A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)37064-3 ◽

1994 ◽

Vol 269 (12) ◽

pp. 8979-8985 ◽

Author(s):

J.M. Ghigo ◽

C. Wandersman

Keyword(s):

Erwinia Chrysanthemi ◽

Amino Acid Motif ◽

Secretion Pathway ◽

Carboxyl Terminal ◽

Protease Secretion

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Correlation of serum IgG antibodies to recombinant P0 fusion protein with IgG antibodies to carboxylterminal 22 synthetic peptides and carboxyl-terminal 22 amino acid-deleted recombinant P0 fusion protein in patients with systemic lupus erythematosus

Arthritis & Rheumatism ◽

10.1002/1529-0131(199707)40:7<1364::aid-art24>3.0.co;2-d ◽

1997 ◽

Vol 40 (7) ◽

pp. 1364-1365

Author(s):

Taku Yoshio ◽

Jun-Ichi Masuyama ◽

Seiji Minota ◽

Masahiro Iwamoto ◽

Akio Mimori ◽

...

Keyword(s):

Systemic Lupus Erythematosus ◽

Fusion Protein ◽

Lupus Erythematosus ◽

Synthetic Peptides ◽

Igg Antibodies ◽

Systemic Lupus ◽

Serum Igg ◽

Carboxyl Terminal

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Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)68344-9 ◽

1988 ◽

Vol 263 (18) ◽

pp. 8583-8591

Author(s):

S Tanaka ◽

E A Robinson ◽

E Appella ◽

M Miller ◽

H L Ammon ◽

...

Keyword(s):

Amino Acid Sequence ◽

Crystallographic Data ◽

Erwinia Chrysanthemi

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Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)48354-8 ◽

1992 ◽

Vol 267 (2) ◽

pp. 794-803 ◽

Author(s):

J Landry ◽

H Lambert ◽

M Zhou ◽

J N Lavoie ◽

E Hickey ◽

...

Keyword(s):

Amino Acid Motif ◽

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Alterations of the carboxyl-terminal amino acid residues of Escherichia coli lipoprotein affect the formation of murein-bound lipoprotein.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)41811-x ◽

1992 ◽

Vol 267 (27) ◽

pp. 19560-19564

Author(s):

W.Y. Zhang ◽

H.C. Wu

Keyword(s):

Escherichia Coli ◽

Amino Acid Residues ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Carboxyl Terminal

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The pathogenicity of T cell epitopes on human Goodpasture antigen and its critical amino acid motif

Journal of Cellular and Molecular Medicine ◽

10.1111/jcmm.13134 ◽

2017 ◽

Vol 21 (9) ◽

pp. 2117-2128 ◽

Author(s):

Shui-yi Hu ◽

Qiu-hua Gu ◽

Jia Wang ◽

Miao Wang ◽

Xiao-yu Jia ◽

...

Keyword(s):

T Cell ◽

T Cell Epitopes ◽

Amino Acid Motif ◽

Critical Amino Acid ◽

Goodpasture Antigen

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Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)45899-1 ◽

1992 ◽

Vol 267 (4) ◽

pp. 2443-2450 ◽

Author(s):

C B Peterson ◽

H K Schachman

Keyword(s):

Alpha Helix ◽

Aspartate Transcarbamoylase ◽

Amino Acid Substitutions ◽

Carboxyl Terminal ◽

Intersubunit Interactions ◽

Allosteric Properties

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Molecular cloning and expression of partial cDNAs and deduced amino acid sequence of a carboxyl-terminal fragment of human apolipoprotein B-100.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.82.21.7265 ◽

1985 ◽

Vol 82 (21) ◽

pp. 7265-7269 ◽

Author(s):

C. F. Wei ◽

S. H. Chen ◽

C. Y. Yang ◽

Y. L. Marcel ◽

R. W. Milne ◽

...

Keyword(s):

Amino Acid Sequence ◽

Molecular Cloning ◽

Apolipoprotein B ◽

Cloning And Expression ◽

Human Apolipoprotein ◽

Terminal Fragment ◽

Carboxyl Terminal

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Identification of an Essential Amino Acid Motif within the C Terminus of the Pituitary Adenylate Cyclase-activating Polypeptide Type I Receptor That Is Critical for Signal Transduction but Not for Receptor Internalization

Journal of Biological Chemistry ◽

10.1074/jbc.m004612200 ◽

2000 ◽

Vol 275 (46) ◽

pp. 36134-36142 ◽

Author(s):

Rong-Ming Lyu ◽

Patrizia M. Germano ◽

Joon Ki Choi ◽

Sang V. Le ◽

Joseph R. Pisegna

Keyword(s):

Signal Transduction ◽

Adenylate Cyclase ◽

Essential Amino Acid ◽

Receptor Internalization ◽

Type I ◽

Amino Acid Motif ◽

Pituitary Adenylate Cyclase

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Role of Tetra Amino Acid Motif Properties on the Function of Protease-Activatable Viral Vectors

ACS Biomaterials Science & Engineering ◽

10.1021/acsbiomaterials.6b00439 ◽

2016 ◽

Vol 2 (11) ◽

pp. 2026-2033 ◽

Author(s):

T. M. Robinson ◽

J. Judd ◽

M. L. Ho ◽

J. Suh

Keyword(s):

Viral Vectors ◽

Amino Acid Motif

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Common principles in the biosynthesis of diverse enzymes

Biochemical Society Transactions ◽

10.1042/bst0330105 ◽

2005 ◽

Vol 33 (1) ◽

pp. 105-107 ◽

Author(s):

R.L. Jack ◽

A. Dubini ◽

T. Palmer ◽

F. Sargent

Keyword(s):

Escherichia Coli ◽

Signal Peptides ◽

Amino Acid Motif ◽

Dmso Reductase ◽

Arginine Transport

A subset of bacterial periplasmic enzymes are transported from the cytoplasm by the twin-arginine transport apparatus. Such proteins contain distinctive N-terminal signal peptides containing a conserved SRRXFLK ‘twin-arginine’ amino acid motif and often bind complex cofactors before the transport event. It is important that assembly of complex cofactor-containing, and often multi-subunit, enzymes is complete before export. Studies of the unrelated [NiFe] hydrogenase, DMSO reductase and trimethylamine N-oxide reductase systems from Escherichia coli have enabled us to define a chaperone-mediated ‘proofreading’ mechanism involved in co-ordinating assembly and export of twin-arginine transport-dependent enzymes.

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