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  • Journals  (63)
  • Articles  (330,789)
  • Wiley  (309,206)
  • Annual Reviews
  • Periodicals Archive Online (PAO)
  • Medicine  (224,172)
  • Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition  (106,681)
Collection
  • Journals  (63)
  • Articles  (330,789)
Years
Journal
Media Type
  • 1
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    Wiley | American Fisheries Society | formerly Taylor & Francis
    Online: 58(2).1996 –
    Online: 58.1996 –
    Publisher: Wiley , American Fisheries Society , formerly Taylor & Francis
    Print ISSN: 0033-0779 , 1522-2055
    Electronic ISSN: 1548-8454 , 1548-8640
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 2
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    Wiley
    Online: 1(1).2016 –
    Publisher: Wiley
    Electronic ISSN: 2380-6761
    Topics: Medicine , Technology
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  • 3
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    Wiley | American Association of Cereal Chemists
    Online: 74.1997 –
    Online: 74.1997 –
    Publisher: Wiley , American Association of Cereal Chemists
    Print ISSN: 0009-0352
    Electronic ISSN: 1943-3638
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
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  • 4
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    Wiley
    Online: 1(1).1982 –
    Publisher: Wiley
    Print ISSN: 0277-6715
    Electronic ISSN: 1097-0258
    Topics: Mathematics , Medicine
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  • 5
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    Wiley | American Fisheries Society | formerly Taylor & Francis
    Online: 125.1996 –
    Online: 125.1996 –
    Publisher: Wiley , American Fisheries Society , formerly Taylor & Francis
    Print ISSN: 0002-8487
    Electronic ISSN: 1548-8659
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 6
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    Wiley
    Online: 61.1997 –
    Online: 61.1997 –
    Publisher: Wiley
    Print ISSN: 0009-9236
    Electronic ISSN: 1532-6535
    Topics: Chemistry and Pharmacology , Medicine
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  • 7
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    Wiley
    Online: 1(1).1980 – 50(6).2002
    Publisher: Wiley
    Print ISSN: 0196-4763
    Electronic ISSN: 1097-0320
    Topics: Biology , Medicine
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  • 8
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    Wiley
    Online: 1.2006 –
    Online: 1.2006 –
    Publisher: Wiley
    Print ISSN: 1860-7179
    Electronic ISSN: 1860-7187
    Topics: Chemistry and Pharmacology , Medicine
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  • 9
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    Wiley | American Society of Agronomy, Crop Science Society of America, and Soil Science Society of America
    Online: 26.1997 –
    Online: 26.1997 –
    Publisher: Wiley , American Society of Agronomy, Crop Science Society of America, and Soil Science Society of America
    Corporation: American Society of Agronomy, ASA , Crop Science Society of America, CSSA , Soil Science Society of America, SSSA
    Print ISSN: 0047-2425
    Electronic ISSN: 1537-2537
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Acronym: JEQ
    Abbreviation: J Env Qual
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  • 10
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    Wiley | Soil Science Society of America
    Online: 61.1997 –
    Online: 61.1997 –
    Publisher: Wiley , Soil Science Society of America
    Print ISSN: 0361-5995
    Electronic ISSN: 1435-0661
    Topics: Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Acronym: SSSAJ
    Abbreviation: Soil Sci Soc Am J
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  • 11
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    Wiley | The Institution of Engineering and Technology and Shenzhen University
    Online: 1(1).2019 –
    Publisher: Wiley , The Institution of Engineering and Technology and Shenzhen University
    Electronic ISSN: 2517-7567
    Topics: Computer Science , Medicine , Psychology
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  • 12
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    Wiley
    Online: 1(1).2019 –
    Publisher: Wiley
    Electronic ISSN: 2639-6181
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 13
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    Wiley | American Society of Agronomy
    Online: 26.1997 –
    Online: 26.1997 –
    Publisher: Wiley , American Society of Agronomy
    Print ISSN: 1059-9053 , 2168-8273
    Electronic ISSN: 1539-1582 , 2168-8281
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 14
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    Wiley
    Online: (1).2010 – (older than 1 month)
    Publisher: Wiley
    Print ISSN: 0176-053X
    Topics: Medicine , Economics
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  • 15
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    Wiley | American Association of Physicists in Medicine
    Online: 24.1997 –
    Online: 24.1997 –
    Publisher: Wiley , American Association of Physicists in Medicine
    Print ISSN: 0094-2405
    Electronic ISSN: 1522-8541 , 2473-4209
    Topics: Medicine , Physics
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  • 16
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    Wiley
    Online: 2(1).2001 – 6(8).2005
    Publisher: Wiley
    Print ISSN: 1531-6912
    Electronic ISSN: 1532-6268
    Topics: Biology , Medicine
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  • 17
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    Wiley | American Society of Agronomy | Crop Science Society of America | Soil Science Society of America
    Online: 42(11).1997 –
    Online: 42(11).1997 –
    Formerly as: Agronomy News; Crop Science, Soil Science, Agronomy News  (–)
    Publisher: Wiley , American Society of Agronomy , Crop Science Society of America , Soil Science Society of America
    Print ISSN: 1529-9163
    Electronic ISSN: 2325-3584
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 18
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    Wiley | Crop Science Society of America
    Online: 37.1997 –
    Online: 37.1997 –
    Publisher: Wiley , Crop Science Society of America
    Print ISSN: 0011-183X
    Electronic ISSN: 1435-0653
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 19
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    Wiley
    Online: 1(1).2004 –
    Publisher: Wiley
    Electronic ISSN: 2397-8325
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 20
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    Wiley
    Online: 1(1).2019 –
    Publisher: Wiley
    Electronic ISSN: 2573-9832
    Topics: Biology , Medicine
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  • 21
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    Wiley
    Online: 1.2018 –
    Online: 1.2018 –
    Publisher: Wiley
    Electronic ISSN: 2573-8488
    Topics: Chemistry and Pharmacology , Medicine
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  • 22
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    Wiley
    Online: 43.2003 – 47.2007
    Publisher: Wiley
    Print ISSN: 0041-3291
    Electronic ISSN: 1556-9179
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 23
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    Wiley | American Society of Agronomy, Crop Science Society of America
    Online: 1(1).2016 –
    Publisher: Wiley , American Society of Agronomy, Crop Science Society of America
