, D’Orsi G, Passarelli D, Avoni P, Avanzini G, Tinuper P, Biondi R, Valle G, Mautner VF, Stephani U. Autosomal dominant lateral temporal epilepsy: Clinical spectrum, new epitempin mutations, and genetic heterogeneity in seven European families. · DOI
  68. Klein KM, Pendziwiat M, Cohen R, Appenzeller S, de Kovel CG, Rosenow F, Koeleman BP, Kuhlenbaumer G, Sheintuch L, Veksler R, Friedman A, Afawi Z, Helbig I. Autosomal dominant epilepsy with auditory features: A new LGI1 family including a phenocopy with cortical dysplasia. · DOI
  69. Dazzo E, Santulli L, Posar A, Fattouch J, Conti S, Loden-van Straaten M, Mijalkovic J, De Bortoli M, Rosa M, Millino C, Pacchioni B, Di Bonaventura C, Giallonardo AT, Striano S, Striano P, Parmeggiani A, Nobile C. Autosomal dominant lateral temporal epilepsy (ADLTE): Novel structural and single-nucleotide LGI1 mutations in families with predominant visual auras. · DOI
  70. Fertig E, Lincoln A, Martinuzzi A, Mattson RH, Hisama FM. Novel LGI1 mutation in a family with autosomal dominant partial epilepsy with auditory features. · DOI
  71. Kawamata J, Ikeda A, Fujita Y, Usui K, Shimohama S, Takahashi R. Mutations in LGI1 gene in Japanese families with autosomal dominant lateral temporal lobe epilepsy: The first report from Asian families. · DOI
  72. Heiman GA, Kamberakis K, Gill R, Kalachikov S, Pedley TA, Hauser WA, Ottman R. Evaluation of depression risk in LGI1 mutation carriers. · DOI
  73. Fumoto N, Matsumoto R, Kawamata J, Koyasu S, Kondo T, Kitamura A, Koshiba Y, Kinoshita M, Kawasaki J, Yamashita H, Takahashi R, Ikeda A. Novel LGI1 mutation in a Japanese autosomal dominant lateral temporal lobe epilepsy family. · DOI
  74. Yokoi N, Fukata Y, Kase D, Miyazaki T, Jaegle M, Ohkawa T, Takahashi N, Iwanari H, Mochizuki Y, Hamakubo T, Imoto K, Meijer D, Watanabe M, Fukata M. Chemical corrector treatment ameliorates increased seizure susceptibility in a mouse model of familial epilepsy. · DOI
  75. Matsubara Y, Murata M, Moriki T, Yokoyama K, Watanabe N, Nakajima H, Handa M, Kawano K, Aoki N, Yoshino H, Ikeda Y. A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within the leucine-rich repeat sequence of platelet glycoprotein Ibalpha. · DOI
  76. Matsubara Y, Murata M, Sugita K, Ikeda Y. Identification of a novel point mutation in platelet glycoprotein Ibalpha, Gly to Ser at residue 233, in a Japanese family with platelet-type von Willebrand disease. · DOI
  77. Murata M, Furihata K, Ishida F, Russell SR, Ware J, Ruggeri ZM. Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness. · DOI
  78. Miller JL, Lyle VA, Cunningham D. Mutation of leucine-57 to phenylalanine in a platelet glycoprotein Ib alpha leucine tandem repeat occurring in patients with an autosomal dominant variant of Bernard-Soulier disease. · DOI
  79. Ware J, Russell SR, Marchese P, Murata M, Mazzucato M, De Marco L, Ruggeri ZM. Point mutation in a leucine-rich repeat of platelet glycoprotein Ib alpha resulting in the Bernard-Soulier syndrome. · DOI
  80. Simsek S, Noris P, Lozano M, Pico M, von dem Borne AE, Ribera A, Gallardo D. Cys209 Ser mutation in the platelet membrane glycoprotein Ib alpha gene is associated with Bernard-Soulier syndrome. · DOI
  81. Miller JL, Cunningham D, Lyle VA, Finch CN. Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease. · DOI
  82. Murata M, Russell SR, Ruggeri ZM, Ware J. Expression of the phenotypic abnormality of platelet-type von Willebrand disease in a recombinant glycoprotein Ib alpha fragment. · DOI
  83. Russell SD, Roth GJ. Pseudo-von Willebrand disease: A mutation in the platelet glycoprotein Ib alpha gene associated with a hyperactive surface receptor. · DOI
  84. Ishida F, Furihata K, Ishida K, Yan J, Kitano K, Kiyosawa K, Furuta S. The largest variant of platelet glycoprotein Ib alpha has four tandem repeats of 13 amino acids in the macroglycopeptide region and a genetic linkage with methionine145. · DOI
  85. de la Salle C, Baas MJ, Lanza F, Schwartz A, Hanau D, Chevalier J, Gachet C, Briquel ME, Cazenave JP. A three-base deletion removing a leucine residue in a leucine-rich repeat of platelet glycoprotein Ib alpha associated with a variant of Bernard-Soulier syndrome (Nancy I). · DOI
  86. Kenny D, Jonsson OG, Morateck PA, Montgomery RR. Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein. · DOI
  87. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES. Characterization of single-nucleotide polymorphisms in coding regions of human genes. · DOI · Paper page
  88. Koskela S, Partanen J, Salmi TT, Kekomaki R. Molecular characterization of two mutations in platelet glycoprotein (GP) Ib alpha in two Finnish Bernard-Soulier syndrome families. · DOI
  89. Savoia A, Balduini CL, Savino M, Noris P, Del Vecchio M, Perrotta S, Belletti S, Poggi Iolascon A. Autosomal dominant macrothrombocytopenia in Italy is most frequently a type of heterozygous Bernard-Soulier syndrome. · DOI
  90. Vettore S, Scandellari R, Moro S, Lombardi AM, Scapin M, Randi ML, Fabris F. Novel point mutation in a leucine-rich repeat of the GPIbalpha chain of the platelet von Willebrand factor receptor, GPIb/IX/V, resulting in an inherited dominant form of Bernard-Soulier syndrome affecting two unrelated families: the N41H variant. · DOI
  91. Yamamoto N, Akamatsu N, Sakuraba H, Matsuno K, Hosoya R, Nogami H, Kasahara K, Mitsuyama S, Arai M. Novel Bernard-Soulier syndrome variants caused by compound heterozygous mutations (case I) or a cytoplasmic tail truncation (case II) of GPIbalpha. · DOI
  92. Othman M, Emsley J. Gene of the issue: GP1BA gene mutations associated with bleeding. · DOI
  93. Kunishima S, Lopez JA, Kobayashi S, Imai N, Kamiya T, Saito H, Naoe T. Missense mutations of the glycoprotein (GP) Ib beta gene impairing the GPIb alpha/beta disulfide linkage in a family with giant platelet disorder. · DOI
  94. Kunishima S, Kamiya T, Saito H. Genetic abnormalities of Bernard-Soulier syndrome. · DOI
  95. Kunishima S, Naoe T, Kamiya T, Saito H. Novel heterozygous missense mutation in the platelet glycoprotein Ib beta gene associated with isolated giant platelet disorder. · DOI
  96. Kurokawa Y, Ishida F, Kamijo T, Kunishima S, Kenny D, Kitano K, Koike K. A missense mutation (Tyr88 to Cys) in the platelet membrane glycoprotein Ibbeta gene affects GPIb/IX complex expression--Bernard-Soulier syndrome in the homozygous form and giant platelets in the heterozygous form. · DOI
  97. Kunishima S, Imai T, Kobayashi R, Kato M, Ogawa S, Saito H. Bernard-Soulier syndrome caused by a hemizygous GPIbbeta mutation and 22q11.2 deletion. · DOI
  98. Wright SD, Michaelides K, Johnson DJ, West NC, Tuddenham EG. Double heterozygosity for mutations in the platelet glycoprotein IX gene in three siblings with Bernard-Soulier syndrome. · DOI
  99. Noris P, Simsek S, Stibbe J, von dem Borne AE. A phenylalanine-55 to serine amino-acid substitution in the human glycoprotein IX leucine-rich repeat is associated with Bernard-Soulier syndrome. · DOI
  100. Noris P, Arbustini E, Spedini P, Belletti S, Balduini CL. A new variant of Bernard-Soulier syndrome characterized by dysfunctional glycoprotein (GP) Ib and severely reduced amounts of GPIX and GPV. · DOI
  101. Kunishima S, Tomiyama Y, Honda S, Kurata Y, Kamiya T, Ozawa K, Saito H. Cys97-->Tyr mutation in the glycoprotein IX gene associated with Bernard-Soulier syndrome. · DOI
  102. Rivera CE, Villagra J, Riordan M, Williams S, Lindstrom KJ, Rick ME. Identification of a new mutation in platelet glycoprotein IX (GPIX) in a patient with Bernard-Soulier syndrome. · DOI
  103. Wang Z, Shi J, Han Y. A novel point mutation in the transmembrane domain of platelet glycoprotein IX gene identified in a Bernard-Soulier syndrome patient.
  104. Boisseau P, Debord C, Eveillard M, Quemener A, Sigaud M, Giraud M, Talarmain P, Thomas C, Landeau G, Bezieau S, Petesch BP, Béné MC, Fouassier M. Two novel variants of uncertain significance in GP9 associated with Bernard-Soulier syndrome: Are they true mutations? · DOI
  105. Miura Y, Mardy S, Awaya Y, Nihei K, Endo F, Matsuda I, Indo Y. Mutation and polymorphism analysis of the TRKA (NTRK1) gene encoding a high-affinity receptor for nerve growth factor in congenital insensitivity to pain with anhidrosis (CIPA) families. · DOI
  106. Mardy S, Miura Y, Endo F, Matsuda I, Indo Y. Congenital insensitivity to pain with anhidrosis (CIPA): Effect of TRKA (NTRK1) missense mutations on autophosphorylation of the receptor tyrosine kinase for nerve growth factor. · DOI
  107. Franco ML, Melero C, Sarasola E, Acebo P, Luque A, Calatayud-Baselga I, Garcia-Barcina M, Vilar M. Mutations in TrkA causing congenital insensitivity to pain with anhidrosis (CIPA) induce misfolding, aggregation, and mutation-dependent neurodegeneration by dysfunction of the autophagic flux. · DOI
  108. Nam TS, Li W, Yoon S, Eom GH, Kim MK, Jung ST, Choi SY. Novel NTRK1 mutations associated with congenital insensitivity to pain with anhidrosis verified by functional studies. · DOI
  109. Altassan R, Saud HA, Masoodi TA, Dosssari HA, Khalifa O, Al-Zaidan H, Sakati N, Rhabeeni Z, Al-Hassnan Z, Binamer Y, Alhashemi N, Wade W, Al-Zayed Z, Al-Sayed M, Al-Muhaizea MA, Meyer B, Al-Owain M, Wakil SM. Exome sequencing identifies novel NTRK1 mutations in patients with HSAN-IV phenotype. · DOI
  110. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O’Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, The BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR. Patterns of somatic mutation in human cancer genomes. · DOI
  111. Rossetti S, Chauveau D, Walker D, Saggar-Malik A, Winearls CG, Torres VE, Harris PC. A complete mutation screen of the ADPKD genes by DHPLC. · DOI
  112. Rossetti S, Chauveau D, Kubly V, Slezak JM, Saggar-Malik AK, Pei Y, Ong AC, Stewart F, Watson ML, Bergstralh EJ, Winearls CG, Torres VE, Harris PC. Association of mutation position in polycystic kidney disease 1 (PKD1) gene and development of a vascular phenotype. · DOI
  113. Hoefele J, Mayer K, Scholz M, Klein HG. Novel PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease (ADPKD). · DOI
  114. Tan YC, Blumenfeld JD, Anghel R, Donahue S, Belenkaya R, Balina M, Parker T, Levine D, Leonard DG, Rennert H. Novel method for genomic analysis of PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease. · DOI
  115. Rossetti S, Strmecki L, Gamble V, Burton S, Sneddon V, Peral B, Roy S, Bakkaloglu A, Komel R, Winearls CG, Harris PC. Mutation analysis of the entire PKD1 gene: Genetic and diagnostic implications. · DOI
  116. Liu B, Chen SC, Yang YM, Yan K, Qian YQ, Zhang JY, Hu YT, Dong MY, Jin F, Huang HF, Xu CM. Identification of novel PKD1 and PKD2 mutations in a Chinese population with autosomal dominant polycystic kidney disease. · DOI
  117. De Leener A, Caltabiano G, Erkan S, Idil M, Vassart G, Pardo L, Costagliola S. Identification of the first germline mutation in the extracellular domain of the follitropin receptor responsible for spontaneous ovarian hyperstimulation syndrome. · DOI
  118. Beau I, Touraine P, Meduri G, Gougeon A, Desroches A, Matuchansky C, Milgrom E, Kuttenn F, Misrahi M. A novel phenotype related to partial loss of function mutations of the follicle stimulating hormone receptor. · DOI
  119. Aittomaki K, Lucena JL, Pakarinen P, Sistonen P, Tapanainen J, Gromoll J, Kaskikari R, Sankila EM, Lehvaslaiho H, Engel AR, Nieschlag E, Huhtaniemi I, de la Chapelle A. Mutation in the follicle-stimulating hormone receptor gene causes hereditary hypergonadotropic ovarian failure. · DOI
  120. Touraine P, Beau I, Gougeon A, Meduri G, Desroches A, Pichard C, Detoeuf M, Paniel B, Prieur M, Zorn JR, Milgrom E, Kuttenn F, Misrahi M. New natural inactivating mutations of the follicle-stimulating hormone receptor: correlations between receptor function and phenotype. · DOI
  121. Allen LA, Achermann JC, Pakarinen P, Kotlar TJ, Huhtaniemi IT, Jameson JL, Cheetham TD, Ball SG. A novel loss of function mutation in exon 10 of the FSH receptor gene causing hypergonadotrophic hypogonadism: Clinical and molecular characteristics. · DOI
  122. Ulloa-Aguirre A, Zarinan T. The follitropin receptor: Matching structure and function. · DOI
  123. Nakamura Y, Maekawa R, Yamagata Y, Tamura I, Sugino N. A novel mutation in exon8 of the follicle-stimulating hormone receptor in a woman with primary amenorrhea. · DOI
  124. Ozcabi B, Tahmiscioglu Bucak F, Ceylaner S, Ozcan R, Buyukunal C, Ercan O, Tuysuz B, Evliyaoglu O. Testotoxicosis: Report of two cases, one with a novel mutation in LHCGR gene. · DOI
  125. Misrahi M, Meduri G, Pissard S, Bouvattier C, Beau I, Loosfelt H, Jolivet A, Rappaport R, Milgrom E, Bougneres P. Comparison of immunocytochemical and molecular features with the phenotype in a case of incomplete male pseudoherma-phroditism associated with a mutation of the luteinizing hormone receptor.
  126. Richter-Unruh A, Verhoef-Post M, Malak S, Homoki J, Hauffa BP, Themmen AP. Leydig cell hypoplasia: Absent luteinizing hormone receptor cell surface expression caused by a novel homozygous mutation in the extracellular domain. · DOI
  127. Qiao J, Han B, Liu BL, Chen X, Ru Y, Cheng KX, Chen FG, Zhao SX, Liang J, Lu YL, Tang JF, Wu YX, Wu WL, Chen JL, Chen MD, Song HD. A splice site mutation combined with a novel missense mutation of LHCGR cause male pseudohermaphroditism. · DOI
  128. Martens JW, Lumbroso S, Verhoef-Post M, Georget V, Richter-Unruh A, Szarras-Czapnik M, Romer TE, Brunner HG, Themmen AP, Sultan C. Mutant luteinizing hormone receptors in a compound heterozygous patient with complete Leydig cell hypoplasia: Abnormal processing causes signaling deficiency. · DOI
  129. Stavrou SS, Zhu YS, Cai LQ, Katz MD, Herrera C, Defillo-Ricart M, Imperato-McGinley J. A novel mutation of the human luteinizing hormone receptor in 46XY and 46XX sisters.
  130. Charmandari E, Guan R, Zhang M, Silveira LG, Fan QR, Chrousos GP, Sertedaki AC, Latronico AC, Segaloff DL. Misfolding ectodomain mutations of the lutropin receptor increase efficacy of hormone stimulation. · DOI
  131. Athanasoulia AP, Stalla GK, Auer MK. Insights into the coexistence of two mutations in the same LHCGR gene locus causing severe Leydig cell hypoplasia. · DOI
  132. Mitri F, Bentov Y, Behan LA, Esfandiari N, Casper RF. A novel compound heterozygous mutation of the luteinizing hormone receptor -implications for fertility. · DOI
  133. Troppmann B, Kleinau G, Krause G, Gromoll J. Structural and functional plasticity of the luteinizing hormone/ choriogonadotrophin receptor. · DOI
  134. Leung MY, Steinbach PJ, Bear D, Baxendale V, Fechner PY, Rennert OM, Chan WY. Biological effect of a novel mutation in the third leucine-rich repeat of human luteinizing hormone receptor. · DOI
  135. Gromoll J, Schulz A, Borta H, Gudermann T, Teerds KJ, Greschniok A, Nieschlag E, Seif FJ. Homozygous mutation within the conserved Ala-Phe-Asn-Glu-Thr motif of exon 7 of the LH receptor causes male pseudohermaphroditism. · DOI
  136. Ho SC, Goh SS, Khoo DH. Association of Graves’ disease with intragenic polymorphism of the thyrotropin receptor gene in a cohort of Singapore patients of multi-ethnic origins. · DOI
  137. Peeters RP, van Toor H, Klootwijk W, de Rijke YB, Kuiper GG, Uitterlinden AG, Visser TJ. Polymorphisms in thyroid hormone pathway genes are associated with plasma TSH and iodothyronine levels in healthy subjects. · DOI
  138. Tonacchera M, Perri A, De Marco G, Agretti P, Montanelli L, Banco ME, Corrias A, Bellone J, Tosi MT, Vitti P, Martino E, Pinchera A, Chiovato L. TSH receptor and Gs(alpha) genetic analysis in children with Down’s syndrome and subclinical hypothyroidism. · DOI
  139. de Roux N, Misrahi M, Brauner R, Houang M, Carel JC, Granier M, Le Bouc Y, Ghinea N, Boumedienne A, Toublanc JE, Milgrom E. Four families with loss of function mutations of the thyrotropin receptor.
  140. Alberti L, Proverbio MC, Costagliola S, Romoli R, Boldrighini B, Vigone MC, Weber G, Chiumello G, Beck-Peccoz P, Persani L. Germline mutations of TSH receptor gene as cause of nonautoimmune subclinical hypothyroidism. · DOI
  141. Clifton-Bligh RJ, Gregory JW, Ludgate M, John R, Persani L, Asteria C, Beck-Peccoz P, Chatterjee VK. Two novel mutations in the thyrotropin (TSH) receptor gene in a child with resistance to TSH.
