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Refinado por: Base de dados/Biblioteca: Academic OneFile remover Nome da Publicação: Nature remover
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1
Conformations of immunoglobulin hypervariable regions
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Artigo
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Conformations of immunoglobulin hypervariable regions

Chothia, Cyrus ; Lesk, Arthur M ; Tramontano, Anna ; Levitt, Michael ; Smith-Gill, Sandra J ; Air, Gillian ; Sheriff, Steven ; Padlan, Eduardo A ; Davies, David ; Tulip, William R ; Colman, Peter M ; Spinelli, Silvia ; Alzari, Pedro M ; Poljak, Roberto J

Nature (London), 1989-12, Vol.342 (6252), p.877-883 [Periódico revisado por pares]

London: Nature Publishing

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2
Novel NADPH-binding domain revealed by the crystal structure of aldose reductase
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Artigo
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Novel NADPH-binding domain revealed by the crystal structure of aldose reductase

Rondeau, J.-M ; Tête-Favier, F ; Podjarny, A ; Reymann, J.-M ; Barth, P ; Biellmann, J.-F ; Moras, D

Nature (London), 1992-01, Vol.355 (6359), p.469-472 [Periódico revisado por pares]

LONDON: MACMILLAN MAGAZINES LTD

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3
Three-dimensional structure of a thermostable bacterial cellulase
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Artigo
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Three-dimensional structure of a thermostable bacterial cellulase

Juy, Michel ; Amrt, Adolfo G ; Alzari, Pedro M ; Poljak, Roberta J ; Claeyssens, Marc ; Béguin, Pierre ; Aubert, Jean-Paul

Nature (London), 1992-05, Vol.357 (6373), p.89-91 [Periódico revisado por pares]

London: Nature Publishing

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4
Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase
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Artigo
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Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase

CAVARELLI, J ; REES, B ; RUFF, M ; THIERRY, J.-C ; MORAS, D

Nature (London), 1993-03, Vol.362 (6416), p.181-184 [Periódico revisado por pares]

London: Nature Publishing

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5
Structure of influenza virus haemagglutinin complexed with a neutralizing antibody
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Artigo
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Structure of influenza virus haemagglutinin complexed with a neutralizing antibody

Bizebard, Thierry ; Gigant, Benoît ; Rigolet, Pascal ; Rasmussen, Bjarne ; Diat, Olivier ; Böseckei, Peter ; Wharton, Steve A ; Skehel, John J ; Knossow, Marcel

Nature (London), 1995-07, Vol.376 (6535), p.92-94 [Periódico revisado por pares]

England: Nature Publishing Group

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6
A tertiary interaction that links active-site domains to the 5′ splice site of a group II intron
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Artigo
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A tertiary interaction that links active-site domains to the 5′ splice site of a group II intron

Pyle, Anna Marie ; Boudvillain, Marc ; de Lencastre, Alexandre

Nature (London), 2000-07, Vol.406 (6793), p.315-318 [Periódico revisado por pares]

London: Nature Publishing

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7
Three-dimensional structure of the bacterial protein-translocation complex SecYEG
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Artigo
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Three-dimensional structure of the bacterial protein-translocation complex SecYEG

Breyton, Cécile ; Collinson, Ian ; Haase, Winfried ; Rapoport, Tom A ; Kühlbrandt, Werner

Nature (London), 2002-08, Vol.418 (6898), p.662-665 [Periódico revisado por pares]

London: Nature Publishing

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8
Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
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Artigo
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Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain

Knossow, Marcel ; Ravelli, Raimond B.G ; Gigant, Benoît ; Curmi, Patrick A ; Jourdain, Isabelle ; Lachkar, Sylvie ; Sobel, André

Nature, 2004-03, Vol.428 (6979), p.198-202 [Periódico revisado por pares]

London: Nature Publishing

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9
Structural basis for the regulation of tubulin by vinblastine
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Artigo
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Structural basis for the regulation of tubulin by vinblastine

Knossow, Marcel ; Gigant, Benoît ; Wang, Chunguang ; Ravelli, Raimond B. G ; Roussi, Fanny ; Steinmetz, Michel O ; Curmi, Patrick A ; Sobel, André

Nature, 2005-05, Vol.435 (7041), p.519-522 [Periódico revisado por pares]

London: Nature Publishing

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10
Correlation of structural elements and infectivity of the HET-s prion
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Artigo
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Correlation of structural elements and infectivity of the HET-s prion

Riek, Roland ; Saupe, Sven J ; Ritter, Christiane ; Maddelein, Marie-Lise ; Lührs, Thorsten ; Ernst, Matthias ; Siemer, Ansgar B ; Meier, Beat H

Nature, 2005-06, Vol.435 (7043), p.844-848 [Periódico revisado por pares]

London: Nature Publishing

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