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Molecular mechanism of signal sequence orientation in the endoplasmic reticulum
44/44 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
The 44 checked references that resolve
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The role of the N region in signal sequence and signal-anchor function.
resolves10.1126/science.287.5456.1232
Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition Particle
resolves10.1016/S0021-9258(17)35269-9
Charged residues are major determinants of the transmembrane orientation of a signal-anchor sequence.
resolves10.1016/0092-8674(92)90202-N
Pause transfer: A topogenic sequence in apolipoprotein B mediates stopping and restarting of translocation
resolves10.1083/jcb.123.4.799
GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor.
resolves10.1002/j.1460-2075.1995.tb00321.x
Transmembrane orientation of signal‐anchor proteins is affected by the folding state but not the size of the N‐terminal domain.
resolves10.1016/0092-8674(86)90786-5
Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
resolves10.1006/excr.1998.4042
The Role of the Hydrophobic Domain in Orienting Natural Signal Sequences within the ER Membrane
resolves10.1083/jcb.147.2.257
Glycosylation Can Influence Topogenesis of Membrane Proteins and Reveals Dynamic Reorientation of Nascent Polypeptides within the Translocon
resolves10.1093/emboj/19.24.6704
In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site‐specific phosphorylation
resolves10.1016/S0092-8674(00)81391-4
Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
resolves10.1074/jbc.273.38.24963
Transmembrane Protein Insertion Orientation in Yeast Depends on the Charge Difference across Transmembrane Segments, Their Total Hydrophobicity, and Its Distribution
resolves10.1038/367654a0
Evolutionary conservation of components of the protein translocation complex
resolves10.1083/jcb.121.4.743
Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion.
resolves10.1016/0092-8674(95)90313-5
A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
resolves10.1016/S0092-8674(00)81418-X
Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
resolves10.1002/j.1460-2075.1992.tb05199.x
The methionine‐rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences.
resolves10.1016/0092-8674(95)90330-5
The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
resolves10.1074/jbc.270.11.6170
The 70 Carboxyl-terminal Amino Acids of Nascent Secretory Proteins Are Protected from Proteolysis by the Ribosome and the Protein Translocation Apparatus of the Endoplasmic Reticulum Membrane
resolves10.1038/366351a0
GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
resolves10.1006/jmbi.2000.3947
A comparison of the yeast and rabbit 80 S ribosome reveals the topology of the nascent chain exit tunnel, inter-subunit bridges and mammalian rRNA expansion segments
resolves10.1083/jcb.142.2.355
Signal Sequence Recognition in Cotranslational Translocation by Protein Components of the Endoplasmic Reticulum Membrane
resolves10.1074/jbc.275.9.6207
Distant Downstream Sequence Determinants Can Control N-tail Translocation during Protein Insertion into the Endoplasmic Reticulum Membrane
resolves10.1016/0092-8674(91)90507-U
Topology of eukaryotic type II membrane proteins: Importance of N-terminal positively charged residues flanking the hydrophobic domain
resolves10.1016/S0021-9258(17)46740-8
Role of NH2-terminal positively charged residues in establishing membrane protein topology.
resolves10.1126/science.1072366
Distinct Modes of Signal Recognition Particle Interaction with the Ribosome
resolves10.1126/science.7660124
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
resolves10.1016/S0092-8674(00)80253-6
Empty Site Forms of the SRP54 and SRα GTPases Mediate Targeting of Ribosome–Nascent Chain Complexes to the Endoplasmic Reticulum
resolves10.1083/jcb.111.5.1793
The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain.
resolves10.1074/jbc.M000456200
The Topogenic Contribution of Uncharged Amino Acids on Signal Sequence Orientation in the Endoplasmic Reticulum
resolves10.1073/pnas.89.1.16
Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge.
resolves10.1073/pnas.85.20.7592
Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum.
resolves10.1016/S0092-8674(00)80669-8
Role of Sec61α in the Regulated Transfer of the Ribosome–Nascent Chain Complex from the Signal Recognition Particle to the Translocation Channel
resolves10.1016/0014-5793(95)00551-J
Heads or tails — what determines the orientation of proteins in the membrane
resolves10.1002/j.1460-2075.1986.tb04601.x
The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans‐membrane topology
resolves10.1083/jcb.137.3.555
Multiple Determinants Direct the Orientation of Signal–Anchor Proteins: The Topogenic Role of the Hydrophobic Signal Domain
resolves10.1146/annurev.cb.10.110194.000511
Signal Sequence Recognition and Protein Targeting to the Endoplasmic Reticulum Membrane
resolves10.1016/S0014-5793(99)01075-3
Oligomeric complexes involved in translocation of proteins across the membrane of the endoplasmic reticulum
resolves10.1016/S0091-679X(08)61686-6
Chapter 13 Analysis of Protein Topology in the Endoplasmic Reticulum
resolves10.1002/j.1460-2075.1990.tb07902.x
The methionine‐rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence.
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