  142. Tonacchera M, Perri A, De Marco G, Agretti P, Banco ME, Di Cosmo C, Grasso L, Vitti P, Chiovato L, Pinchera A. Low prevalence of thyrotropin receptor mutations in a large series of subjects with sporadic and familial nonautoimmune subclinical hypothyroidism. · DOI
  143. Sunthornthepvarakui T, Gottschalk ME, Hayashi Y, Refetoff S. Brief report: resistance to thyrotropin caused by mutations in the thyrotropin-receptor gene. · DOI
  144. Rodien P, Bremont C, Sanson ML, Parma J, Van Sande J, Costagliola S, Luton JP, Vassart G, Duprez L. Familial gestational hyperthyroidism caused by a mutant thyrotropin receptor hypersensitive to human chorionic gonadotropin. · DOI
  145. Kopp P, Muirhead S, Jourdain N, Gu WX, Jameson JL, Rodd C. Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation (serine281-->isoleucine) in the extracellular domain of the thyrotropin receptor. · DOI
  146. Ohno M, Endo T, Ohta K, Gunji K, Onaya T. Point mutations in the thyrotropin receptor in human thyroid tumors. · DOI
  147. Parma J, Duprez L, Van Sande J, Hermans J, Rocmans P, Van Vliet G, Costagliola S, Rodien P, Dumont JE, Vassart G. Diversity and prevalence of somatic mutations in the thyrotropin receptor and Gs alpha genes as a cause of toxic thyroid adenomas.
  148. Russo D, Betterle C, Arturi F, Chiefari E, Girelli ME, Filetti S. A novel mutation in the thyrotropin (TSH) receptor gene causing loss of TSH binding but constitutive receptor activation in a family with resistance to TSH.
  149. Bech-Hansen NT, Naylor MJ, Maybaum TA, Sparkes RL, Koop B, Birch DG, Bergen AA, Prinsen CF, Polomeno RC, Gal A, Drack AV, Musarella MA, Jacobson SG, Young RS, Weleber RG. Mutations in NYX, encoding the leucine-rich proteoglycan nyctalopin, cause X-linked complete congenital stationary night blindness. · DOI
  150. Pusch CM, Zeitz C, Brandau O, Pesch K, Achatz H, Feil S, Scharfe C, Maurer J, Jacobi FK, Pinckers A, Andreasson S, Hardcastle A, Wissinger B, Berger W, Meindl A. The complete form of X-linked congenital stationary night blindness is caused by mutations in a gene encoding a leucine-rich repeat protein. · DOI
  151. Zhou L, Li T, Song X, Li Y, Li H, Dan H. NYX mutations in four families with high myopia with or without CSNB1.
  152. Leroy BP, Budde BS, Wittmer M, De Baere E, Berger W, Zeitz C. A common NYX mutation in Flemish patients with X linked CSNB. · DOI
  153. Dai S, Ying M, Wang K, Wang L, Han R, Hao P, Li N. Two novel NYX gene mutations in the chinese families with X-linked congenital stationary night blindness. · DOI
  154. Pradhan M, Sharp D, Mora J, Wittmer M, Berger W, Vincent A. A novel NYX mutation associated with X-linked congenital stationary night blindness in a New Zealand family.
  155. Wang Q, Gao Y, Li S, Guo X, Zhang Q. Mutation screening of TRPM1, GRM6, NYX and CACNA1F genes in patients with congenital stationary night blindness. · DOI
  156. Xiao X, Jia X, Guo X, Li S, Yang Z, Zhang Q. CSNB1 in Chinese families associated with novel mutations in NYX. · DOI
  157. Zeitz C, Minotti R, Feil S, Matyas G, Cremers FP, Hoyng CB, Berger W. Novel mutations in CACNA1F and NYX in Dutch families with X-linked congenital stationary night blindness.
  158. Sui R, Li F, Zhao J, Jiang R. Clinical and genetic characterization of a Chinese family with CSNB1. · DOI
  159. Yip SP, Li CC, Yiu WC, Hung WH, Lam WW, Lai MC, Ng PW, Fung WY, Chu PH, Jiang B, Chan HH, Yap MK. A novel missense mutation in the NYX gene associated with high myopia. · DOI
  160. Zhang Q, Xiao X, Li S, Jia X, Yang Z, Huang S, Caruso RC, Guan T, Sergeev Y, Guo X, Hejtmancik JF. Mutations in NYX of individuals with high myopia, but without night blindness.
  161. . Zeitz, C.; Jacobson, S.G.; Hamel, C.P.; Bujakowska, K.; Neuille, M.; Orhan, E.; Zanlonghi, X.; Lancelot, M.E.; Michiels, C.; Schwartz, S.B.; Bocquet, B.; Congenital Stationary Night Blindness Consortium; Antonio, A.; Audier, C.; Letexier, M.; Saraiva, J.P.; Luu, T.D.; Sennlaub, F.; Nguyen, H.; Poch, O.; Dollfus, H.; Lecompte, O.; Kohl, S.; Sahel, J.A.; Bhattacharya, S.S.; Audo, I. Whole-exome sequencing identifies LRIT3 mutations as a cause of autosomal-recessive complete congenital stationary night blindness. · DOI
  162. Dan H, Song X, Li J, Xing Y, Li T. Mutation screening of the LRIT3, CABP4, and GPR179 genes in Chinese patients with Schubert-Bornschein congenital stationary night blindness. · DOI
  163. Zeitz C, Robson AG, Audo I. Congenital stationary night blindness: an analysis and update of genotype-phenotype correlations and pathogenic mechanisms. · DOI
  164. Gorlov IP, Kamat A, Bogatcheva NV, Jones E, Lamb DJ, Truong A, Bishop CE, McElreavey K, Agoulnik AI. Mutations of the GREAT gene cause cryptorchidism. · DOI
  165. Bogatcheva NV, Ferlin A, Feng S, Truong A, Gianesello L, Foresta C, Agoulnik AI. T222P mutation of the insulin-like 3 hormone receptor LGR8 is associated with testicular maldescent and hinders receptor expression on the cell surface membrane. · DOI
  166. Fofanova-Gambetti OV, Hwa V, Kirsch S, Pihoker C, Chiu HK, Hogler W, Cohen LE, Jacobsen C, Derr MA, Rosenfeld RG. Three novel IGFALS gene mutations resulting in total ALS and severe circulating IGF-I/IGFBP-3 deficiency in children of different ethnic origins.
  167. David A, Rose SJ, Miraki-Moud F, Metherell LA, Savage MO, Clark AJ, Camacho-Hubner C. Acid-labile subunit deficiency and growth failure: Description of two novel cases. · DOI
  168. Hess O, Khayat M, Hwa V, Heath KE, Teitler A, Hritan Y, Allon-Shalev S, Tenenbaum-Rakover Y. A novel mutation in IGFALS, c.380T>C (p.L127P), associated with short stature, delayed puberty, osteopenia and hyperinsulinaemia in two siblings: Insights into the roles of insulin growth factor-1 (IGF1). · DOI
  169. Domene HM, Scaglia PA, Lteif A, Mahmud FH, Kirmani S, Frystyk J, Bedecarras P, Gutierrez M, Jasper HG. Phenotypic effects of null and haploinsufficiency of acid-labile subunit in a family with two novel IGFALS gene mutations. · DOI
  170. Heath KE, Argente J, Barrios V, Pozo J, Diaz-Gonzalez F, Martos-Moreno GA, Caimari M, Gracia R, Campos-Barros A. Primary acid-labile subunit deficiency due to recessive IGFALS mutations results in postnatal growth deficit associated with low circulating insulin growth factor (IGF)-I, IGF binding protein-3 levels, and hyperinsulinemia. · DOI
  171. Hwa V, Haeusler G, Pratt KL, Little BM, Frisch H, Koller D, Rosenfeld RG. Total absence of functional acid labile subunit, resulting in severe insulin-like growth factor deficiency and moderate growth failure. · DOI
  172. Scaglia PA, Keselman AC, Braslavsky D, Martucci LC, Karabatas LM, Domene S, Gutierrez ML, Ballerini MG, Ropelato MG, Spinola-Castro A, Siviero-Miachon AA, Tartuci JS, Rodríguez Azrak MS, Rey RA, Jasper HG, Bergadá I, Domené HM. Characterization of four Latin American families confirms previous findings and reveals novel features of acid-labile subunit deficiency. · DOI
  173. Schreiner F, Schoenberger S, Koester B, Domene HM, Woelfle J. Novel acid-labile subunit (IGFALS) mutation p.T145K (c.434C>A) in a patient with ALS deficiency, normal stature and immunological dysfunction. · DOI
  174. Kang H, Han KA, Won SY, Kim HM, Lee YH, Ko J, Um JW. Slitrk Missense Mutations associated with neuropsychiatric disorders distinctively impair slitrk trafficking and synapse formation.
  175. Piton A, Gauthier J, Hamdan FF, Lafreniere RG, Yang Y, Henrion E, Laurent S, Noreau A, Thibodeau P. Karemera. L.; Spiegelman, D.; Kuku, F.; Duguay, J.; Destroismaisons, L.; Jolivet, P.; Côté, M.; Lachapelle, K.; Diallo, O.; Raymond, A.; Marineau, C.; Champagne, N.; Xiong, L.; Gaspar, C.; Rivière, J.B.; Tarabeux, J.; Cossette, P.; Krebs, M.O.; Rapoport, J.L.; Addington, A.; Delisi, L.E.; Mottron, L.; Joober, R.; Fombonne, E.; Drapeau, P.; Rouleau, G.A. Systematic resequencing of X-chromosome synaptic genes in autism spectrum disorder and schizophrenia. · DOI
  176. Song M, Mathews CA, Stewart SE, Shmelkov SV, Mezey JG, Rodriguez-Flores JL, Rasmussen SA, Britton JC, Oh YS, Walkup JT, Lee FS, Glatt CE. Rare synaptogenesis-impairing mutations in SLITRK5 are associated with obsessive compulsive disorder. · DOI
  177. Xiong D, Li G. Li.; K, Xu.; Q, Pan.; Z, Ding.; F, Vedell, P.; Liu, P.; Cui, P.; Hua, X.; Jiang, H.; Yin, Y.; Zhu, Z.; Li, X.; Zhang, B.; Ma, D.; Wang, Y.; You, M. Exome sequencing identifies MXRA5 as a novel cancer gene frequently mutated in non-small cell lung carcinoma from Chinese patients. · DOI
  178. Arbour NC, Lorenz E, Schutte BC, Zabner J, Kline JN, Jones M, Frees K, Watt JL, Schwartz DA. TLR4 mutations are associated with endotoxin hyporesponsiveness in humans. · DOI · Paper page
  179. Zareparsi S, Buraczynska M, Branham KE, Shah S, Eng D, Li M, Pawar H, Yashar BM, Moroi SE, Lichter PR, Petty HR, Richards JE, Abecasis GR, Elner VM, Swaroop A. Toll-like receptor 4 variant D299G is associated with susceptibility to age-related macular degeneration. · DOI · Paper page
  180. Franchimont D, Vermeire S, El Housni H, Pierik M, Van Steen K, Gustot T, Quertinmont E, Abramowicz M, Van Gossum A, Deviere J, Rutgeerts P. Deficient host-bacteria interactions in inflammatory bowel disease? The toll-like receptor (TLR)-4 Asp299gly polymorphism is associated with Crohn’s disease and ulcerative colitis. · DOI
  181. Oostenbrug LE, Drenth JP, de Jong DJ, Nolte IM, Oosterom E, van Dullemen HM, van der Linde K, te Meerman GJ, van der Steege G, Kleibeuker JH, Jansen PL. Association between Toll-like receptor 4 and inflammatory bowel disease. · DOI
  182. Browning BL, Huebner C, Petermann I, Gearry RB, Barclay ML, Shelling AN, Ferguson LR. Has toll-like receptor 4 been prematurely dismissed as an inflammatory bowel disease gene? Association study combined with meta-analysis shows strong evidence for association. · DOI
  183. De Jager PL, Franchimont D, Waliszewska A, Bitton A, Cohen A, Langelier D, Belaiche J, Vermeire S, Farwell L, Goris A, Libioulle C, Jani N, Dassopoulos T, Bromfield GP, Dubois B, Cho JH, Brant SR, Duerr RH, Yang H, Rotter JI, Silverberg MS, Steinhart AH, Daly MJ, Podolsky DK, Louis E, Hafler DA, Rioux JD. Quebec IBD Genetics Consortium NIDDK IBD Genetics Consortium. The role of the Toll receptor pathway in susceptibility to inflammatory bowel diseases. · DOI
  184. Meena NK, Ahuja V, Meena K, Paul J. Association of TLR5 gene polymorphisms in ulcerative colitis patients of north India and their role in cytokine homeostasis. · DOI
  185. Sales ML, Schreiber R, Ferreira-Sae MC, Fernandes MN, Piveta CS, Cipolli JA, Cardoso CC, Matos-Souza JR, Geloneze B, Franchini KG, Nadruz W. Toll-like receptor 6 Ser249Pro polymorphism is associated with lower left ventricular wall thickness and inflammatory response in hypertensive women. · DOI
  186. Uff S, Clemetson JM, Harrison T, Clemetson KJ, Emsley J. (2002) Crystal structure of the platelet glycoprotein Ib alpha N-terminal domain reveals an unmasking mechanism for receptor activation. · DOI
  187. Kumari D, Tiwari A, Choudhury M, Kumar A, Rao A, Dixit M. A novel KERA mutation in a case of autosomal recessive cornea plana with primary angle-closure glaucoma. · DOI
  188. Ebenezer ND, Patel CB, Hariprasad SM, Chen LL, Patel RJ, Hardcastle AJ, Allen RC. Clinical and molecular characterization of a family with autosomal recessive cornea plana. · DOI
  189. Lehmann OJ, El-ashry MF, Ebenezer ND, Ocaka L, Francis PJ, Wilkie SE, Patel RJ, Ficker L, Jordan T, Khaw PT, Bhattacharya SS. A novel keratocan mutation causing autosomal recessive cornea plana.
