Characterization of the receptors for axon guidance factor netrin-4 and identification of the binding domains

2007 ◽  
Vol 34 (2) ◽  
pp. 243-250 ◽  
Author(s):  
Shutong Qin ◽  
Lihong Yu ◽  
Yan Gao ◽  
Renping Zhou ◽  
Chenggang Zhang
Keyword(s):  
Axon Guidance ◽  
Binding Domains

Characterization of axon guidance cue sensitivity of human embryonic stem cell-derived dopaminergic neurons

2010 ◽  
Vol 45 (4) ◽  
pp. 324-334 ◽  
Author(s):  
Branden J. Cord ◽  
Jie Li ◽  
Melissa Works ◽  
Susan K. McConnell ◽  
Theo Palmer ◽  
...  
Keyword(s):  
Stem Cell ◽  
Embryonic Stem Cell ◽  
Axon Guidance ◽  
Dopaminergic Neurons ◽  
Human Embryonic Stem Cell ◽  
Embryonic Stem ◽  
Guidance Cue

scholarly journals On Reflexive Binding in North Sami

Nordlyd ◽  
10.7557/12.35 ◽  
2004 ◽  
Vol 31 (4) ◽  
Author(s):  
Hanna Outakoski
Keyword(s):  
Binding Domain ◽  
Local Domain ◽  
Binding Theory ◽  
Binding Domains ◽  
Complement Clause ◽  
The Subject

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.

Isolation and characterization of collagen-binding domains from human von Willebrand factor

2009 ◽  
Vol 24 (3) ◽  
pp. 150-154 ◽  
Author(s):  
N. E. Sharapova ◽  
A. P. Kotnova ◽  
Z. M. Galushkina ◽  
N. N. Poletaeva ◽  
N. V. Lavrova ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Collagen Binding ◽  
Binding Domains ◽  
Isolation And Characterization ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms

Science ◽  
2020 ◽  
Vol 370 (6519) ◽  
pp. 950-957 ◽  
Author(s):  
M. Alejandra Tortorici ◽  
Martina Beltramello ◽  
Florian A. Lempp ◽  
Dora Pinto ◽  
Ha V. Dang ◽  
...  
Keyword(s):  
Neutralizing Antibodies ◽  
Viral Escape ◽  
Angiotensin Converting Enzyme 2 ◽  
Effector Functions ◽  
Human Antibodies ◽  
Binding Domains ◽  
Isolation And Characterization ◽  
Cryo Electron Microscopy ◽  
Escape Mutants

Efficient therapeutic options are needed to control the spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that has caused more than 922,000 fatalities as of 13 September 2020. We report the isolation and characterization of two ultrapotent SARS-CoV-2 human neutralizing antibodies (S2E12 and S2M11) that protect hamsters against SARS-CoV-2 challenge. Cryo–electron microscopy structures show that S2E12 and S2M11 competitively block angiotensin-converting enzyme 2 (ACE2) attachment and that S2M11 also locks the spike in a closed conformation by recognition of a quaternary epitope spanning two adjacent receptor-binding domains. Antibody cocktails that include S2M11, S2E12, or the previously identified S309 antibody broadly neutralize a panel of circulating SARS-CoV-2 isolates and activate effector functions. Our results pave the way to implement antibody cocktails for prophylaxis or therapy, circumventing or limiting the emergence of viral escape mutants.

scholarly journals Characterization of quail Pax-6 (Pax-QNR) proteins expressed in the neuroretina.

1993 ◽  
Vol 13 (12) ◽  
pp. 7257-7266 ◽  
Author(s):  
C Carriere ◽  
S Plaza ◽  
P Martin ◽  
B Quatannens ◽  
M Bailly ◽  
...  
Keyword(s):  
Dna Binding ◽  
Autosomal Dominant ◽  
Paired Domain ◽  
Terminal Part ◽  
Dominant Mutation ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Carboxyl Terminal

After differential screening of a cDNA library constructed from quail neuroretina cells (QNR) infected with the v-myc-containing avian retrovirus MC29, we have isolated a cDNA clone, Pax-QNR, homologous to the murine Pax-6, which is mutated in the autosomal dominant mutation small eye of mice and in the disorder aniridia in humans. Here we report the characterization of the Pax-QNR proteins expressed in the avian neuroretina. From bacterially expressed Pax-QNR peptides, we obtained rabbit antisera directed against different domains of the protein: paired domain (serum 11), domain between the paired domain and homeodomain (serum 12), homeodomain (serum 13), and carboxyl-terminal part (serum 14). Sera 12, 13, and 14 were able to specifically recognize five proteins (48, 46, 43, 33, and 32 kDa) in the neuroretina. In contrast to proteins of 48, 46, and 43 kDa, proteins of 33 and 32 kDa were not recognized by the paired antiserum (serum 11). Paired-less and paired-containing proteins exhibited the same half-life (6 h) and were phosphorylated mostly on serine residues. Immunoprecipitations performed with subcellular fractions of neuroretinas showed that the paired-containing proteins were located in the nucleus, whereas the 33- and 32-kDa proteins were found essentially in the cytoplasmic compartment. However, immunofluorescence experiments performed after transient transfections showed that p46 and p33/32 were also located in vivo into the nucleus. Thus, the Pax-QNR/Pax-6 gene can produce proteins with two DNA-binding domains as well as proteins containing only the DNA-binding homeodomain.

Purification and characterization of recombinant ligand-binding domains from the ecdysone receptors of four pest insects

2007 ◽  
Vol 53 (2) ◽  
pp. 309-324 ◽  
Author(s):  
Lloyd D. Graham ◽  
Patricia A. Pilling ◽  
Ruth E. Eaton ◽  
Jeffrey J. Gorman ◽  
Carl Braybrook ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Purification And Characterization ◽  
Binding Domains ◽  
Pest Insects

scholarly journals Terminal short arm domains of basement membrane laminin are critical for its self-assembly.

1990 ◽  
Vol 110 (3) ◽  
pp. 825-832 ◽  
Author(s):  
J C Schittny ◽  
P D Yurchenco
Keyword(s):  
Self Assembly ◽  
Affinity Column ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Calcium Dependent ◽  
Domain Specific ◽  
Binding Domains ◽  
Individual Domain ◽  
The Individual

Laminin self-assembles into large polymers by a cooperative two-step calcium-dependent mechanism (Yurchenco, P. D., E. C. Tsilibary, A. S. Charonis, and H. Furthmayr. 1985. J. Biol. Chem. 260:7636-7644). The domain specificity of this process was investigated using defined proteolytically generated fragments corresponding to the NH2-terminal globule and adjacent stem of the short arm of the B1 chain (E4), a complex of the two short arms of the A and B2 chains attached to the proximal stem of a third short arm (E1'), a similar complex lacking the globular domains (P1'), and the distal half of the long arm attached to the adjacent portion of the large globule (E8). Polymerization, followed by an increase of turbidity at 360 nm in neutral isotonic TBS containing CaCl2 at 35 degrees C, was quantitatively inhibited in a concentration-dependent manner with laminin fragments E4 and E1' but not with fragments E8 and P1'. Affinity retardation chromatography was used for further characterization of the binding of laminin domains. The migration of fragment E4, but not of fragments E8 and P1', was retarded in a temperature- and calcium-dependent fashion on a laminin affinity column but not on a similar BSA column. These data are evidence that laminin fragments E4 and E1' possess essential terminal binding domains for the self-aggregation of laminin, while fragments E8 and P1' do not. Furthermore, the individual domain-specific interactions that contribute to assembly are calcium dependent and of low affinity.

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