human
TASK: Your task is to answer biomedical questions using the given abstract. Only output yes, no, or maybe as answer.
INPUT: ['The glycoprotein (GP)Ib-IX complex is critical to hemostasis and thrombosis. Its proper assembly is closely correlated with its surface expression level and requires cooperative interactions among extracellular and transmembrane domains of Ibα, Ibβ and IX subunits. Two interfaces have been previously identified between the extracellular domains of Ibβ and IX.', 'To understand how extracellular domains interact in GPIb-IX.', 'The Ibβ extracellular domain (IbβE ) or the IX counterpart (IXE ) in GPIb-IX was replaced with a well-folded IbβE /IXE chimera called IbβEabc , and the effect of domain replacement on assembly and expression of the receptor complex in transiently transfected Chinese hamster ovary cells was analyzed.', 'Replacing IXE with IbβEabc in GPIb-IX retained interface 1 but not interface 2 between the extracellular domains. While this domain replacement preserved complex integrity, the expression levels of Ibβ and Ibα were significantly reduced. Additional domain replacement with IbβEabc or IbβE in GPIb-IX produced the complex at disparate expression levels that cannot be simply explained by two separate interfaces. In particular, when IbβE in GPIb-IX was replaced by IbβEabc , Ibα and IX were expressed at approximately 70% of the wild-type level. Their levels were not reduced when IXE was changed further to IbβE .'] Does analysis of inter-subunit contacts reveal the structural malleability of extracellular domains in platelet glycoprotein Ib-IX complex?
OUTPUT:

agent
yes
TASK: Your task is to answer biomedical questions using the given abstract. Only output yes, no, or maybe as answer.
INPUT: ['The glycoprotein (GP)Ib-IX complex is critical to hemostasis and thrombosis. Its proper assembly is closely correlated with its surface expression level and requires cooperative interactions among extracellular and transmembrane domains of Ibα, Ibβ and IX subunits. Two interfaces have been previously identified between the extracellular domains of Ibβ and IX.', 'To understand how extracellular domains interact in GPIb-IX.', 'The Ibβ extracellular domain (IbβE ) or the IX counterpart (IXE ) in GPIb-IX was replaced with a well-folded IbβE /IXE chimera called IbβEabc , and the effect of domain replacement on assembly and expression of the receptor complex in transiently transfected Chinese hamster ovary cells was analyzed.', 'Replacing IXE with IbβEabc in GPIb-IX retained interface 1 but not interface 2 between the extracellular domains. While this domain replacement preserved complex integrity, the expression levels of Ibβ and Ibα were significantly reduced. Additional domain replacement with IbβEabc or IbβE in GPIb-IX produced the complex at disparate expression levels that cannot be simply explained by two separate interfaces. In particular, when IbβE in GPIb-IX was replaced by IbβEabc , Ibα and IX were expressed at approximately 70% of the wild-type level. Their levels were not reduced when IXE was changed further to IbβE .'] Does analysis of inter-subunit contacts reveal the structural malleability of extracellular domains in platelet glycoprotein Ib-IX complex?
OUTPUT:
