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1
Control of Crystal Size and Lattice Formation by Starmaker in Otolith Biomineralization
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Control of Crystal Size and Lattice Formation by Starmaker in Otolith Biomineralization

Söllner, Christian ; Burghammer, Manfred ; Busch-Nentwich, Elisabeth ; Berger, Jürgen ; Schwarz, Heinz ; Riekel, Christian ; Nicolson, Teresa

Science (American Association for the Advancement of Science), 2003-10, Vol.302 (5643), p.282-286 [Periódico revisado por pares]

Washington, DC: American Association for the Advancement of Science

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2
INTERMEDIATE FILAMENTS: Molecular Structure, Assembly Mechanism, and Integration Into Functionally Distinct Intracellular Scaffolds
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INTERMEDIATE FILAMENTS: Molecular Structure, Assembly Mechanism, and Integration Into Functionally Distinct Intracellular Scaffolds

Herrmann, Harald ; Aebi, Ueli

Annual review of biochemistry, 2004-01, Vol.73 (1), p.749-789 [Periódico revisado por pares]

Palo Alto, CA 94303-0139: Annual Reviews

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3
Chondroitin Sulfate Proteoglycans: Structure-Function Relationship with Implication in Neural Development and Brain Disorders
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Chondroitin Sulfate Proteoglycans: Structure-Function Relationship with Implication in Neural Development and Brain Disorders

Avram, Speranta ; Shaposhnikov, Sergey ; Buiu, Catalin ; Mernea, Maria Chan, Sun-On

BioMed research international, 2014-01, Vol.2014, p.642798-11 [Periódico revisado por pares]

United States: Hindawi Publishing Corporation

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4
Ligand binding and conformational motions in myoglobin
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Ligand binding and conformational motions in myoglobin

Nienhaus, G. Ulrich ; Ostermann, Andreas ; Waschipky, Robert ; Parak, Fritz G

Nature (London), 2000-03, Vol.404 (6774), p.205-208 [Periódico revisado por pares]

London: Nature Publishing

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5
The structures of HsIU and the ATP-dependent protease HsIU-HsIV
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The structures of HsIU and the ATP-dependent protease HsIU-HsIV

BOCHTIER, M ; HARTMANN, C ; HYUN KYU SONG ; BOURENKOV, G. P ; BARTUNIK, H. D ; HUBER, R

Nature (London), 2000-02, Vol.403 (6771), p.800-805 [Periódico revisado por pares]

London: Nature Publishing

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6
Crystal Structure of a Central Stalk Subunit C and Reversible Association/Dissociation of Vacuole-Type ATPase
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Crystal Structure of a Central Stalk Subunit C and Reversible Association/Dissociation of Vacuole-Type ATPase

Iwata, Momi ; Imamura, Hiromi ; Stambouli, Elizabeth ; Ikeda, Chiyo ; Tamakoshi, Masatada ; Nagata, Koji ; Makyio, Hisayoshi ; Hankamer, Ben ; Barber, Jim ; Yoshida, Masasuke ; Yokoyama, Ken ; Iwata, So

Proceedings of the National Academy of Sciences - PNAS, 2004-01, Vol.101 (1), p.59-64 [Periódico revisado por pares]

United States: National Academy of Sciences

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7
Crystal Structure of the Ectodomain of Human Transferrin Receptor
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Crystal Structure of the Ectodomain of Human Transferrin Receptor

Lawrence, C. Martin ; Ray, Sanjoy ; Babyonyshev, Marina ; Galluser, Renate ; Borhani, David W. ; Harrison, Stephen C.

Science (American Association for the Advancement of Science), 1999-10, Vol.286 (5440), p.779-782 [Periódico revisado por pares]

Washington, DC: American Society for the Advancement of Science

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8
c-Abl tyrosine kinase and inhibition by the cancer drug imatinib (Gleevec/STI-571)
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c-Abl tyrosine kinase and inhibition by the cancer drug imatinib (Gleevec/STI-571)

NAGAR, Bhushan

The Journal of nutrition, 2007-06, Vol.137 (6S), p.1518S-1523S [Periódico revisado por pares]

Bethesda, MD: American Society for Nutritional Sciences

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9
Aspartic acid nucleates the apatite crystallites of bone: a hypothesis
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Aspartic acid nucleates the apatite crystallites of bone: a hypothesis

Sarig, Sara

Bone (New York, N.Y.), 2004-07, Vol.35 (1), p.108-113 [Periódico revisado por pares]

New York, NY: Elsevier Inc

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10
Structure of the intact transactivation domain of the human papillomavirus E2 protein
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Structure of the intact transactivation domain of the human papillomavirus E2 protein

Wilson, Keith S ; Antson, Alfred A ; Burns, Julie E ; Moroz, Olga V ; Scott, David J ; Sanders, Cyril M ; Bronstein, Igor B ; Dodson, G. Guy ; Maitland, Norman J

Nature (London), 2000-02, Vol.403 (6771), p.805-809 [Periódico revisado por pares]

London: Nature Publishing

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