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PonyProg - Serial device programmer
PonyProg - Serial device programmer

Critical roles of isoleucine-364 and adjacent residues in a hydrophobic  gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2 |  PNAS
Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2 | PNAS

Critical roles of isoleucine-364 and adjacent residues in a hydrophobic  gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2 |  PNAS
Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2 | PNAS

Single-component multilayered self-assembling protein nanoparticles  presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as  HIV-1 vaccine candidates | Nature Communications
Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as HIV-1 vaccine candidates | Nature Communications

Single-component multilayered self-assembling protein nanoparticles  presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as  HIV-1 vaccine candidates | bioRxiv
Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as HIV-1 vaccine candidates | bioRxiv

Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature  Communications
Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature Communications

Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature  Communications
Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature Communications

EEProm Hex Editor – EcuResources
EEProm Hex Editor – EcuResources

IJMS | Free Full-Text | P4 ATPases: Flippases in Health and Disease
IJMS | Free Full-Text | P4 ATPases: Flippases in Health and Disease

Transport mechanism of P4 ATPase phosphatidylcholine flippases | eLife
Transport mechanism of P4 ATPase phosphatidylcholine flippases | eLife

Biomedicines | Free Full-Text | Exploring the Phospholipid Transport  Mechanism of ATP8A1-CDC50
Biomedicines | Free Full-Text | Exploring the Phospholipid Transport Mechanism of ATP8A1-CDC50

Single-component multilayered self-assembling protein nanoparticles  presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as  HIV-1 vaccine candidates | Nature Communications
Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as HIV-1 vaccine candidates | Nature Communications

Cryo-EM reveals mechanistic insights into lipid-facilitated polyamine  export by human ATP13A2 - ScienceDirect
Cryo-EM reveals mechanistic insights into lipid-facilitated polyamine export by human ATP13A2 - ScienceDirect

Single-component, self-assembling, protein nanoparticles presenting the  receptor binding domain and stabilized spike as SARS-CoV-2 vaccine  candidates | Science Advances
Single-component, self-assembling, protein nanoparticles presenting the receptor binding domain and stabilized spike as SARS-CoV-2 vaccine candidates | Science Advances

Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature  Communications
Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature Communications

Single-component multilayered self-assembling protein nanoparticles  presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as  HIV-1 vaccine candidates | bioRxiv
Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as HIV-1 vaccine candidates | bioRxiv

Critical roles of isoleucine-364 and adjacent residues in a hydrophobic  gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2 |  PNAS
Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2 | PNAS

Single-component multilayered self-assembling protein nanoparticles  presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as  HIV-1 vaccine candidates | bioRxiv
Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as HIV-1 vaccine candidates | bioRxiv

Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature  Communications
Activation and substrate specificity of the human P4-ATPase ATP8B1 | Nature Communications

Crystal structure of a human plasma membrane phospholipid flippase -  Journal of Biological Chemistry
Crystal structure of a human plasma membrane phospholipid flippase - Journal of Biological Chemistry

Transmembrane Cu( i ) P-type ATPase pumps are electrogenic uniporters -  Dalton Transactions (RSC Publishing) DOI:10.1039/D0DT01380C
Transmembrane Cu( i ) P-type ATPase pumps are electrogenic uniporters - Dalton Transactions (RSC Publishing) DOI:10.1039/D0DT01380C

Frontiers | Multimerization of Ebola GPΔmucin on protein nanoparticle  vaccines has minimal effect on elicitation of neutralizing antibodies
Frontiers | Multimerization of Ebola GPΔmucin on protein nanoparticle vaccines has minimal effect on elicitation of neutralizing antibodies

IJMS | Free Full-Text | Endometrial Stem Cell Markers: Current Concepts and  Unresolved Questions
IJMS | Free Full-Text | Endometrial Stem Cell Markers: Current Concepts and Unresolved Questions

Viruses | Free Full-Text | Structural and Functional Properties of the  Hepatitis C Virus p7 Viroporin
Viruses | Free Full-Text | Structural and Functional Properties of the Hepatitis C Virus p7 Viroporin

Single-component multilayered self-assembling nanoparticles presenting  rationally designed glycoprotein trimers as Ebola virus vaccines | Nature  Communications
Single-component multilayered self-assembling nanoparticles presenting rationally designed glycoprotein trimers as Ebola virus vaccines | Nature Communications