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Refinado por: Nome da Publicação: European Journal of Biochemistry remover assunto: Binding Sites remover
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1
The membrane-bound hydrogenase from paracoccus denitrificans: purification and molecular characterization
The membrane-bound hydrogenase from paracoccus denitrificans: purification and molecular characterization
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The membrane-bound hydrogenase from paracoccus denitrificans: purification and molecular characterization

KNÜTTEL, K ; SCHNEIDER, K ; SCHLEGEL, H. G ; MÜLLER, A

European journal of biochemistry, 1989-01, Vol.179 (1), p.101-108 [Periódico revisado por pares]

Oxford: Blackwell

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2
The lumazine synthase/riboflavin synthase complex of Bacillus subtilis. X-ray structure analysis of hollow reconstituted beta-subunit capsids
The lumazine synthase/riboflavin synthase complex of Bacillus subtilis. X-ray structure analysis of hollow reconstituted beta-subunit capsids
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The lumazine synthase/riboflavin synthase complex of Bacillus subtilis. X-ray structure analysis of hollow reconstituted beta-subunit capsids

Ladenstein, R ; Ritsert, K ; Huber, R ; Richter, G ; Bacher, A

European journal of biochemistry, 1994-08, Vol.223 (3), p.1007-1017 [Periódico revisado por pares]

England

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3
Structural and functional comparison of 15S‐ and 15R‐specific cyclooxygenases from the coral Plexaura homomalla
Structural and functional comparison of 15S‐ and 15R‐specific cyclooxygenases from the coral Plexaura homomalla
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Structural and functional comparison of 15S‐ and 15R‐specific cyclooxygenases from the coral Plexaura homomalla

Valmsen, Karin ; Boeglin, William E. ; Järving, Ivar ; Schneider, Claus ; Varvas, Külliki ; Brash, Alan R. ; Samel, Nigulas

European journal of biochemistry, 2004-09, Vol.271 (17), p.3533-3538 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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4
Identification of catalytically important residues in the active site of Escherichia coli transaldolase
Identification of catalytically important residues in the active site of Escherichia coli transaldolase
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Identification of catalytically important residues in the active site of Escherichia coli transaldolase

Schörken, Ulrich ; Thorell, Stina ; Schürmann, Melanie ; Jia, Jia ; Sprenger, Georg A. ; Schneider, Gunter

European journal of biochemistry, 2001-04, Vol.268 (8), p.2408-2415 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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5
His103 in yeast transketolase is required for substrate recognition and catalysis
His103 in yeast transketolase is required for substrate recognition and catalysis
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His103 in yeast transketolase is required for substrate recognition and catalysis

Wikner, C ; Meshalkina, L ; Nilsson, U ; Backstrom, S ; Lindqvist, Y ; Schneider, G

European journal of biochemistry, 1995-11, Vol.233 (3), p.750-755 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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6
Identification of the β‐dystroglycan binding epitope within the C‐terminal region of α‐dystroglycan
Identification of the β‐dystroglycan binding epitope within the C‐terminal region of α‐dystroglycan
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Identification of the β‐dystroglycan binding epitope within the C‐terminal region of α‐dystroglycan

Sciandra, Francesca ; Schneider, Martina ; Giardina, Bruno ; Baumgartner, Stefan ; Petrucci, Tamara C. ; Brancaccio, Andrea

European journal of biochemistry, 2001-08, Vol.268 (16), p.4590-4597 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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7
Identification of peptides inhibiting enzyme I of the bacterial phosphotransferase system using combinatorial cellulose‐bound peptide libraries
Identification of peptides inhibiting enzyme I of the bacterial phosphotransferase system using combinatorial cellulose‐bound peptide libraries
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Identification of peptides inhibiting enzyme I of the bacterial phosphotransferase system using combinatorial cellulose‐bound peptide libraries

Mukhija, Seema ; Germeroth, Lothar ; Schneider‐Mergener, Jens ; Erni, Bernhard

European journal of biochemistry, 1998-06, Vol.254 (2), p.433-438 [Periódico revisado por pares]

Berlin & Heidelberg: Springer‐Verlag

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8
Crystal structure of thiamindiphosphate‐dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole‐3‐acetic acid
Crystal structure of thiamindiphosphate‐dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole‐3‐acetic acid
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Crystal structure of thiamindiphosphate‐dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole‐3‐acetic acid

Schütz, Anja ; Sandalova, Tatyana ; Ricagno, Stefano ; Hübner, Gerhard ; König, Stephan ; Schneider, Gunter

European journal of biochemistry, 2003-05, Vol.270 (10), p.2312-2321 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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9
Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate : implications for the reaction mechanism
Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate : implications for the reaction mechanism
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Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate : implications for the reaction mechanism

LINDQVIST, Y ; SCHNEIDER, G ; VIHKO, P

European journal of biochemistry, 1994-04, Vol.221 (1), p.139-142 [Periódico revisado por pares]

Oxford: Blackwell

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10
Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme
Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme
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Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme

Adolph, H W ; Maurer, P ; Schneider-Bernlöhr, H ; Sartorius, C ; Zeppezauer, M

European journal of biochemistry, 1991-11, Vol.201 (3), p.615-625 [Periódico revisado por pares]

England

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