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Refinado por: assunto: Models, Molecular remover
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1
Protein engineering and design
Protein engineering and design
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Protein engineering and design

Carey, Paul R

San Diego, Calif: Academic Press 1996

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2
Protein Engineering and Design
Protein Engineering and Design
Protein Engineering and Design
Material Type:
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Protein Engineering and Design

Paul R. Carey, Paul R Carey P. R Carey; Paul R Carey

Burlington Academic Press 1996

Acesso online. A biblioteca também possui exemplares impressos.

3
Structure–function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site
Structure–function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site
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Structure–function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site

Peters, Nick T. ; Morlot, Cécile ; Yang, Desirée C. ; Uehara, Tsuyoshi ; Vernet, Thierry ; Bernhardt, Thomas G.

Molecular microbiology, 2013-08, Vol.89 (4), p.690-701 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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4
Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod
Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod
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Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod

Masson, Soizic ; Kern, Thomas ; Le Gouëllec, Audrey ; Giustini, Cécile ; Simorre, Jean-Pierre ; Callow, Philip ; Vernet, Thierry ; Gabel, Frank ; Zapun, André

The Journal of biological chemistry, 2009-10, Vol.284 (40), p.27687-27700 [Periódico revisado por pares]

United States: Elsevier Inc

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5
Modification of the Electrostatic Environment is Tolerated in the Oxyanion Hole of the Cysteine Protease Papain
Modification of the Electrostatic Environment is Tolerated in the Oxyanion Hole of the Cysteine Protease Papain
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Modification of the Electrostatic Environment is Tolerated in the Oxyanion Hole of the Cysteine Protease Papain

Menard, Robert ; Plouffe, Celine ; Laflamme, Pierre ; Vernet, Thierry ; Tessier, Daniel C ; Thomas, David Y ; Storer, Andrew C

Biochemistry (Easton), 1995-01, Vol.34 (2), p.464-471 [Periódico revisado por pares]

United States: American Chemical Society

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6
Polymorphism in the lipase genes of Geotrichum candidum strains
Polymorphism in the lipase genes of Geotrichum candidum strains
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Polymorphism in the lipase genes of Geotrichum candidum strains

BERTOLINI, Maria Célia ; LARAMÉE, Louise ; THOMAS, David Y. ; CYGLER, Miroslaw ; SCHRAG, Joseph D. ; VERNET, Thierry

European journal of biochemistry, 1994-01, Vol.219 (1‐2), p.119-125 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

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7
The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation
The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation
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The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation

Thomas, David Y ; Taylor, Sean C ; Ferguson, Andrew D ; Bergeron, John J M

Nature structural & molecular biology, 2004-02, Vol.11 (2), p.128-134 [Periódico revisado por pares]

United States: Nature Publishing Group

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8
Loss of specificity variants of WzxC suggest that substrate recognition is coupled with transporter opening in MOP‐family flippases
Loss of specificity variants of WzxC suggest that substrate recognition is coupled with transporter opening in MOP‐family flippases
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Loss of specificity variants of WzxC suggest that substrate recognition is coupled with transporter opening in MOP‐family flippases

Sham, Lok‐To ; Zheng, Sanduo ; Yakhnina, Anastasiya A ; Kruse, Andrew C ; Bernhardt, Thomas G

Molecular microbiology, 2018-09, Vol.109 (5), p.633-641 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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9
A PBP2x from a Clinical Isolate of Streptococcus pneumoniae Exhibits an Alternative Mechanism for Reduction of Susceptibility to β-Lactam Antibiotics
A PBP2x from a Clinical Isolate of Streptococcus pneumoniae Exhibits an Alternative Mechanism for Reduction of Susceptibility to β-Lactam Antibiotics
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A PBP2x from a Clinical Isolate of Streptococcus pneumoniae Exhibits an Alternative Mechanism for Reduction of Susceptibility to β-Lactam Antibiotics

Pernot, Lucile ; Chesnel, Laurent ; Le Gouellec, Audrey ; Croizé, Jacques ; Vernet, Thierry ; Dideberg, Otto ; Dessen, Andréa

The Journal of biological chemistry, 2004-04, Vol.279 (16), p.16463-16470 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Crystal Structure and Pathophysiological Role of the Pneumococcal Nucleoside-binding Protein PnrA
Crystal Structure and Pathophysiological Role of the Pneumococcal Nucleoside-binding Protein PnrA
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Crystal Structure and Pathophysiological Role of the Pneumococcal Nucleoside-binding Protein PnrA

Abdullah, Mohammed R. ; Batuecas, María T. ; Jennert, Franziska ; Voß, Franziska ; Westhoff, Philipp ; Kohler, Thomas P. ; Molina, Rafael ; Hirschmann, Stephanie ; Lalk, Michael ; Hermoso, Juan A. ; Hammerschmidt, Sven

Journal of molecular biology, 2021-01, Vol.433 (2), p.166723-166723, Article 166723 [Periódico revisado por pares]

England: Elsevier Ltd

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Deste Autor:

  1. Carey, P

Neste Assunto:

  1. Models, Molecular
  2. Models, Molecular
  3. Science & Technology
  4. Life Sciences & Biomedicine
  5. Biochemistry & Molecular Biology

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