    Print ISSN: 2352-0566
    Electronic ISSN: 2352-0574 , 2575-1220
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 24
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    Wiley
    Online: 3(3).1995 – 6(4).1998
    Publisher: Wiley
    Print ISSN: 0966-9051
    Electronic ISSN: 1361-6374
    Topics: Biology , Medicine
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  • 25
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    Wiley | JSTOR | formerly Oxford University Press (OUP)
    Online: 10(1).1988 –
    Formerly as: Illinois Agricultural Economics; North Central Journal of Agricultural Economics; Review of Agricultural Economics  (1961–2009)
    Publisher: Wiley , JSTOR , formerly Oxford University Press (OUP)
    Print ISSN: 0191-9016 , 1058-7195 , 2040-5790
    Electronic ISSN: 1467-9353 , 2040-5804
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Economics
    Keywords: JSTOR Archive Collection Business II
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  • 26
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    Wiley
    Online: 80.1997 –
    Online: 80.1997 –
    Publisher: Wiley
    Print ISSN: 0001-6683 , 0901-9928 , 1742-7835
    Electronic ISSN: 1600-0773 , 1742-7843
    Topics: Chemistry and Pharmacology , Medicine
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  • 27
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    Annual Reviews
    Online: 1.1999 – 18.2016
    Online: 1.1999 – 18.2016
    Online: 1.2021 –
    Publisher: Annual Reviews
    Print ISSN: 1523-9829
    Electronic ISSN: 1545-4274
    Topics: Medicine , Technology
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  • 28
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    Annual Reviews
    Online: 1.2017 –
    Publisher: Annual Reviews
    Electronic ISSN: 2472-3428
    Topics: Biology , Medicine
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  • 29
    Journal cover
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    Annual Reviews
    Online: 1.1983 – 34.2016
    Online: 1.1983 – 34.2016
    Publisher: Annual Reviews
    Print ISSN: 0732-0582
    Electronic ISSN: 1545-3278
    Topics: Biology , Medicine
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  • 30
    Journal cover
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    Annual Reviews
    Online: 1.1985 – 32.2016
    Online: 1.1985 – 32.2016
    Formerly as: Annual Review of Cell Biology  (1985–1994)
    Publisher: Annual Reviews
    Print ISSN: 0743-4634 , 1081-0706
    Electronic ISSN: 1530-8995
    Topics: Biology , Medicine
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  • 31
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    Annual Reviews
    Online: 1.1939 – 78.2016
    Online: 1.1939 – 78.2016
    Publisher: Annual Reviews
    Print ISSN: 0066-4278
    Electronic ISSN: 1545-1585
    Topics: Biology , Medicine
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  • 32
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    Wiley | American Society of Agronomy
    Online: 89.1997 –
    Online: 89.1997 –
    Publisher: Wiley , American Society of Agronomy
    Print ISSN: 0002-1962
    Electronic ISSN: 1435-0645
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 33
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    Wiley | formerly Oxford University Press (OUP)
    Online: 1.1919 –
    Formerly as: Journal of Farm Economics  (1919–1967)
    Publisher: Wiley , formerly Oxford University Press (OUP)
    Print ISSN: 0002-9092
    Electronic ISSN: 1467-8276
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Economics
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  • 34
    Journal cover
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    Annual Reviews
    Online: 1.1978 – 39.2016
    Online: 1.1978 – 39.2016
    Publisher: Annual Reviews
    Print ISSN: 0147-006X
    Electronic ISSN: 1545-4126
    Topics: Biology , Medicine
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  • 35
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    Annual Reviews
    Online: 1.1961 – 56.2016
    Online: 1.1961 – 56.2016
    Formerly as: Annual Review of Pharmacology  (1961–1975)
    Publisher: Annual Reviews
    Print ISSN: 0066-4251 , 0362-1642
    Electronic ISSN: 1545-4304
    Topics: Chemistry and Pharmacology , Medicine
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  • 36
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    Annual Reviews
    Online: 1.1963 – 54.2016
    Online: 1.1963 – 54.2016
    Publisher: Annual Reviews
    Print ISSN: 0066-4286
    Electronic ISSN: 1545-2107
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 37
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    Wiley | American Society of Agronomy, Crop Science Society of America, Soil Science Society of America
    Online: 1(1).2016 –
    Publisher: Wiley , American Society of Agronomy, Crop Science Society of America, Soil Science Society of America
    Electronic ISSN: 2471-9625
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 38
    Journal cover
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    Wiley | Alliance of Crop, Soil and Environmental Science Societies (ACSESS)
    Online: 1(1).2018 –
    Publisher: Wiley , Alliance of Crop, Soil and Environmental Science Societies (ACSESS)
    Electronic ISSN: 2639-6696
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 39
    Journal cover
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    Wiley
    Online: 116.2003 –
    Online: 116.2003 –
    Formerly as: American Journal of Medical Genetics  (1977–2002)
    Publisher: Wiley
    Print ISSN: 0148-7299 , 1552-4825
    Electronic ISSN: 1096-8628 , 1552-4833
    Topics: Biology , Medicine
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  • 40
    Journal cover
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    Annual Reviews
    Online: 1.1981 – 36.2016
    Online: 1.1981 – 36.2016
    Publisher: Annual Reviews
    Print ISSN: 0199-9885
    Electronic ISSN: 1545-4312
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 41
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    Wiley
    Online: 11.1997 –
    Online: 11.1997 –
    Publisher: Wiley
    Print ISSN: 0767-3981
    Electronic ISSN: 1472-8206
    Topics: Chemistry and Pharmacology , Medicine
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  • 42
    Journal cover
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    Wiley | American Geophysical Union
    Online: 1.2017 –
    Publisher: Wiley , American Geophysical Union
    Electronic ISSN: 2471-1403
    Topics: Geosciences , Medicine
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  • 43
    Journal cover
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    Wiley | American Society of Agronomy and the Crop Science Society of America
    Online: 1.2015 –
    Online: 1.2015 –
    Publisher: Wiley , American Society of Agronomy and the Crop Science Society of America
    Electronic ISSN: 2374-3832
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 44
    Journal cover
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    Wiley | American Society of Agronomy
    Online: 40.2007 –
    Online: 40.2007 –
    Publisher: Wiley , American Society of Agronomy
    Print ISSN: 0162-5098
    Electronic ISSN: 2325-3606
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 45
    Formerly as: Cytometry  (1980–2002)
    Publisher: Wiley
    Corporation: International Society for Analytical Cytology, ISAC
    Print ISSN: 1552-4949
    Electronic ISSN: 1552-4957
    Topics: Biology , Medicine
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  • 46
    Journal cover
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    Wiley | American Society of Agronomy and Crop Science Society of America
    Online: 1(1).2018 –
    Publisher: Wiley , American Society of Agronomy and Crop Science Society of America
    Electronic ISSN: 2578-2703
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 47
    Journal cover
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    Wiley | American Fisheries Society | formerly Taylor & Francis
    Online: 16.1996 –
    Online: 16.1996 –
    Publisher: Wiley , American Fisheries Society , formerly Taylor & Francis
    Print ISSN: 0275-5947
    Electronic ISSN: 1548-8675
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 48
    Journal cover
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    Wiley
    Online: 1(1).1987 –
    Publisher: Wiley
    Print ISSN: 0951-418X
    Electronic ISSN: 1099-1573
    Topics: Chemistry and Pharmacology , Medicine
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  • 49
    Journal cover
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    Wiley
    Online: 1(1).1992 –
    Publisher: Wiley
    Print ISSN: 1053-8569
    Electronic ISSN: 1099-1557
    Topics: Chemistry and Pharmacology , Medicine
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  • 50
    Journal cover
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    Wiley
    Online: 1(1).1982 –
    Formerly as: Quantitative Structure-Activity Relationships / QSAR and Combinatorial Science  (1982–2009)
    Publisher: Wiley
    Print ISSN: 0722-3676 , 0931-8771 , 1611-020X , 1868-1743
    Electronic ISSN: 1521-3838 , 1611-0218 , 1868-1751
    Topics: Chemistry and Pharmacology , Medicine
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  • 51
    Journal cover
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    Wiley
    Online: 1(1).1966 –
    Publisher: Wiley
    Print ISSN: 0020-7136
    Electronic ISSN: 1097-0215
    Topics: Biology , Medicine
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  • 52
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    International Turfgrass Society | Wiley
    Online: 13.2017 –
    Publisher: International Turfgrass Society , Wiley
    Print ISSN: 1817-0641
    Electronic ISSN: 2573-1513
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 53
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    Wiley | formerly Taylor & Francis
    Online: 1.2012 –
    Publisher: Wiley , formerly Taylor & Francis
    Electronic ISSN: 2001-3078
    Topics: Biology , Medicine
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  • 54
    Publisher: Wiley
    Print ISSN: 0021-9754 , 0091-2700 , 0095-9863 , 0096-0284
    Electronic ISSN: 1552-4604
    Topics: Chemistry and Pharmacology , Medicine
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  • 55
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    Wiley
    Online: 1.1990 – 6.1995
    Publisher: Wiley
    Print ISSN: 1045-4861
    Electronic ISSN: 1549-9316
    Topics: Medicine , Technology
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  • 56
    facet.materialart.
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    Wiley | American Fisheries Society | formerly Taylor & Francis
    Online: 8.1996 –
    Online: 8.1996 –
    Publisher: Wiley , American Fisheries Society , formerly Taylor & Francis
    Print ISSN: 0899-7659
    Electronic ISSN: 1548-8667
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Medicine
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  • 57
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    Wiley
    Online: 1(1).2013 –
    Publisher: Wiley
    Electronic ISSN: 2048-7177
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 58
    Journal cover
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    Wiley | American Fisheries Society | formerly Taylor & Francis
    Online: 21.1996 –
    Online: 21.1996 –
    Publisher: Wiley , American Fisheries Society , formerly Taylor & Francis
    Print ISSN: 0363-2415
    Electronic ISSN: 1548-8446
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 59
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    Wiley
    Online: 1(1).2012 –
    Publisher: Wiley
    Electronic ISSN: 2048-3694
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 60
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    Wiley
    Online: 1(1).2020 –
    Publisher: Wiley
    Electronic ISSN: 2643-8429
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 61
    Journal cover
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    Wiley | Crop Science Society of America
    Online: 1.2007 –
    Online: 1.2007 –
    Publisher: Wiley , Crop Science Society of America
    Print ISSN: 1936-5209
    Electronic ISSN: 1940-3496
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
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  • 62
    Journal cover
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    Wiley | Soil Science Society of America (SSSA)
    Online: 17.2018 –
    Publisher: Wiley , Soil Science Society of America (SSSA)
    Corporation: Soil Science Society of America, SSSA
    Electronic ISSN: 1539-1663
    Topics: Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Acronym: VZJ
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  • 63
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    Wiley | Policy Studies Organization (PSO) | Royal Institute of Thailand
    Online: 1.2014 –
    Publisher: Wiley , Policy Studies Organization (PSO) , Royal Institute of Thailand
    Electronic ISSN: 2372-8639
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Political Science
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  • 64
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 11 (1995), S. 35-71 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 65
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 11 (1995), S. 241-265 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 66
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 11 (1995), S. 497-518 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 67
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 11 (1995), S. 633-675 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 68
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 12 (1996), S. 1-26 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Most chloroplast proteins are nuclear encoded, synthesized as larger precursor proteins in the cytosol, posttranslationally imported into the organelle, and routed to one of six different compartments. Import across the outer and inner envelope membranes into the stroma is the major means for entry of proteins destined for the stroma, the thylakoid membrane, and the thylakoid lumen. Recent investigations have identified several unique protein components of the envelope translocation machinery. These include two GTP-binding proteins that appear to participate in the early events of import and probably regulate precursor recognition and advancement into the translocon. Localization of imported precursor proteins to the thylakoid membrane and thylakoid lumen is accomplished by four distinct mechanisms; two are homologous to bacterial and endoplasmic reticulum protein transport systems, one appears unique, and the last may be a spontaneous mechanism. Thus chloroplast protein targeting is a unique and surprisingly complex process. The presence of GTP-binding proteins in the envelope translocation machinery indicates a different precursor recognition process than is present in mitochondria. Mechanisms for thylakoid protein localization are in part derived from the prokaryotic endosymbiont, but are more unusual and diverse than expected.
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    Annual Review of Cell and Developmental Biology 12 (1996), S. 181-220 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Receptors for the Fc domain of immunoglobulins play an important role in immune defense. There are two well-defined functional classes of mammalian receptors. One class of receptors transports immunoglobulins across epithelial tissues to their main sites of action. This class includes the neonatal Fc receptor (FcRn), which transports immunoglobulin G (IgG), and the polymeric immunoglobulin receptor (pIgR), which transports immunoglobulin A (IgA) and immunoglobulin M (IgM). Another class of receptors present on the surfaces of effector cells triggers various biological responses upon binding antibody-antigen complexes. Of these, the IgG receptors (FcgammaR) and immunoglobulin E (IgE) receptors (FcepsilonR) are the best characterized. The biological responses elicited include antibody-dependent, cell-mediated cytotoxicity, phagocytosis, release of inflammatory mediators, and regulation of lymphocyte proliferation and differentiation. We summarize the current knowledge of the structures and functions of FcRn, pIgR, and the FcgammaR and FcepsilonRI proteins, concentrating on the interactions of the extracellular portions of these receptors with immunoglobulins.
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    Annual Review of Cell and Developmental Biology 12 (1996), S. 335-363 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Peroxisome proliferator-activated receptors (PPARs) are lipid-activated transcription factors that belong to the steroid/thyroid/retinoic acid receptor superfamily. All their characterized target genes encode proteins that participate in lipid homeostasis. The recent finding that antidiabetic thiazolidinediones and adipogenic prostanoids are ligands of one of the PPARs reveals a novel signaling pathway that directly links these compounds to processes involved in glucose homeostasis and lipid metabolism including adipocyte differentiation. A detailed understanding of this pathway could designate PPARs as targets for the development of novel efficient treatments for several metabolic disorders.
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    Annual Review of Cell and Developmental Biology 12 (1996), S. 441-461 
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    Notes: Abstract Proteins that function in transport vesicle docking are being identified at a rapid rate. So-called v- and t-SNAREs form the core of a vesicle docking complex. Additional accessory proteins are required to protect SNAREs from promiscuous binding and to deprotect SNAREs under conditions in which transport vesicle docking should occur. Because access to SNAREs must be regulated, other proteins must also contain specificity determinants to accomplish delivery of transport vesicles to their distinct and specific membrane targets.
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    Annual Review of Cell and Developmental Biology 12 (1996), S. 417-439 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Myosin is a highly conserved, ubiquitous protein found in all eukaryotic cells, where it provides the motor function for diverse movements such as cytokinesis, phagocytosis, and muscle contraction. All myosins contain an amino-terminal motor/head domain and a carboxy-terminal tail domain. Due to the extensive number of different molecules identified to date, myosins have been divided into seven distinct classes based on the properties of the head domain. One such class, class II myosins, consists of the conventional two-headed myosins that form filaments and are composed of two myosin heavy chain (MYH) subunits and four myosin light chain subunits. The MYH subunit contains the ATPase activity providing energy that is the driving force for contractile processes mentioned above, and numerous MYH isoforms exist in vertebrates to carry out this function. The MYHs involved in striated muscle contraction in mammals are the focus of the current review. The genetics, molecular biology, and biochemical properties of mammalian MYHs are discussed below. MYH gene expression patterns in developing and adult striated muscles are described in detail, as are studies of regulation of MYH genes in the heart. The discovery that mutant MYH isoforms have a causal role in the human disease familial hypertrophic cardiomyopathy (FHC) has implemented structure/function investigations of MYHs. The regulation of MYH genes expressed in skeletal muscle and the potential functional implications that distinct MYH isoforms may have on muscle physiology are addressed.
