DOI: 10.1002/pro.5560030901. Structure and functions of arrestins

10.1002/pro.5560030901

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractTransmembrane signal transductions in a variety of cell types that mediate signals as diverse as those carried by neurotransmitters, hormones, and sensory signals share basic biochemical mechanisms that include: (1) an extracellular perturbation (neurotransmitter, hormone, odor, light); (2) specific receptors; (3) coupling proteins, such as G proteins; and (4) effector enzymes or ion channels. Parallel to these amplification reactions, receptors are precisely inactivated by mechanisms that involve protein kinases and regulatory proteins called arrestins. The structure and functions of arrestins are the focus of this review.

Bibliography

Palczewski, K. (1994). Structure and functions of arrestins. Protein Science, 3(9), 1355â1361. Portico.

Authors 1

Krzysztof Palczewski (first)

References 71 Referenced 65

10.1016/S0021-9258(19)37125-X / J Biol Chem / β‐Arrestin‐2, a novel member of the arrestin/β‐arrestin gene family by Attramadal H (1992)
10.1021/bi00405a049
10.1073/pnas.84.24.8879
10.1111/j.1432-1033.1993.tb18117.x
10.1016/S0021-9258(18)98645-X / J Biol Chem / Expression of S‐antigen in retina, pineal gland, lens, and brain is directed by 5′‐flanking sequences by Breitman ML (1991)
10.1073/pnas.88.6.2568
10.1016/S0021-9258(17)41820-5
10.1016/0888-7543(89)90075-X
10.1126/science.8381559
10.1126/science.8316831
10.1016/0167-4838(92)90403-Z
10.1016/S0021-9258(19)37139-X / J Biol Chem / Activation of bovine rod outer segment phospholipase C by arrestin by Ghalayini AJ (1992)
10.1016/0014-5793(91)80530-G
10.1016/S0021-9258(19)36700-6
10.1016/S0021-9258(19)50248-4
10.1016/S0021-9258(19)85275-4
10.1002/bies.950150107
{'key': 'e_1_2_1_19_1', 'first-page': '267', 'volume-title': 'Handbook of experimental pharmacology, vol 108/II. GTPases in biology II', 'author': 'Hofmann KP', 'year': '1993'} / Handbook of experimental pharmacology, vol 108/II. GTPases in biology II by Hofmann KP (1993)
10.1016/S0021-9258(19)49592-6
10.1016/S0021-9258(19)38873-8 / J Biol Chem / Ca2+ binding capacity of cytoplasmic proteins from rod photoreceptors is mainly due to arrestin by Huppertz B (1990)
10.1073/pnas.87.3.1008
10.1016/S0021-9258(20)80439-6
10.1016/S0021-9258(18)98738-7 / J Biol Chem / A 48‐kDa, S‐antigen‐like phosphoprotein in yeast DNA‐replicative complex preparations by Jeansonne NE (1991)
10.1016/S0006-291X(88)80754-X
10.1016/0003-9861(91)90338-J
10.1016/S0021-9258(17)41852-7 / J Biol Chem / Arrestin‐rhodopsin interaction. Multi‐site binding delineated by peptide inhibition by Krupnick JG (1994)
10.1016/0925-4773(90)90131-5
10.1016/S0021-9258(18)42479-9 / J Biol Chem / Receptor‐specific desensitization with purified proteins. Kinase dependence and receptor specificity of β‐arrestin and arrestin in the β2‐adrenergic receptor and rhodopsin systems by Lohse MJ (1992)
10.1126/science.2163110
10.1016/0896-6273(94)90309-3
10.1016/0006-291X(91)90683-X
10.1021/bi00069a036
10.1016/0014-5793(93)81712-9
10.1016/0888-7543(90)90521-U
10.1073/pnas.90.8.3241
10.1021/bi00170a022
10.1021/bi00072a030
10.1016/0968-0004(91)90157-Q
10.1016/S0021-9258(18)98620-5 / J Biol Chem / Role of the carboxyl‐terminal region of arrestin in binding to phosphorylated rhodopsin by Palczewski K (1991)
10.1002/pro.5560030215
10.1016/S0021-9258(20)64307-1
10.1016/S0021-9258(18)71543-3 / J Biol Chem / Regulation of rhodopsin dephosphorylation by arrestin by Palczewski K (1989)
10.1016/0014-5793(91)81416-6
10.1016/S0021-9258(18)55112-7
10.1021/bi00131a003
10.1016/0896-6273(92)90113-R
10.1021/bi00074a002
10.1016/S0021-9258(18)98412-7 / J Biol Chem / Molecular analysis of human β‐arrestin‐1: Cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing by Parruti G (1993)
10.1016/S0021-9258(18)53678-4 / J Biol Chem / Overexpression of β‐arrestin and β‐adrenergic receptor kinase augment desensitization of β2‐adrenergic receptors by Pippig S (1993)
{'key': 'e_1_2_1_51_1', 'first-page': '1248', 'article-title': 'Effect of sulfhydryl group modification on arrestin interaction with phosphorylated rhodopsin', 'volume': '6', 'author': 'Pogozheva ID', 'year': '1989', 'journal-title': 'Biol Membr'} / Biol Membr / Effect of sulfhydryl group modification on arrestin interaction with phosphorylated rhodopsin by Pogozheva ID (1989)
10.1021/bi00214a002
10.1016/0014-5793(93)80609-X
10.1016/0303-7207(92)90038-8
10.1021/bi00430a052
10.1073/pnas.84.20.6975
10.1016/0278-4327(88)90020-X
{'key': 'e_1_2_1_58_1', 'first-page': '197', 'article-title': 'The structure of bovine retinal S‐antigen: Sequence analysis and identification of monoclonal antibody epitopes and uveitogenic site', 'volume': '31', 'author': 'Shinohara T', 'year': '1987', 'journal-title': 'Jpn J Ophthalmol'} / Jpn J Ophthalmol / The structure of bovine retinal S‐antigen: Sequence analysis and identification of monoclonal antibody epitopes and uveitogenic site by Shinohara T (1987)
10.1016/0305-0491(92)90361-T
10.1016/S0021-9258(17)40691-0 / J Biol Chem / Splice variant of arrestin: Molecular cloning and localization in bovine retina by Smith CW (1994)
10.1073/pnas.87.3.1003
10.1016/S0021-9258(18)82304-3 / J Biol Chem / Polypeptide variants of β‐arrestin and arrestin 3 by Sterne‐Marr R (1993)
10.1111/j.1432-1033.1991.tb21053.x
10.1016/0378-1119(88)90308-3
10.4049/jimmunol.119.6.1949 / J Immunol / Experimental allergic uveitis. Isolation, characterization, and localization of a soluble uveitopathogenic antigen from bovine retina by Wacker WB (1977)
10.1016/0014-5793(88)81242-0
10.1111/j.1432-1033.1990.tb19360.x
10.1073/pnas.83.5.1174
10.1126/science.2158671
10.1016/S0021-9258(17)45280-X / J Biol Chem / Structural organization of the human S‐antigen gene. cDNA, amino acid, intron, exon, promoter, in vitro transcription, retina, and pineal gland by Yamaki K (1990)
10.1016/0014-5793(86)80008-4
10.1016/0014-5793(88)80516-7

