Most of my citations are printed correctly (as I wished) in the pdf Version. But for 2 out of 60 citations, the initials of the first author are also printed. So, intead of Sun et al. 2000, I get Y. Sun et al.. I checked my .bib-file and the author line of the affected citations follow the same logic (last name, first name and last name, first name, etc.) as the other "correct" citations. This is an excerpt from my document:
\documentclass[11pt,a4paper,twoside]{article}
\usepackage[ngerman,english]{babel}
\usepackage[babel, german=quotes]{csquotes}
\selectlanguage{english}
\usepackage[backend=biber,sorting=nyt, style=authoryear]{biblatex}
\addbibresource{References.bib}
\addbibresource{ReferencesExtra.bib}
\ExecuteBibliographyOptions{maxbibnames=99, maxcitenames=2, firstinits=true, date=year}
\ExecuteBibliographyOptions{isbn=false, url=false, eprint=false}
\DefineBibliographyStrings{english}{in={}} %change "In: <magazine>" to "<magazine>"
\begin{document}
....\cite{...}
\printbibliography[heading=none]
\end{document}
Example for "correct" citation with only the last name in-text is (from my .bib-file):
@article{Takimoto2009,
abstract = {Optimizing the anticodon recognition between orthogonal tRNA and synthetase significantly increased the incorporation efficiencies of various unnatural amino acids in mammalian cells, and the enhanced incorporation enabled efficient photocrosslinking of interacting proteins in mammalian cells. {\textcopyright} The Royal Society of Chemistry 2009.},
author = {Takimoto, Jeffrey K. and Adams, Katrina L. and Xiang, Zheng and Wang, Lei},
doi = {10.1039/b904228h},
issn = {1742206X},
journal = {Molecular BioSystems},
number = {9},
pages = {931--934},
title = {{Improving orthogonal tRNA-synthetase recognition for efficient unnatural amino acid incorporation and application in mammalian cells}},
volume = {5},
year = {2009}
}
The ones that print the initial "incorrectly" in-text are:
@article{Sun2002,
abstract = {Ligand-gated ion channels transduce chemical signals into electrical impulses by opening a transmembrane pore in response to binding one or more neurotransmitter molecules. After activation, many ligand-gated ion channels enter a desensitized state in which the neurotransmitter remains bound but the ion channel is closed. Although receptor desensitization is crucial to the functioning of many ligand-gated ion channels in vivo, the molecular basis of this important process has until now defied analysis. Using the GluR2 AMPA-sensitive glutamate receptor, we show here that the ligand-binding cores form dimers and that stabilization of the intradimer interface by either mutations or allosteric modulators reduces desensitization. Perturbations that destabilize the interface enhance desensitization. Receptor activation involves conformational changes within each subunit that result in an increase in the separation of portions of the receptor that are linked to the ion channel. Our analysis defines the dimer interface in the resting and activated state, indicates how ligand binding is coupled to gating, and suggests modes of dimer dimer interaction in the assembled tetramer. Desensitization occurs through rearrangement of the dimer interface, which disengages the agonist-induced conformational change in the ligand-binding core from the ion channel gate.},
author = {Sun, Yu and Olson, Rich and Horning, Michelle and Armstrong, Neali and Mayer, Mark and Gouaux, Eric},
doi = {10.1038/417245a},
isbn = {0028-0836},
issn = {0028-0836},
journal = {Nature},
number = {6886},
pages = {245--253},
pmid = {12015593},
title = {{Mechanism of glutamate receptor desensitization}},
url = {http://www.nature.com/doifinder/10.1038/417245a},
volume = {417},
year = {2002}
}
@article{Chen2017,
abstract = {Nature has invented photoreceptor proteins that are involved in sensing and response to light in living organisms. Genetic code expansion (GCE) technology has provided new tools to transform light insensitive proteins into novel photoreceptor proteins. It is achieved by the site-specific incorporation of unnatural amino acids (Uaas) that carry light sensitive moieties serving as "pigments" that react to light via photo-decaging, cross-linking, or isomerization. Over the last two decades, various proteins including ion channels, GPCRs, transporters, and kinases have been successfully rendered light responsive owing to the functionalities of Uaas. Very recently, Cas9 protein has been engineered to enable light activation of genomic editing by CRISPR. Those novel proteins have not only led to discoveries of dynamic protein conformational changes with implications in diseases, but also facilitated the screening of ligand-protein and protein-protein interactions of pharmacological significance. This review covers the genetic editing principles for genetic code expansion and design concepts that guide the engineering of light-sensitive proteins. The applications have brought up a new concept of "optoproteomics" that, in contrast to "optogenetics," aims to combine optical methods and site-specific proteomics for investigating and intervening in biological functions.},
author = {Chen, Yuting and Lu, Linjie and Ye, Shixin},
issn = {1551-4056},
journal = {The Yale journal of biology and medicine},
keywords = {Genetic code expansion,ion channels,kinases interactions,optochemical genetics,optoproteomics,unnatural amino acids},
number = {4},
pages = {599--610},
pmid = {29259524},
title = {{Genetic Code Expansion and Optoproteomics.}},
url = {http://www.ncbi.nlm.nih.gov/pubmed/29259524{\%}0Ahttp://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=PMC5733852},
volume = {90},
year = {2017}
}
@article{Chen1999,
author = {Chen, Guo{-Qiang} and Cui, C and Mayer, Mark L and Gouaux, Eric},
number = {December},
title = {{Functional characterization of a potassium-selective prokaryotic glutamate receptor}},
volume = {402},
year = {1999}
}
Do you have an idea, what the problem might be? Thanks