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    Annual Review of Cell and Developmental Biology 12 (1996), S. 697-715 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Proteins that contain the Arg-Gly-Asp (RGD) attachment site, together with the integrins that serve as receptors for them, constitute a major recognition system for cell adhesion. The RGD sequence is the cell attachment site of a large number of adhesive extracellular matrix, blood, and cell surface proteins, and nearly half of the over 20 known integrins recognize this sequence in their adhesion protein ligands. Some other integrins bind to related sequences in their ligands. The integrin-binding activity of adhesion proteins can be reproduced by short synthetic peptides containing the RGD sequence. Such peptides promote cell adhesion when insolubilized onto a surface, and inhibit it when presented to cells in solution. Reagents that bind selectively to only one or a few of the RGD-directed integrins can be designed by cyclizing peptides with selected sequences around the RGD and by synthesizing RGD mimics. As the integrin-mediated cell attachment influences and regulates cell migration, growth, differentiation, and apoptosis, the RGD peptides and mimics can be used to probe integrin functions in various biological systems. Drug design based on the RGD structure may provide new treatments for diseases such as thrombosis, osteoporosis, and cancer.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 1-23 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Transcriptional regulation is important in all eukaryotic organisms for cell growth, development, and responses to environmental change. Saccharomyces cerevisiae, or bakers' yeast, has provided a powerful system for genetic analysis of transcriptional regulation, and findings from the study of this model system have proven broadly applicable to higher organisms. Transcriptional regulation requires the interactions of regulatory proteins with various components of the transcription machinery. Recently, genetic analysis of a diverse set of transcriptional regulatory responses has converged with studies of the function of the RNA polymerase II carboxy-terminal domain (CTD) to reveal regulatory roles for proteins associated with the CTD. These proteins, designated Srb/mediator proteins, are broadly involved in both positive and negative regulatory responses in vivo. This review focuses on the connections between genetic analysis of transcriptional regulation and the functions of the Srb/mediator proteins associated with the RNA polymerase II CTD.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 53-82 
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    Notes: Abstract Most animal species exhibit left-right asymmetry in their body plans and show a strong bias for one handedness over the other. The mechanism of handedness choice, recognized as an intriguing problem over a century ago, is still a mystery. However, from recent advances in understanding when and how asymmetry arises in both invertebrates and vertebrates, developmental pathways for establishment and maintenance of left-right differences are beginning to take shape, and speculations can be made on the initial choice mechanism.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 83-117 
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    Notes: Abstract The polymerization dynamics of microtubules are central to their biological functions. Polymerization dynamics allow microtubules to adopt spatial arrangements that can change rapidly in response to cellular needs and, in some cases, to perform mechanical work. Microtubules utilize the energy of GTP hydrolysis to fuel a unique polymerization mechanism termed dynamic instability. In this review, we first describe progress toward understanding the mechanism of dynamic instability of pure tubulin and then discuss the function and regulation of microtubule dynamic instability in living cells.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 25-51 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Mitochondria import most of their proteins from the cytosol. Dynamic protein complexes in the mitochondrial outer and inner membranes are responsible for the specific recognition and membrane translocation of preproteins. The preprotein translocase of the outer mitochondrial membrane contains several import receptors and a general import pore. The preprotein translocase of the inner membrane consists of a channel interacting with preproteins in transit and an import motor that includes the matrix heat shock protein Hsp70. Acidic patches of import components are thought to guide the import of positively charged signal sequences (acid chain hypothesis). Energy input is derived from the inner membrane potential and ATP. Proteins in the mitochondrial matrix are required for proteolytic processing and folding of imported proteins. The dynamic nature of the membrane translocase permits sorting of preproteins at distinct stages of the import pathway.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 119-146 
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    Notes: Abstract Adherens junctions are specialized forms of cadherin-based adhesive contacts important for tissue organization in developing and adult organisms. Cadherins form protein complexes with cytoplasmic proteins (catenins) that convert the specific, homophilic-binding capacity of the extracellular domain into stable cell adhesion. The extracellular domains of cadherins form parallel dimers that possess intrinsic homophilic-binding activity. Cytoplasmic interactions can influence the function of the ectodomain by a number of potential mechanisms, including redistribution of binding sites into clusters, providing cytoskeletal anchorage, and mediating physiological regulation of cadherin function. Adherens junctions are likely to serve specific, specialized functions beyond the basic adhesive process. These functions include coupling cytoskeletal force generation to strongly adherent sites on the cell surface and the regulation of intracellular signaling events.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 147-170 
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    Notes: Abstract The Drosophila ovary provides a favorable model system in which to study cellular morphogenesis. The development of a mature egg involves a syncytium of 16 germline cells and over 1000 somatically derived follicle cells. Intercellular transport, stable intercellular bridges, cell migrations, cell shape changes, and specific subcellular localization of many embryonic patterning determinants contribute to egg development and require a dynamic cytoskeleton. We discuss many of the recent genetic and cell biological studies that have led to insights into how the actin cytoskeleton is assembled and regulated during the morphogenesis of the Drosophila egg.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 333-361 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Notch, LIN-12, and GLP-1 are receptors that mediate a broad range of cell interactions during Drosophila and nematode development. Signaling by these receptors relies on a conserved pathway with three core components: DSL ligand, LNG receptor, and a CSL effector that links the receptor to its transcriptional response. Although key functional regions have been identified in each class of proteins, the mechanism for signal transduction is not yet understood. Diverse regulatory mechanisms influence signaling by the LIN-12/Notch pathway. Inductive signaling relies on the synthesis of ligand and receptor in distinct but neighboring cells. By contrast, lateral signaling leads to the transformation of equivalent cells that express both ligand and receptor into nonequivalent cells that express either ligand or receptor. This transformation appears to rely on regulatory feedback loops within the LIN-12/Notch pathway. In addition, the pathway can be regulated by intrinsic factors that are asymmetrically segregated during cell division or by extrinsic cues via other signaling pathways. Specificity in the pathway does not appear to reside in the particular ligand or receptor used for a given cell-cell interaction. The existence of multiple ligands and receptors may have evolved from the stringent demands placed upon the regulation of genes encoding them.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 363-393 
