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Refinado por: Base de dados/Biblioteca: MEDLINE Complete remover Nome da Publicação: The Journal Of Biological Chemistry remover
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1
Discovery of Intracellular Heme-binding Protein HrtR, Which Controls Heme Efflux by the Conserved HrtB-HrtA Transporter in Lactococcus lactis
Discovery of Intracellular Heme-binding Protein HrtR, Which Controls Heme Efflux by the Conserved HrtB-HrtA Transporter in Lactococcus lactis
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Discovery of Intracellular Heme-binding Protein HrtR, Which Controls Heme Efflux by the Conserved HrtB-HrtA Transporter in Lactococcus lactis

Lechardeur, Delphine ; Cesselin, Bénédicte ; Liebl, Ursula ; Vos, Marten H. ; Fernandez, Annabelle ; Brun, Célia ; Gruss, Alexandra ; Gaudu, Philippe

Cellular and molecular life sciences : CMLS, 2012-02, Vol.287 (7), p.4752-4758 [Periódico revisado por pares]

United States: Elsevier Inc

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2
Crystal structure of osmotin, a plant antifungal protein
Crystal structure of osmotin, a plant antifungal protein
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Crystal structure of osmotin, a plant antifungal protein

Min, Kyeongsik ; Ha, Sung Chul ; Hasegawa, Paul M. ; Bressan, Ray A. ; Yun, Dae-Jin ; Kim, Kyeong Kyu

Proteins, structure, function, and bioinformatics, 2004-01, Vol.54 (1), p.170-173 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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3
Protein crystal perfection and its application
Protein crystal perfection and its application
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Protein crystal perfection and its application

Helliwell, John R.

Acta crystallographica. Section D, Biological crystallography., 2005-06, Vol.61 (6), p.793-798 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers

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4
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1-143)
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1-143)
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Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1-143)

Huang, Mingdong ; Mazar, Andrew P. ; Parry, Graham ; Higazi, Abd Al-Roof ; Kuo, Alice ; Cines, Douglas B.

Acta crystallographica. Section D, Biological crystallography., 2005-06, Vol.61 (6), p.697-700 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers

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5
Insights into the DNA repair process by the formamidopyrimidine‐DNA glycosylase investigated by molecular dynamics
Insights into the DNA repair process by the formamidopyrimidine‐DNA glycosylase investigated by molecular dynamics
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Insights into the DNA repair process by the formamidopyrimidine‐DNA glycosylase investigated by molecular dynamics

Amara, Patricia ; Serre, Laurence ; Castaing, Bertrand ; Thomas, Aline

Protein science, 2004-08, Vol.13 (8), p.2009-2021 [Periódico revisado por pares]

Bristol: Cold Spring Harbor Laboratory Press

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6
A Novel NAD-binding Protein Revealed by the Crystal Structure of 2,3-Diketo-l-gulonate Reductase (YiaK)
A Novel NAD-binding Protein Revealed by the Crystal Structure of 2,3-Diketo-l-gulonate Reductase (YiaK)
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A Novel NAD-binding Protein Revealed by the Crystal Structure of 2,3-Diketo-l-gulonate Reductase (YiaK)

Forouhar, Farhad ; Lee, Insun ; Benach, Jordi ; Kulkarni, Kaushal ; Xiao, Rong ; Acton, Thomas B. ; Montelione, Gaetano T. ; Tong, Liang

The EMBO journal, 2004-03, Vol.279 (13), p.13148-13155 [Periódico revisado por pares]

United States: Elsevier Inc

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7
The Molecular Basis for Modulation of Human Vγ9Vδ2 T Cell Responses by CD277/Butyrophilin-3 (BTN3A)-specific Antibodies
The Molecular Basis for Modulation of Human Vγ9Vδ2 T Cell Responses by CD277/Butyrophilin-3 (BTN3A)-specific Antibodies
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The Molecular Basis for Modulation of Human Vγ9Vδ2 T Cell Responses by CD277/Butyrophilin-3 (BTN3A)-specific Antibodies

Palakodeti, Aparna ; Sandstrom, Andrew ; Sundaresan, Lakshmi ; Harly, Christelle ; Nedellec, Steven ; Olive, Daniel ; Scotet, Emmanuel ; Bonneville, Marc ; Adams, Erin J.

Nature immunology, 2012-09, Vol.287 (39), p.32780-32790 [Periódico revisado por pares]

United States: Elsevier Inc

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