On Reflexive Binding in North Sami

Principle A of the Binding Theory states that an anaphor must be A-bound in the local domain containing it, its governor and an accessible subject. However, if the anaphor is contained in an infinitival complement clause, it may, in North Sami, be bound either by the clause-mate subject or by the subject of the tensed clause. Thus, it appears that there is a larger binding domain for anaphors in addition to that determined by the condition A of standard binding theory. This domain can in some languages, as in North Sami, be defined by the notion of Tense whereas in other languages this need not be case, as in English. This supports the approach that the characterization of binding domains is parameterized and that languages pick different values of the parameter.

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Structural Characterization of the Erythrocyte Binding Domain of the Reticulocyte Binding Protein Homologue Family of Plasmodium yoelii

Infection and Immunity ◽

10.1128/iai.01326-10 ◽

2011 ◽

Vol 79 (7) ◽

pp. 2880-2888 ◽

Cited By ~ 11

Author(s):

Ardina Grüber ◽

Karthigayan Gunalan ◽

Jeya Kumar Ramalingam ◽

Malathy S. S. Manimekalai ◽

Gerhard Grüber ◽

...

Keyword(s):

Binding Protein ◽

Intervention Strategy ◽

Plasmodium Yoelii ◽

Binding Domain ◽

Content Type ◽

Binding Domains ◽

X Ray Scattering ◽

Ligand Interactions ◽

Erythrocyte Binding

ABSTRACTInvasion of the host cell by the malaria parasite is a key step for parasite survival and the only stage of its life cycle where the parasite is extracellular, and it is therefore a target for an antimalaria intervention strategy. Multiple members of the reticulocyte binding protein homologues (RH) family are found in all plasmodia and have been shown to bind to host red blood cells directly. In the study described here, we delineated the erythrocyte binding domain (EBD) of one member of the RH family, termed Py235, fromPlasmodium yoelii. Moreover, we have obtained the low-resolution structure of the EBD using small-angle X-ray scattering. Comparison of the EDB structure to other characterizedPlasmodiumreceptor binding domains suggests that there may be an overall structural conservation. These findings may help in developing new approaches to target receptor ligand interactions mediated by parasite proteins.

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Characterization of the dead ringer gene identifies a novel, highly conserved family of sequence-specific DNA-binding proteins.

Molecular and Cellular Biology ◽

10.1128/mcb.16.3.792 ◽

1996 ◽

Vol 16 (3) ◽

pp. 792-799 ◽

Cited By ~ 96

Author(s):

S L Gregory ◽

R D Kortschak ◽

B Kalionis ◽

R Saint

Keyword(s):

Dna Binding ◽

Binding Proteins ◽

Dna Binding Proteins ◽

Binding Domain ◽

Dna Binding Domain ◽

Dna Binding Domains ◽

Binding Domains ◽

The Dead

We reported the identification of a new family of DNA-binding proteins from our characterization of the dead ringer (dri) gene of Drosophila melanogaster. We show that dri encodes a nuclear protein that contains a sequence-specific DNA-binding domain that bears no similarity to known DNA-binding domains. A number of proteins were found to contain sequences homologous to this domain. Other proteins containing the conserved motif include yeast SWI1, two human retinoblastoma binding proteins, and other mammalian regulatory proteins. A mouse B-cell-specific regulator exhibits 75% identity with DRI over the 137-amino-acid DNA-binding domains of these proteins, indicating a high degree of conservation of this domain. Gel retardation and optimal binding site screens revealed that the in vitro sequence specificity of DRI is strikingly similar to that of many homeodomain proteins, although the sequence and predicted secondary structure do not resemble a homeodomain. The early general expression of dri and the similarity of DRI and homeodomain in vitro DNA-binding specificity compound the problem of understanding the in vivo specificity of action of these proteins. Maternally derived dri product is found throughout the embryo until germ band extension, when dri is expressed in a developmentally regulated set of tissues, including salivary gland ducts, parts of the gut, and a subset of neural cells. The discovery of this new, conserved DNA-binding domain offers an explanation for the regulatory activity of several important members of this class and predicts significant regulatory roles for the others.

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Characterization of the Antibody Response to the Receptor Binding Domain of Botulinum Neurotoxin Serotypes A and E

Infection and Immunity ◽

10.1128/iai.73.10.6998-7005.2005 ◽

2005 ◽

Vol 73 (10) ◽

pp. 6998-7005 ◽

Cited By ~ 43

Author(s):

Michael R. Baldwin ◽

William H. Tepp ◽

Christina L. Pier ◽

Marite Bradshaw ◽

Mengfei Ho ◽

...

Keyword(s):

Receptor Binding ◽

Clostridium Botulinum ◽

Binding Domain ◽

Classical Type ◽

Enzyme Linked Immunosorbent Assay ◽

Receptor Binding Domain ◽

Binding Domains ◽

C Terminus ◽

Neutralizing Capacity

ABSTRACT Clostridium botulinum neurotoxins (BoNTs) are the most toxic proteins for humans. The current clostridial-derived vaccines against BoNT intoxication have limitations including production and accessibility. Conditions were established to express the soluble receptor binding domain (heavy-chain receptor [HCR]) of BoNT serotypes A and E in Escherichia coli. Sera isolated from mice and rabbits immunized with recombinant HCR/A1 (rHCR/A1) from the classical type A-Hall strain (ATCC 3502) (BoNT/A1) and rHCR/E from BoNT serotype E Beluga (BoNT/EB) neutralized the homologous serotype of BoNT but displayed differences in cross-recognition and cross-protection. Enzyme-linked immunosorbent assay and Western blotting showed that α-rHCR/A1 recognized epitopes within the C terminus of the HCR/A and HCR/E, while α-rHCR/E recognized epitopes within the N terminus or interface between the N and C termini of the HCR proteins. α-rHCR/EB sera possessed detectable neutralizing capacity for BoNT/A1, while α-rHCR/A1 did not neutralize BoNT/E. rHCR/A was an effective immunogen against BoNT/A1 and the Kyoto F infant strain (BoNT/A2), but not BoNT serotype E Alaska (BoNT/EA), while rHCR/EB neutralized BoNT/EA, and under hyperimmunization conditions protected against BoNT/A1 and BoNT/A2. The protection elicited by rHCR/A1 to BoNT/A1 and BoNT/A2 and by rHCR/EB to BoNT/EA indicate that immunization with receptor binding domains elicit protection within sub-serotypes of BoNT. The protection elicited by hyperimmunization with rHCR/E against BoNT/A suggests the presence of common neutralizing epitopes between the serotypes E and A. These results show that a receptor binding domain subunit vaccine protects against serotype variants of BoNTs.

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Faculty Opinions recommendation of Characterization of Arabidopsis thaliana methyl-CpG-binding domain (MBD) proteins.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1013829.191882 ◽

2003 ◽

Author(s):

Pat Heslop-Harrison

Keyword(s):

Arabidopsis Thaliana ◽

Binding Domain ◽

Mbd Proteins

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Molecular Characterization of Rotavirus Porcine OSU Carbohydrate- Binding Domain VP8*

Current Proteomics ◽

10.2174/1570164612666150226232936 ◽

2015 ◽

Vol 12 (1) ◽

pp. 69-72

Author(s):

Hao Li ◽

Wei Zhang ◽

Hong-hao Zhou ◽

Xiao-li Li

Keyword(s):

Molecular Characterization ◽

Binding Domain ◽

Carbohydrate Binding

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The Image of the Accountant in a German Context

Accounting and the Public Interest ◽

10.2308/api.2004.4.1.62 ◽

2004 ◽

Vol 4 (1) ◽

pp. 62-89 ◽

Cited By ~ 22

Author(s):

Andreas Hoffjan

Keyword(s):

Content Analysis ◽

Empirical Study ◽

Cost Reduction ◽

Maximum Degree ◽

Work Ethic ◽

Personal Characteristics ◽

Management Accountant ◽

The Subject ◽

Professional Context

This study introduces content analysis as a method of examining the accountant's role. The empirical study is based on 73 advertisements, which are directed primarily at employees who are affected by the management accountant's work. The findings of the study indicate that the subject of accountancy is used particularly in connection with promises of “cost reduction.” Consequently, the majority of advertisements use the accountant stereotype of “savings personified.” In a professional context, the work ethic of the management accountant is given particular emphasis in the advertisements. He/she identifies him/herself with his/her task to the maximum degree, is regarded as loyal to his/her company and, for the most part, is well organized in his/her work. However, the characterization of the management accountant as a well disciplined company-person conflicts with the negative portrayal of his/her professional qualities. In advertisements, the management accountant is portrayed as a rather inflexible, passive, and uncreative specialist who, as a result of these qualities, often demotivates others. The personal characteristics of the management accountant are shown in a negative light. This gives him/her the unappealing image of a humorless, envious, dissociated, and ascetic corporate-person.

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