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    Notes: Abstract Molecules involved in cell adhesion processes are often both structurally and functionally modular, with subdomains that are members of large protein families. Recently, high-resolution structures have been determined for representative members of many of these families including fragments of integrins, cadherins, fibronectin-like domains, and immunoglobulin-like domains. These structures have enhanced our understanding of cell adhesion processes at several levels. In almost all cases, ligand-binding sites have been visualized and provide insight into how these molecules mediate biologically important interactions. Metal-binding sites have been identified and characterized, allowing assessment of the role of bound ions in cell adhesion processes. Many of these structures serve as templates for modeling homologous domains in other proteins or, when the structure of a fragment consisting of more than one domain is determined, the structure of multidomain arrays of homologous domains. Knowledge of atomic structure also allows rational design of drugs that either mimic or target specific binding sites. In many cases, high-resolution structures have revealed unexpected relationships that pose questions about the evolutionary origin of specific domains. This review briefly describes several recently determined structures of cell adhesion molecules, summarizes some of the main results of each structure, and highlights common features of different systems.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 395-424 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Bacteria usually divide by building a central septum across the middle of the cell. This review focuses on recent results indicating that the tubulin-like FtsZ protein plays a central role in cytokinesis as a major component of a contractile cytoskeleton. Assembly of this cytoskeletal element abutting the membrane is a key point for regulation. The characterization of FtsZ homologues in Mycoplasmas, Archaea, and chloroplasts implies that the constriction mechanism is conserved and that FtsZ can constrict in the absence of peptidoglycan synthesis. In most Eubacteria, the internal cytoskeleton must also regulate synthesis of septal peptidoglycan. The Escherichia coli septum-specific penicillin-binding protein 3 (PBP3) forms a complex with other enzymes involved in murein metabolism, suggesting a centrally located transmembrane complex capable of splicing multiple new strands of peptidoglycan into the cell wall. Important questions remain about the spatial and temporal control of bacterial division.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 425-456 
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    Notes: Abstract NCAM, L1, and DCC-immunoglobulin cell adhesion molecules (Ig CAMs)-are widely expressed during development. Many workers have dismissed a role for such molecules in the control of axonal growth and guidance because they do not show highly restricted expression patterns. Yet evidence from a number of model systems suggests all three CAMs play a role in the development of specific projections in the nervous system. For example, there is a reduction in mossy fiber tracts in the hippocampus of mice that lack NCAM, a requirement for DCC in the response of commissural neurons to a floor plate-derived chemoattractant, and a loss of corticospinal tracts in humans who carry mutations in the L1 gene. The above paradox might be explained by the observation that differential post-translational processing can modulate CAMs function and that alternative splicing can generate functionally distinct isoforms of a CAM. Activation of the FGF tyrosine kinase receptor is required for the responses stimulated by NCAM and L1, and the importance of regulated tyrosine phosphorylation for growth and guidance is underscored by the involvement of receptor tyrosine phosphatases in this process.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 513-609 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Src family protein tyrosine kinases are activated following engagement of many different classes of cellular receptors and participate in signaling pathways that control a diverse spectrum of receptor-induced biological activities. While several of these kinases have evolved to play distinct roles in specific receptor pathways, there is considerable redundancy in the functions of these kinases, both with respect to the receptor pathways that activate these kinases and the downstream effectors that mediate their biological activities. This chapter reviews the evidence implicating Src family kinases in specific receptor pathways and describes the mechanisms leading to their activation, the targets that interact with these kinases, and the biological events that they regulate.
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    Notes: Abstract The chemosensory pathway of bacterial chemotaxis has become a paradigm for the two-component superfamily of receptor-regulated phosphorylation pathways. This simple pathway illustrates many of the fundamental principles and unanswered questions in the field of signaling biology. A molecular description of pathway function has progressed rapidly because it is accessible to diverse structural, biochemical, and genetic approaches. As a result, structures are emerging for most of the pathway elements, biochemical studies are elucidating the mechanisms of key signaling events, and genetic methods are revealing the intermolecular interactions that transmit information between components. Recent advances include (a) the first molecular picture of a conformational transmembrane signal in a cell surface receptor, (b) four new structures of kinase domains and adaptation enzymes, and (c) significant new insights into the mechanisms of receptor-mediated kinase regulation, receptor adaptation, and the phospho-activation of signaling proteins. Overall, the chemosensory pathway and the propulsion system it regulates provide an ideal system in which to probe molecular principles underlying complex cellular signaling and behavior.
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    Annual Review of Cell and Developmental Biology 13 (1997), S. 611-667 
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    Notes: Abstract The organizer is formed in an equatorial sector of the blastula stage amphibian embryo by cells that have responded to two maternal agents: a general meso-endoderm inducer (involving the TFG-beta signaling pathway) and a dorsal modifier (probably involving the Wnt signaling pathway). The meso-endoderm inducer is secreted by most vegetal cells, those containing maternal materials that had been localized in the vegetal hemisphere of the oocyte during oogenesis. As a consequence of the inducer's distribution and action, the competence domains of prospective ectoderm, mesoderm, and endoderm are established in an animal-to-vegetal order in the blastula. The dorsal modifier signal is secreted by a sector of cells of the animal and vegetal hemispheres on one side of the blastula. These cells contain maternal materials transported there in the first cell cycle from the vegetal pole of the egg along microtubules aligned by cortical rotation. The Nieuwkoop center is the region of blastula cells secreting both maternal signals, and hence specifying the organizer in an equatorial sector. Final steps of organizer formation at the late blastula or early gastrula stage may involve locally secreted zygotic signals as well. At the gastrula stage, the organizer secretes a variety of zygotic proteins that act as antagonists to various members of the BMP and Wnt families of ligands, which are secreted by cells of the competence domains surrounding the organizer. BMPs and Wnts favor ventral development, and cells near the organizer are protected from these agents by the organizer's inducers. The nearby cells are derepressed in their inherent capacity for dorsal development, which is apparent in the neural induction of the ectoderm, dorsalization of the mesoderm, and anteriorization of the endoderm. The organizer also engages in extensive specialized morphogenesis, which brings it within range of responsive cell groups. It also self-differentiates to a variety of axial tissues of the body.
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    Annual Review of Cell and Developmental Biology 14 (1998), S. 305-338 
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    Notes: Abstract The actin cytoskeleton is a highly dynamic network composed of actin polymers and a large variety of associated proteins. The main functions of the actin cytoskeleton are to mediate cell motility and cell shape changes during the cell cycle and in response to extracellular stimuli, to organize the cytoplasm, and to generate mechanical forces within the cell. The reshaping and functions of the actin cytoskeleton are regulated by signaling pathways. Here we broadly review the actin cytoskeleton and the signaling pathways that regulate it. We place heavy emphasis on the yeast actin cytoskeleton.
