Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
JD Johnson, M Fleshner - Journal of leukocyte biology, 2006 - academic.oup.com
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72.
JD Johnson, M Fleshner - Journal of Leukocyte Biology, 2005 - europepmc.org
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
[PDF][PDF] Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
JD Johnson, M Fleshner - Journal of Leukocyte Biology, 2006 - Citeseer
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
[引用][C] Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
JD Johnson, M Fleshner - Journal of Leukocyte Biology, 2005 - cir.nii.ac.jp
Releasing signals, secretory pathways, and immune function of endogenous extracellular
heat shock protein 72 | CiNii Research CiNii 国立情報学研究所 学術情報ナビゲータ[サイニィ] …
heat shock protein 72 | CiNii Research CiNii 国立情報学研究所 学術情報ナビゲータ[サイニィ] …
Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
JD Johnson, M Fleshner - Journal of Leukocyte Biology, 2006 - Wiley Online Library
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
JD Johnson, M Fleshner - Journal of leukocyte biology, 2006 - pubmed.ncbi.nlm.nih.gov
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
[PDF][PDF] Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
JD Johnson, M Fleshner - Journal of Leukocyte Biology, 2006 - Citeseer
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …