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Circulation Research, ISSN 0009-7330, 06/2017, Volume 121, Issue 5, pp. 525 - 536
Journal Article
Nature Genetics, ISSN 1061-4036, 2006, Volume 38, Issue 8, pp. 917 - 920
Journal Article
FEBS Letters, ISSN 0014-5793, 10/2015, Volume 589, Issue 20, pp. 3119 - 3125
Mutations in rhodopsin can cause misfolding and aggregation of the receptor, which leads to retinitis pigmentosa, a progressive retinal degenerative disease.... 
G protein-coupled receptor | Retinal degeneration | Membrane protein | Protein aggregation | Protein misfolding | Secondary structure | Förster resonance energy transfer | cyan fluorescent protein | circular dichroism | mTq | CFP | WT-KKYL | mTurquoise | FTIR | yellow fluorescent protein | FRET | wild-type with an ER retention sequence | wheat germ agglutinin | Fourier transform infrared | polymerase chain reaction | YFP | dodecyl | metarhodopsin II | MII | maltoside | WGA | retinitis pigmentosa | GPCR | wild-type | murine rhodopsin | endoplasmic reticulum | mRho | PCR | UBIQUITIN-PROTEASOME SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEGMENT DISC MEMBRANES | PROTEIN-COUPLED RECEPTORS | RHODOPSIN MUTATIONS | DOMINANT RETINITIS-PIGMENTOSA | CELL BIOLOGY | ORGANIZATION | XENOPUS-LAEVIS | BIOPHYSICS | THIOFLAVINE-T | DEGRADATION | AGGREGATION | Opsins - genetics | Protein Structure, Secondary | Humans | Endoplasmic Reticulum - metabolism | Retinitis Pigmentosa - genetics | Rhodopsin - metabolism | Spectroscopy, Fourier Transform Infrared | Protein Folding | Microscopy, Confocal | Animals | Opsins - chemistry | Rhodopsin - genetics | HEK293 Cells | Opsins - metabolism | Fluorescence Resonance Energy Transfer | Luminescent Proteins - genetics | Mice | Mutation | Spectrophotometry | Luminescent Proteins - metabolism | Index Medicus | BASIC BIOLOGICAL SCIENCES | secondary structure | membrane protein | retinal degeneration | protein aggregation | protein misfolding
Journal Article
Nature Genetics, ISSN 1061-4036, 12/2013, Volume 45, Issue 12, pp. 1439 - 1445
Journal Article
by Robinson, Giles and Robinson, Giles and Parker, Matthew and Parker, Matthew and Kranenburg, Tanya A and Kranenburg, Tanya A and Lu, Charles and Lu, Charles and Chen, Xiang and Chen, Xiang and Ding, Li and Ding, Li and Phoenix, Timothy N and Phoenix, Timothy N and Hedlund, Erin and Hedlund, Erin and Wei, Lei and Wei, Lei and Zhu, Xiaoyan and Zhu, Xiaoyan and Chalhoub, Nader and Chalhoub, Nader and Baker, Suzanne J and Baker, Suzanne J and Huether, Robert and Huether, Robert and Kriwacki, Richard and Kriwacki, Richard and Curley, Natasha and Curley, Natasha and Thiruvenkatam, Radhika and Thiruvenkatam, Radhika and Wang, Jianmin and Wang, Jianmin and Wu, Gang and Wu, Gang and Rusch, Michael and Rusch, Michael and Hong, Xin and Hong, Xin and Becksfort, Jared and Becksfort, Jared and Gupta, Pankaj and Gupta, Pankaj and Ma, Jing and Ma, Jing and Easton, John and Easton, John and Vadodaria, Bhavin and Vadodaria, Bhavin and Onar-Thomas, Arzu and Onar-Thomas, Arzu and Lin, Tong and Lin, Tong and Li, Shaoyi and Li, Shaoyi and Pounds, Stanley and Pounds, Stanley and Paugh, Steven and Paugh, Steven and Zhao, David and Zhao, David and Kawauchi, Daisuke and Kawauchi, Daisuke and Roussel, Martine F and Roussel, Martine F and Finkelstein, David and Finkelstein, David and Ellison, David W and Ellison, David W and Lau, Ching C and Lau, Ching C and Bouffet, Eric and Bouffet, Eric and Hassall, Tim and Hassall, Tim and Gururangan, Sridharan and Gururangan, Sridharan and Cohn, Richard and Cohn, Richard and Fulton, Robert S and Fulton, Robert S and Fulton, Lucinda L and Fulton, Lucinda L and Dooling, David J and Dooling, David J and Ochoa, Kerri and Ochoa, Kerri and Gajjar, Amar and Gajjar, Amar and Mardis, Elaine R and Mardis, Elaine R and Wilson, Richard K and Wilson, Richard K and Downing, James R and Downing, James R and Zhang, Jinghui and Zhang, Jinghui and Gilbertson, Richard J and Gilbertson, Richard J
Nature, ISSN 0028-0836, 08/2012, Volume 488, Issue 7409, pp. 43 - 48
Journal Article
Nature Medicine, ISSN 1078-8956, 12/2014, Volume 20, Issue 12, pp. 1410 - 1416
The protein cytotoxic T lymphocyte antigen-4 (CTLA-4) is an essential negative regulator of immune responses, and its loss causes fatal autoimmunity in mice.... 
PATHWAYS | MEDICINE, RESEARCH & EXPERIMENTAL | CLINICAL-PICTURE | HOMEOSTASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | AUTOIMMUNITY | REGULATORY T-CELLS | GERMLINE MUTATIONS | MICE | BLOCKADE | IMMUNODEFICIENCY | ABATACEPT | Recurrence | Agammaglobulinemia - immunology | Agammaglobulinemia - genetics | Purpura, Thrombocytopenic, Idiopathic - genetics | Exons | Immune System Diseases - genetics | Humans | Middle Aged | Male | Anemia, Hemolytic, Autoimmune - genetics | Mutation, Missense | Respiratory Tract Infections - genetics | T-Lymphocytes, Regulatory - immunology | Autoimmune Diseases - genetics | Young Adult | Purpura, Thrombocytopenic, Idiopathic - immunology | Adult | Female | Endocytosis - genetics | Polyendocrinopathies, Autoimmune - genetics | Child | Endocytosis - immunology | Granuloma - genetics | Autoimmune Diseases - immunology | CTLA-4 Antigen - genetics | B7-1 Antigen - metabolism | Codon, Nonsense | CTLA-4 Antigen - immunology | Syndrome | Polyendocrinopathies, Autoimmune - immunology | Lung Diseases, Interstitial - immunology | Animals | B-Lymphocytes - immunology | Lung Diseases, Interstitial - genetics | Pedigree | Anemia, Hemolytic, Autoimmune - immunology | Adolescent | Respiratory Tract Infections - immunology | Granuloma - immunology | Heterozygote | Mice | Antigens | Gene mutations | Physiological aspects | Genetic aspects | Immunologic diseases | Research | Risk factors | Proteins | Homeostasis | Cytotoxicity | Ligands | T cell receptors | Mutation | Immune system
Journal Article