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    Annual Review of Cell and Developmental Biology 14 (1998), S. 265-303 
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    Notes: Abstract Proteins that control mitochondrial dynamics in yeast are being identified at a rapid pace. These proteins include cytoskeletal elements that regulate organelle distribution and inheritance and several outer membrane proteins that are required to maintain the branched, mitochondrial reticulum. Interestingly, three of the high molecular weight GTPases encoded by the yeast genome are required for mitochondrial integrity and are potential regulators of mitochondrial branching, distribution, and membrane fusion. The recent finding that mtDNA mixing is restricted in the mitochondrial matrix has stimulated the hunt for the molecular machinery that anchors mitochondrial nucleoids in the organelle. Considering that many aspects of mitochondrial structure and behavior are strikingly similar in different cell types, the functional analyses of these yeast proteins should provide general insights into the mechanisms governing mitochondrial dynamics in all eukaryotes.
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    Annual Review of Cell and Developmental Biology 14 (1998), S. 459-485 
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    Notes: Abstract Cells respond to an accumulation of unfolded proteins in the endoplasmic reticulum (ER) by increasing transcription of genes encoding ER resident proteins. The information is transmitted from the ER lumen to the nucleus by an intracellular signaling pathway called the unfolded protein response (UPR). Recent work has shown that this signaling pathway utilizes several novel mechanisms, including translational attenuation and a regulated mRNA splicing step. In this review we aim to integrate these recent advances with current knowledge about maintenance of ER composition and abundance.
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    Annual Review of Cell and Developmental Biology 15 (1999), S. 185-230 
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    Notes: Abstract Ubiquitous among eukaryotes, the ADF/cofilins are essential proteins responsible for the high turnover rates of actin filaments in vivo. In vertebrates, ADF and cofilin are products of different genes. Both bind to F-actin cooperatively and induce a twist in the actin filament that results in the loss of the phalloidin-binding site. This conformational change may be responsible for the enhancement of the off rate of subunits at the minus end of ADF/cofilin-decorated filaments and for the weak filament-severing activity. Binding of ADF/cofilin is competitive with tropomyosin. Other regulatory mechanisms in animal cells include binding of phosphoinositides, phosphorylation by LIM kinases on a single serine, and changes in pH. Although vertebrate ADF/cofilins contain a nuclear localization sequence, they are usually concentrated in regions containing dynamic actin pools, such as the leading edge of migrating cells and neuronal growth cones. ADF/cofilins are essential for cytokinesis, phagocytosis, fluid phase endocytosis, and other cellular processes dependent upon actin dynamics.
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    Annual Review of Cell and Developmental Biology 15 (1999), S. 393-410 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Endoderm, one of the three principal germ layers, contributes to all organs of the alimentary tract. For simplicity, this review divides formation of endodermal organs into four fundamental steps: (a) formation of endoderm during gastrulation, (b) morphogenesis of a gut tube from a sheet of cells, (c) budding of organ domains from the tube, and (d) differentiation of organ-specific cell types within the growing buds. We discuss possible mechanisms that regulate how undifferentiated endoderm becomes specified into a myriad of cell types that populate the respiratory and gastrointestinal tracts.
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    Annual Review of Cell and Developmental Biology 15 (1999), S. 291-339 
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    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
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    Notes: Abstract Information can be transferred between the nucleus and the cytoplasm by translocating macromolecules across the nuclear envelope. Communication of extracellular or intracellular changes to the nucleus frequently leads to a transcriptional response that allows cells to survive in a continuously changing environment. Eukaryotic cells have evolved ways to regulate this movement of macromolecules between the cytoplasm and the nucleus such that the transfer of information occurs only under conditions in which a transcriptional response is required. This review focuses on the ways in which cells regulate movement of proteins across the nuclear envelope and the significance of this regulation for controlling diverse biological processes.
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    Annual Review of Cell and Developmental Biology 15 (1999), S. 469-517 
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    Notes: Abstract In Dictyostelium amoebae, cell-type differentiation, spatial patterning, and morphogenesis are controlled by a combination of cell-autonomous mechanisms and intercellular signaling. A chemotactic aggregation of ~105 cells leads to the formation of a multicellular organism. Cell-type differentiation and cell sorting result in a small number of defined cell types organized along an anteroposterior axis. Finally, a mature fruiting body is created by the terminal differentiation of stalk and spore cells. Analysis of the regulatory program demonstrates a role for several molecules, including GSK-3, signal transducers and activators of transcription (STAT) factors, and cAMP-dependent protein kinase (PKA), that control spatial patterning in metazoans. Unexpectedly, two component systems containing histidine kinases and response regulators also play essential roles in controlling Dictyostelium development. This review focuses on the role of cAMP, which functions intracellularly to mediate the activity of PKA, an essential component in aggregation, cell-type specification, and terminal differentiation. Cytoplasmic cAMP levels are controlled through both the regulated activation of adenylyl cyclases and the degradation by a phosphodiesterase containing a two-component system response regulator. Extracellular cAMP regulates G-protein-dependent and -independent pathways to control aggregation as well as the activity of GSK-3 and the transcription factors GBF and STATa during multicellular development. The integration of these pathways with others regulated by the morphogen DIF-1 to control cell fate decisions are discussed.
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    Annual Review of Cell and Developmental Biology 15 (1999), S. 799-842 
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    Notes: Abstract Cotranslational protein translocation across and integration into the membrane of the endoplasmic reticulum (ER) occur at sites termed translocons. Translocons are composed of several ER membrane proteins that associate to form an aqueous pore through which secretory proteins and lumenal domains of membrane proteins pass from the cytoplasm to the ER lumen. These sites are not passive holes in the bilayer, but instead are quite dynamic both structurally and functionally. Translocons cycle between ribosome-bound and ribosome-free states, and convert between translocation and integration modes of operation. These changes in functional state are accompanied by structural rearrangements that alter translocon conformation, composition, and interactions with ligands such as the ribosome and BiP. Recent studies have revealed that the translocon is a complex and sophisticated molecular machine that regulates the movement of polypeptides through the bilayer, apparently in both directions as well as laterally into the bilayer, all while maintaining the membrane permeability barrier.