Dates

Type	When
Created	16 years, 6 months ago (Feb. 9, 2009, 8:58 p.m.)
Deposited	1 year, 10 months ago (Oct. 24, 2023, 8:52 a.m.)
Indexed	1 year, 3 months ago (May 6, 2024, 5:25 p.m.)
Issued	30 years, 11 months ago (Sept. 1, 1994)
Published	30 years, 11 months ago (Sept. 1, 1994)
Published Online	16 years, 7 months ago (Dec. 31, 2008)
Published Print	30 years, 11 months ago (Sept. 1, 1994)

Funders 0

None

BibTeX

@article{Palczewski_1994, title={Structure and functions of arrestins}, volume={3}, ISSN={1469-896X}, url={http://dx.doi.org/10.1002/pro.5560030901}, DOI={10.1002/pro.5560030901}, number={9}, journal={Protein Science}, publisher={Wiley}, author={Palczewski, Krzysztof}, year={1994}, month=sep, pages={1355–1361} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2024,
        5,
        6
      ]
    ],
    "date-time": "2024-05-06T21:25:47Z",
    "timestamp": 1715030747002
  },
  "reference-count": 71,
  "publisher": "Wiley",
  "issue": "9",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2008,
            12,
            31
          ]
        ],
        "date-time": "2008-12-31T00:00:00Z",
        "timestamp": 1230681600000
      },
      "content-version": "vor",
      "delay-in-days": 5235,
      "URL": "http://onlinelibrary.wiley.com/termsAndConditions#vor"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        1994,
        9
      ]
    ]
  },
  "abstract": "<jats:title>Abstract</jats:title><jats:p>Transmembrane signal transductions in a variety of cell types that mediate signals as diverse as those carried by neurotransmitters, hormones, and sensory signals share basic biochemical mechanisms that include: (1) an extracellular perturbation (neurotransmitter, hormone, odor, light); (2) specific receptors; (3) coupling proteins, such as G proteins; and (4) effector enzymes or ion channels. Parallel to these amplification reactions, receptors are precisely inactivated by mechanisms that involve protein kinases and regulatory proteins called arrestins. The structure and functions of arrestins are the focus of this review.</jats:p>",
  "DOI": "10.1002/pro.5560030901",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2009,
        2,
        10
      ]
    ],
    "date-time": "2009-02-10T01:58:36Z",
    "timestamp": 1234231116000
  },
  "page": "1355-1361",
  "source": "Crossref",
  "is-referenced-by-count": 65,
  "title": "Structure and functions of arrestins",
  "prefix": "10.1002",
  "volume": "3",
  "author": [
    {
      "given": "Krzysztof",
      "family": "Palczewski",
      "sequence": "first",
      "affiliation": []
    }
  ],
  "member": "311",
  "published-online": {
    "date-parts": [
      [
        2008,
        12,
        31
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_2_1_2_1",
      "doi-asserted-by": "crossref",
      "first-page": "17882",
      "DOI": "10.1016/S0021-9258(19)37125-X",
      "article-title": "\u03b2\u2010Arrestin\u20102, a novel member of the arrestin/\u03b2\u2010arrestin gene family",
      "volume": "267",
      "author": "Attramadal H",
      "year": "1992",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_3_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00405a049"
    },
    {
      "key": "e_1_2_1_4_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.84.24.8879"
    },
    {
      "key": "e_1_2_1_5_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1993.tb18117.x"
    },
    {
      "key": "e_1_2_1_6_1",
      "doi-asserted-by": "crossref",
      "first-page": "15505",
      "DOI": "10.1016/S0021-9258(18)98645-X",
      "article-title": "Expression of S\u2010antigen in retina, pineal gland, lens, and brain is directed by 5\u2032\u2010flanking sequences",
      "volume": "266",
      "author": "Breitman ML",
      "year": "1991",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_7_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.88.6.2568"
    },
    {
      "key": "e_1_2_1_8_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(17)41820-5"
    },
    {
      "key": "e_1_2_1_9_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0888-7543(89)90075-X"
    },
    {
      "key": "e_1_2_1_10_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.8381559"
    },
    {
      "key": "e_1_2_1_11_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.8316831"
    },
    {
      "key": "e_1_2_1_12_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0167-4838(92)90403-Z"
    },
    {
      "key": "e_1_2_1_13_1",
      "doi-asserted-by": "crossref",
      "first-page": "17977",
      "DOI": "10.1016/S0021-9258(19)37139-X",
      "article-title": "Activation of bovine rod outer segment phospholipase C by arrestin",
      "volume": "267",
      "author": "Ghalayini AJ",
      "year": "1992",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_14_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(91)80530-G"
    },
    {
      "key": "e_1_2_1_15_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)36700-6"
    },
    {
      "key": "e_1_2_1_16_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)50248-4"
    },
    {
      "key": "e_1_2_1_17_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)85275-4"
    },
    {
      "key": "e_1_2_1_18_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bies.950150107"
    },
    {
      "key": "e_1_2_1_19_1",
      "first-page": "267",
      "volume-title": "Handbook of experimental pharmacology, vol 108/II. GTPases in biology II",
      "author": "Hofmann KP",
      "year": "1993"
    },
    {
      "key": "e_1_2_1_20_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)49592-6"
    },
    {
      "key": "e_1_2_1_21_1",
      "doi-asserted-by": "crossref",
      "first-page": "9470",
      "DOI": "10.1016/S0021-9258(19)38873-8",
      "article-title": "Ca2+ binding capacity of cytoplasmic proteins from rod photoreceptors is mainly due to arrestin",
      "volume": "265",
      "author": "Huppertz B",
      "year": "1990",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_22_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.87.3.1008"
    },
    {
      "key": "e_1_2_1_23_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(20)80439-6"
    },
    {
      "key": "e_1_2_1_24_1",
      "doi-asserted-by": "crossref",
      "first-page": "14675",
      "DOI": "10.1016/S0021-9258(18)98738-7",
      "article-title": "A 48\u2010kDa, S\u2010antigen\u2010like phosphoprotein in yeast DNA\u2010replicative complex preparations",
      "volume": "266",
      "author": "Jeansonne NE",
      "year": "1991",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_25_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0006-291X(88)80754-X"
    },
    {
      "key": "e_1_2_1_26_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0003-9861(91)90338-J"
    },
    {
      "key": "e_1_2_1_27_1",
      "doi-asserted-by": "crossref",
      "first-page": "3226",
      "DOI": "10.1016/S0021-9258(17)41852-7",
      "article-title": "Arrestin\u2010rhodopsin interaction. Multi\u2010site binding delineated by peptide inhibition",
      "volume": "269",
      "author": "Krupnick JG",
      "year": "1994",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_28_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0925-4773(90)90131-5"
    },
    {
      "key": "e_1_2_1_29_1",
      "doi-asserted-by": "crossref",
      "first-page": "8558",
      "DOI": "10.1016/S0021-9258(18)42479-9",
      "article-title": "Receptor\u2010specific desensitization with purified proteins. Kinase dependence and receptor specificity of \u03b2\u2010arrestin and arrestin in the \u03b22\u2010adrenergic receptor and rhodopsin systems",
      "volume": "267",
      "author": "Lohse MJ",
      "year": "1992",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_30_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.2163110"
    },
    {
      "key": "e_1_2_1_31_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0896-6273(94)90309-3"
    },
    {
      "key": "e_1_2_1_32_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0006-291X(91)90683-X"
    },
    {
      "key": "e_1_2_1_33_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00069a036"
    },
    {
      "key": "e_1_2_1_34_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(93)81712-9"
    },
    {
      "key": "e_1_2_1_35_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0888-7543(90)90521-U"
    },
    {
      "key": "e_1_2_1_36_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.90.8.3241"
    },
    {
      "key": "e_1_2_1_37_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00170a022"
    },
    {
      "key": "e_1_2_1_38_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00072a030"
    },
    {
      "key": "e_1_2_1_39_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0968-0004(91)90157-Q"
    },
    {
      "key": "e_1_2_1_40_1",
      "doi-asserted-by": "crossref",
      "first-page": "15334",
      "DOI": "10.1016/S0021-9258(18)98620-5",
      "article-title": "Role of the carboxyl\u2010terminal region of arrestin in binding to phosphorylated rhodopsin",
      "volume": "266",
      "author": "Palczewski K",
      "year": "1991",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_41_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/pro.5560030215"
    },
    {
      "key": "e_1_2_1_42_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(20)64307-1"
    },
    {
      "key": "e_1_2_1_43_1",
      "doi-asserted-by": "crossref",
      "first-page": "15770",
      "DOI": "10.1016/S0021-9258(18)71543-3",
      "article-title": "Regulation of rhodopsin dephosphorylation by arrestin",
      "volume": "264",
      "author": "Palczewski K",
      "year": "1989",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_44_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(91)81416-6"
    },
    {
      "key": "e_1_2_1_45_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(18)55112-7"
    },
    {
      "key": "e_1_2_1_46_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00131a003"
    },
    {
      "key": "e_1_2_1_47_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0896-6273(92)90113-R"
    },
    {
      "key": "e_1_2_1_48_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00074a002"
    },
    {
      "key": "e_1_2_1_49_1",
      "doi-asserted-by": "crossref",
      "first-page": "9753",
      "DOI": "10.1016/S0021-9258(18)98412-7",
      "article-title": "Molecular analysis of human \u03b2\u2010arrestin\u20101: Cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing",
      "volume": "268",
      "author": "Parruti G",
      "year": "1993",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_50_1",