  190. Pellegata NS, Dieguez-Lucena JL, Joensuu T, Lau S, Montgomery KT, Krahe R, Kivela T, Kucherlapati R, Forsius H, de la Chapelle A. Mutations in KERA, encoding keratocan, cause cornea plana. · DOI
  191. Roos L, Bertelsen B, Harris P, Bygum A, Jensen H, Gronskov K, Tumer Z. Case report: A novel KERA mutation associated with cornea plana and its predicted effect on protein function. · DOI
  192. Dudakova L, Vercruyssen JHJ, Balikova I, Postolache L, Leroy BP, Skalicka P, Liskova P. Analysis of KERA in four families with cornea plana identifies two novel mutations. · DOI
  193. Wang P, Li S, Xiao X, Guo X, Zhang Q. An evaluation of OPTC and EPYC as candidate genes for high myopia.
  194. Majava M, Bishop PN, Hagg P, Scott PG, Rice A, Inglehearn C, Hammond CJ, Spector TD, Ala-Kokko L, Mannikko M. Novel mutations in the small leucine-rich repeat protein/proteoglycan (SLRP) genes in high myopia. · DOI
  195. Acharya M, Mookherjee S, Bhattacharjee A, Thakur SK, Bandyopadhyay AK, Sen A, Chakrabarti S, Ray K. Evaluation of the OPTC gene in primary open angle glaucoma: Functional significance of a silent change. · DOI
  196. Cho SY, Bae JS, Kim NKD, Forzano F, Girisha KM, Baldo C, Faravelli F, Cho TJ, Kim D, Lee KY, Ikegawa S, Shim JS, Ko AR, Miyake N, Nishimura G, Superti-Furga A, Spranger J, Kim OH, Park WY, Jin DK. BGN mutations in X-linked spondyloepimetaphyseal dysplasia. · DOI
  197. Meester JA, Vandeweyer G, Pintelon I, Lammens M, Van Hoorick L, De Belder S, Waitzman K, Young L, Markham LW, Vogt J, Richer J, Beauchesne LM, Unger S, Superti-Furga A, Prsa M, Dhillon R, Reyniers E, Dietz HC, Wuyts W, Mortier G, Verstraeten A, Van Laer L, Loeys BL. Loss-of-function mutations in the X-linked biglycan gene cause a severe syndromic form of thoracic aortic aneurysms and dissections. · DOI
  198. Miraoui H, Dwyer AA, Sykiotis GP, Plummer L, Chung W, Feng B, Beenken A, Clarke J, Pers TH, Dworzynski P, Keefe K, Niedziela M, Raivio T, Crowley WF, Seminara SB, Quinton R, Hughes VA, Kumanov P, Young J, Yialamas MA, Hall JE, Van Vliet G, Chanoine JP, Rubenstein J, Mohammadi M, Tsai PS, Sidis Y, Lage K, Pitteloud N. Mutations in FGF17, IL17RD, DUSP6, SPRY4, and FLRT3 are identified in individuals with congenital hypogonadotropic hypogonadism. · DOI · Paper page
  199. Matsushima N, Ohyanagi T, Tanaka T, Kretsinger RH. Super-motifs and evolution of tandem leucine-rich repeats within the small proteoglycans--biglycan, decorin, lumican, fibromodulin, PRELP, keratocan, osteoadherin, epiphycan, and osteoglycin. · DOI
  200. Batkhishig D, Bilguun K, Enkhbayar P, Miyashita H, Kretsinger RH, Matsushima N. Super secondary structure consisting of a polyproline ii helix and a beta-turn in leucine rich repeats in bacterial Type III secretion system effectors. · DOI

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Authors
Matsushima, N., Takatsuka, S., Miyashita, H., & Kretsinger, R. H.
Affiliations
  • Center for Medical Education, Sapporo Medical University, Sapporo 060-8556, Japan
  • Institute of Tandem Repeats, Noboribetsu 059-0464, Japan
  • Department of Biology, University of Virginia, Charlottesville, VA 22904, United States
Venue
Protein & Peptide Letters
Publisher
Bentham Science Publishers Ltd.
Published
2019-02-20
Volume
26
Issue
2
Pages
108-131
ISSN
0929-8665
DOI
10.2174/0929866526666181208170027
Cited by
73
References
2
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Leucine Rich Repeat Proteins: Sequences, Mutations, Structures and Diseases. https://app.cochat.ai/papers/10.2174/0929866526666181208170027
The paper
Matsushima, N., Takatsuka, S., Miyashita, H., & Kretsinger, R. H. (2019). Leucine Rich Repeat Proteins: Sequences, Mutations, Structures and Diseases. Protein & Peptide Letters. https://doi.org/10.2174/0929866526666181208170027