Corrigendum to: β-Barrel Membrane Bacterial Proteins: Structure, Function, Assembly and Interaction with Lipids.

IF 1.9 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Current protein & peptide science Pub Date : 2023-01-01 DOI:10.2174/138920372410231115093314

Stefania Galdiero, Massimiliano Galdiero, Carlo Pedone

引用次数: 0

Abstract

The authors declare after the publication of the article entitled ‘β-Barrel Membrane Bacterial Proteins: Structure, Function, Assembly and Interaction with Lipids’’, published in Current Protein and Peptide Science, 2007, 8, 63-82 [1], that a reference by Koebnik was inadvertently omitted. The missing reference has now been included as: Original: [1] Rosenbusch, J.P. (1988) Zentralbl. Bakteriol., 17, 259-266. Corrected: [1] (a) Rosenbusch, J.P. (1988) Zentralbl. Bakteriol., 17, 259-266. (b) Koebnik, R.; Locher, K.P.; Gelder, P.V. Structure and function of bacterial outer membrane proteins: Barrels in a nutshell. Mol. Biol., 2000, 37(2), 239-53. The original article can be found online at: https://www.eurekaselect.com/article/22780

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β-桶膜细菌蛋白:结构，功能，组装和与脂质的相互作用的勘误。

作者在发表题为“β-桶膜细菌蛋白:结构、功能、组装和与脂质的相互作用”的文章后声明，发表在《Current Protein and Peptide Science》，2007,8,63-82[1]，无意中省略了Koebnik的参考文献。原:所有的供体和受体通过在相邻的-链之间形成氢键而在-螺旋状或-桶状的节段内饱和[1]。[1]陈志强，陈志强(1998)。微生物学报，17,259-266。更正:所有的供体和受体在α-螺旋的节段内或在β-桶的节段间通过在相邻β-链之间形成氢键而饱和[1a, 1b]。[1a]陈志强，陈志强(1998)。微生物学报，17,259-266。[11]李志强，李志强。打孔机,陷入;细菌外膜蛋白的结构和功能:桶壳。摩尔。杂志。中华医学杂志，2000,37(2)，239-53。原文可在https://www.eurekaselect.com/article/22780上找到。我们对这一错误表示遗憾，并向读者道歉。这里提供了错误的细节和更正。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Current protein & peptide science 生物-生化与分子生物学

CiteScore

5.20

自引率

0.00%

发文量

审稿时长

6 months

期刊介绍： Current Protein & Peptide Science publishes full-length/mini review articles on specific aspects involving proteins, peptides, and interactions between the enzymes, the binding interactions of hormones and their receptors; the properties of transcription factors and other molecules that regulate gene expression; the reactions leading to the immune response; the process of signal transduction; the structure and function of proteins involved in the cytoskeleton and molecular motors; the properties of membrane channels and transporters; and the generation and storage of metabolic energy. In addition, reviews of experimental studies of protein folding and design are given special emphasis. Manuscripts submitted to Current Protein and Peptide Science should cover a field by discussing research from the leading laboratories in a field and should pose questions for future studies. Original papers, research articles and letter articles/short communications are not considered for publication in Current Protein & Peptide Science.