      "doi-asserted-by": "crossref",
      "first-page": "3201",
      "DOI": "10.1016/S0021-9258(18)53678-4",
      "article-title": "Overexpression of \u03b2\u2010arrestin and \u03b2\u2010adrenergic receptor kinase augment desensitization of \u03b22\u2010adrenergic receptors",
      "volume": "268",
      "author": "Pippig S",
      "year": "1993",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_51_1",
      "first-page": "1248",
      "article-title": "Effect of sulfhydryl group modification on arrestin interaction with phosphorylated rhodopsin",
      "volume": "6",
      "author": "Pogozheva ID",
      "year": "1989",
      "journal-title": "Biol Membr"
    },
    {
      "key": "e_1_2_1_52_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00214a002"
    },
    {
      "key": "e_1_2_1_53_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(93)80609-X"
    },
    {
      "key": "e_1_2_1_54_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0303-7207(92)90038-8"
    },
    {
      "key": "e_1_2_1_55_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00430a052"
    },
    {
      "key": "e_1_2_1_56_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.84.20.6975"
    },
    {
      "key": "e_1_2_1_57_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0278-4327(88)90020-X"
    },
    {
      "key": "e_1_2_1_58_1",
      "first-page": "197",
      "article-title": "The structure of bovine retinal S\u2010antigen: Sequence analysis and identification of monoclonal antibody epitopes and uveitogenic site",
      "volume": "31",
      "author": "Shinohara T",
      "year": "1987",
      "journal-title": "Jpn J Ophthalmol"
    },
    {
      "key": "e_1_2_1_59_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0305-0491(92)90361-T"
    },
    {
      "key": "e_1_2_1_60_1",
      "doi-asserted-by": "crossref",
      "first-page": "15407",
      "DOI": "10.1016/S0021-9258(17)40691-0",
      "article-title": "Splice variant of arrestin: Molecular cloning and localization in bovine retina",
      "volume": "269",
      "author": "Smith CW",
      "year": "1994",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_61_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.87.3.1003"
    },
    {
      "key": "e_1_2_1_62_1",
      "doi-asserted-by": "crossref",
      "first-page": "15640",
      "DOI": "10.1016/S0021-9258(18)82304-3",
      "article-title": "Polypeptide variants of \u03b2\u2010arrestin and arrestin 3",
      "volume": "268",
      "author": "Sterne\u2010Marr R",
      "year": "1993",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_63_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1991.tb21053.x"
    },
    {
      "key": "e_1_2_1_64_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0378-1119(88)90308-3"
    },
    {
      "key": "e_1_2_1_65_1",
      "doi-asserted-by": "crossref",
      "first-page": "1949",
      "DOI": "10.4049/jimmunol.119.6.1949",
      "article-title": "Experimental allergic uveitis. Isolation, characterization, and localization of a soluble uveitopathogenic antigen from bovine retina",
      "volume": "119",
      "author": "Wacker WB",
      "year": "1977",
      "journal-title": "J Immunol"
    },
    {
      "key": "e_1_2_1_66_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(88)81242-0"
    },
    {
      "key": "e_1_2_1_67_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1990.tb19360.x"
    },
    {
      "key": "e_1_2_1_68_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.83.5.1174"
    },
    {
      "key": "e_1_2_1_69_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.2158671"
    },
    {
      "key": "e_1_2_1_70_1",
      "doi-asserted-by": "crossref",
      "first-page": "20757",
      "DOI": "10.1016/S0021-9258(17)45280-X",
      "article-title": "Structural organization of the human S\u2010antigen gene. cDNA, amino acid, intron, exon, promoter, in vitro transcription, retina, and pineal gland",
      "volume": "265",
      "author": "Yamaki K",
      "year": "1990",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_1_71_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(86)80008-4"
    },
    {
      "key": "e_1_2_1_72_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(88)80516-7"
    }
  ],
  "container-title": "Protein Science",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fpro.5560030901",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.5560030901",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        10,
        24
      ]
    ],
    "date-time": "2023-10-24T12:52:19Z",
    "timestamp": 1698151939000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://onlinelibrary.wiley.com/doi/10.1002/pro.5560030901"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1994,
        9
      ]
    ]
  },
  "references-count": 71,
  "journal-issue": {
    "issue": "9",
    "published-print": {
      "date-parts": [
        [
          1994,
          9
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1002/pro.5560030901"
  ],
  "URL": "http://dx.doi.org/10.1002/pro.5560030901",
  "relation": {},
  "ISSN": [
    "0961-8368",
    "1469-896X"
  ],
  "subject": [],
  "container-title-short": "Protein Science",
  "published": {
    "date-parts": [
      [
        1994,
        9
      ]
    ]
  }
}