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    Annual Review of Cell and Developmental Biology 15 (1999), S. 733-798 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Synaptic vesicles, which have been a paradigm for the fusion of a vesicle with its target membrane, also serve as a model for understanding the formation of a vesicle from its donor membrane. Synaptic vesicles, which are formed and recycled at the periphery of the neuron, contain a highly restricted set of neuronal proteins. Insight into the trafficking of synaptic vesicle proteins has come from studying not only neurons but also neuroendocrine cells, which form synaptic-like microvesicles (SLMVs). Formation and recycling of synaptic vesicles/SLMVs takes place from the early endosome and the plasma membrane. The cytoplasmic machinery of synaptic vesicle/SLMV formation and recycling has been studied by a variety of experimental approaches, in particular using cell-free systems. This has revealed distinct machineries for membrane budding and fission. Budding is mediated by clathrin and clathrin adaptors, whereas fission is mediated by dynamin and its interacting protein SH3p4, a lysophosphatidic acid acyl transferase.
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    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 17 (2001), S. 53-86 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract The bacterial pathogen Salmonella enterica has evolved a very sophisticated functional interface with its vertebrate hosts. At the center of this interface is a specialized organelle, the type III secretion system, that directs the translocation of bacterial proteins into the host cell. Salmonella spp. encode two such systems that deliver a remarkable array of bacterial proteins capable of modulating a variety of cellular functions, including actin cytoskeleton dynamics, nuclear responses, and endocytic trafficking. Many of these bacterial proteins operate by faithful mimicry of host proteins, in some cases representing the result of extensive molecular tinkering and convergent evolution. The coordinated action of these type III secreted proteins secures the replication and survival of the bacteria avoiding overt damage to the host. The study of this remarkable pathogen is not only illuminating general paradigms in microbial pathogenesis but is also providing valuable insight into host cell functions.
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    Annual Review of Cell and Developmental Biology 17 (2001), S. 87-132 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Vertebrate limb buds are embryonic structures for which much molecular and cellular data are known regarding the mechanisms that control pattern formation during development. Specialized regions of the developing limb bud, such as the zone of polarizing activity (ZPA), the apical ectodermal ridge (AER), and the non-ridge ectoderm, direct and coordinate the development of the limb bud along the anterior-posterior (AP), dorsal-ventral (DV), and proximal-distal (PD) axes, giving rise to a stereotyped pattern of elements well conserved among tetrapods. In recent years, specific gene functions have been shown to mediate the organizing and patterning activities of the ZPA, the AER, and the non-ridge ectoderm. The analysis of these gene functions has revealed the existence of complex interactions between signaling pathways operated by secreted factors of the HH, TGF-beta/BMP, WNT, and FGF superfamilies, which interact with many other genetic networks to control limb positioning, outgrowth, and patterning. The study of limb development has helped to establish paradigms for the analysis of pattern formation in many other embryonic structures and organs.
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    Annual Review of Cell and Developmental Biology 17 (2001), S. 133-157 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Cells in the immune and nervous systems communicate through informational synapses. The two-dimensional chemistry underlying the process of synapse formation is beginning to be explored using fluorescence imaging and mechanical techniques. Early analysis of two-dimensional kinetic rates (kon and koff) and equilibrium constants (Kd) provides a number of biological insights. First, there are two regimes for adhesion-one disordered with slow kon and the other self-ordered with 104-fold faster kon. Despite huge variation in two-dimensional kon, the two-dimensional koff is like koff in solution, and two-dimensional koff is more closely related to intrinsic properties of the interaction than the two-dimensional kon. Thus difference in koff can be used to set signaling thresholds. Early signaling complexes are compartmentalized to generate synergistic signaling domains. Immune antigen receptor components have a role in neural synapse editing. This suggests significant parallels in informational synapse formation based on common two-dimensional chemistry and signaling strategies.
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    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 17 (2001), S. 159-187 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Pollen tubes and root hairs are highly elongated, cylindrically shaped cells whose polarized growth permits them to explore the environment for the benefit of the entire plant. Root hairs create an enormous surface area for the uptake of water and nutrients, whereas pollen tubes deliver the sperm cells to the ovule for fertilization. These cells grow exclusively at the apex and at prodigious rates (in excess of 200 nm/s for pollen tubes). Underlying this rapid growth are polarized ion gradients and fluxes, turnover of cytoskeletal elements (actin microfilaments), and exocytosis and endocytosis of membrane vesicles. Intracellular gradients of calcium and protons are spatially localized at the growing apex; inward fluxes of these ions are apically directed. These gradients and fluxes oscillate with the same frequency as the oscillations in growth rate but not with the same phase. Actin microfilaments, which together with myosin generate reverse fountain streaming, undergo rapid turnover in the apical domain, possibly being regulated by key actin-binding proteins, e.g., profilin, villin, and ADF/cofilin, in concert with the ion gradients. Exocytosis of vesicles at the apex, also dependent on the ion gradients, provides precursor material for the continuously expanding cell wall of the growing cell. Elucidation of the interactions and of the dynamics of these different components is providing unique insight into the mechanisms of polarized growth.
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    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 17 (2001), S. 189-214 
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Developing organisms may contain billions of cells destined to differentiate in numerous different ways. One strategy organisms use to simplify the orchestration of development is the separation of cell populations into distinct functional units. Our expanding knowledge of boundary formation and function in different systems is beginning to reveal general principles of this process. Fields of cells are subdivided by the interpretation of morphogen gradients, and these subdivisions are then maintained and refined by local cell-cell interactions. Sharp and stable separation between cell populations requires special mechanisms to keep cells segregated, which in many cases appear to involve the regulation of cell affinity. Once cell populations become distinct, specialized cells are often induced along the borders between them. These boundary cells can then influence the patterning of surrounding cells, which can result in progressively finer subdivisions of a tissue. Much has been learned about the signaling pathways that establish boundaries, but a key challenge for the future remains to elucidate the cellular and molecular mechanisms that actually keep cell populations separated.
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