| 1996 |
LGN was identified as a novel protein that interacts with the alpha-subunit of the heterotrimeric GTP-binding protein Gαi2, confirmed by yeast two-hybrid screening and in vitro binding assay using recombinant proteins. LGN contains 10 Leu-Gly-Asn repeats, seven N-terminal repeats (~40 aa each) and four C-terminal repeats (~34 aa each). |
Yeast two-hybrid screen; in vitro binding assay with recombinant proteins |
Gene |
Medium |
8973305
|
| 2000 |
Drosophila Pins (ortholog of LGN/GPSM2) was identified as a binding partner of Inscuteable and a Gα subunit in vivo, localizing to the apical cortex of neuroblasts. In pins mutants, spindle orientation and basal localization of Numb/Miranda were defective, and Inscuteable lost its apical localization during mitosis, establishing Pins as essential for asymmetric cell division. |
In vivo co-immunoprecipitation; genetic loss-of-function (pins mutants); immunofluorescence localization |
Current biology : CB |
High |
10753746
|
| 2002 |
LGN binds with high affinity to the C-terminal tail of NuMA. A small domain within the C terminus of NuMA stabilizes microtubules in vitro, and LGN blocks this stabilization by steric exclusion, as the MT-binding domain on NuMA overlaps by ten amino acid residues with the LGN-binding domain. |
In vitro microtubule stabilization assay; frog egg extracts; in vitro binding assays; domain mapping |
Current biology : CB |
High |
12445386
|
| 2002 |
LGN localizes to the midbody structure separating daughter cells during the later stages of mitosis in PC12 and COS7 cells, moving from the nucleus to the midbody during cytokinesis. Its subcellular localization is differentially regulated by the cell cycle compared to the closely related AGS3. |
Immunocytochemistry; cell fractionation; expression of LGN-specific antisera |
The Journal of biological chemistry |
Medium |
11832491
|
| 2003 |
Mouse PINS (LGN/GPSM2 ortholog) can asymmetrically localize to the apical cortex of Drosophila neuroblasts when ectopically expressed, and can functionally substitute for Drosophila Pins in all aspects of neuroblast asymmetric cell division. The N-terminal TPR domain directly interacts with the asymmetric localization domain of Inscuteable, and the C-terminal GoLoco region directs cortical localization. |
Ectopic expression in Drosophila neuroblasts; direct binding assay; genetic rescue experiments |
Journal of cell science |
High |
12571286
|
| 2003 |
In C. elegans, GPR-1 and GPR-2 (homologs of mammalian AGS3/LGN and Drosophila Pins) control spindle position by acting as GDP dissociation inhibitors (GDI) for GOA-1 (Gαo). LIN-5 (NuMA homolog) binds GPR proteins and is required for their cortical association. GPR proteins are enriched at the posterior cortex in a PAR-dependent manner, generating asymmetric pulling forces on spindle poles. |
RNAi depletion; GDI fluorescence assay; Co-IP; genetic epistasis |
Current biology : CB |
High |
12814548
|
| 2003 |
LGN exhibits enriched cortical localization during mitosis in certain mammalian cell lines (WISH, PC12, NRK but not COS cells). The Gα-binding C-terminal portion of LGN is sufficient for cortical localization. Cortical localization depends on microfilaments, and overexpression of Gα subunits can redirect LGN to the cortex in COS cells. Interfering with LGN function disrupts cell cycle progression. |
Overexpression of LGN domain truncations; immunofluorescence; cytochalasin D treatment; dominant-negative experiments |
Molecular biology of the cell |
Medium |
12925752
|
| 2004 |
Mammalian LGN (GPSM2) acts as a conformational switch: in its closed (autoinhibited) state, the N-terminal (TPR) and C-terminal (GoLoco) domains interact intramolecularly. NuMA or Gαi can disrupt this autoinhibitory interaction, allowing LGN to simultaneously bind both proteins and recruit them to the cell cortex. During mitosis, LGN recruits NuMA to the cell cortex; cortical association of LGN requires Gα binding. Overexpression of Gαi or YFP-LGN causes metaphase spindle oscillation. |
FRET biosensor; Co-immunoprecipitation; live cell imaging; overexpression |
Cell |
High |
15537540
|
| 2005 |
GPSM2 GoLoco motifs 1-4 all function as guanine nucleotide dissociation inhibitors (GDIs) for Gαi1, Gαi2, and Gαi3, but display significantly lower GDI activity and binding affinity for Gαo. Surface plasmon resonance binding assays showed all four GoLoco motifs bind Gαi1 but not Gαs, establishing Gαi subunits as the primary in vivo targets. |
Surface plasmon resonance; fluorescence-based nucleotide binding (GDI) assay; recombinant GST-fusion proteins |
Biochimica et biophysica acta |
High |
15946753
|
| 2005 |
In Drosophila neuroblasts, astral microtubules, kinesin Khc-73, and Discs large (Dlg) induce cortical polarization of Pins/Gαi; Dlg/Khc-73 and Dlg/Pins co-immunoprecipitate, suggesting Dlg mediates the link between microtubules and Pins/Gαi cortical polarity. This microtubule/Khc-73/Dlg pathway acts in parallel to the Inscuteable/Par pathway. |
Co-immunoprecipitation; live imaging; genetic loss-of-function; immunofluorescence |
Cell |
High |
16377571
|
| 2005 |
Mammalian Ric-8A catalytically dissociates Gαi-GDP/LGN/NuMA complexes in vitro, releasing activated Gαi-GTP and concomitantly liberating NuMA from LGN. This establishes a mechanism whereby Ric-8A GEF activity for Gαi regulates the LGN-NuMA interaction during cell division. |
In vitro biochemical dissociation assay with purified proteins; fluorescence-based GTPase assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
16275912
|
| 2005 |
LGN is expressed in photoreceptor inner segments and co-localizes with transducin α (Gαt) following its light-dependent translocation. LGN and Gαt co-precipitate from retinal extracts, and the GPR domain of LGN potently inhibits receptor-mediated guanine nucleotide exchange and GTPase activity of transducin, identifying a role for LGN in modulating transducin function in photoreceptors. |
Immunostaining; serial tangential sectioning with immunoblot; co-precipitation; in vitro GDI/GTPase inhibition assay |
Molecular and cellular neurosciences |
Medium |
15737739
|
| 2005 |
LGN directly binds Lgl2 (mammalian homolog of Drosophila l(2)gl) with Kd ~56 nM via the C-terminal tail of Lgl2. Endogenous Lgl2 forms a complex with aPKC, Par-6, and LGN, enhanced during metaphase. Overexpression of Lgl2 C-terminal tail mislocalized NuMA and disorganized the mitotic spindle; knockdown of Lgl1/2 caused spindle disorganization and micronuclei formation, mediated through regulation of the LGN-NuMA complex. |
Co-immunoprecipitation; in vitro binding with Kd measurement; siRNA knockdown; immunofluorescence |
The Journal of biological chemistry |
High |
15632202
|
| 2006 |
Drosophila Pins (LGN ortholog) directly binds and co-immunoprecipitates with the NuMA-related Mushroom body defect (Mud) protein. Pins recruits Mud to the neuroblast apical cortex; in mud mutants, spindle alignment with cortical polarity is lost. This establishes a direct Pins-Mud interaction linking cortical polarity to spindle orientation. |
Direct binding assay; co-immunoprecipitation; genetic loss-of-function (mud mutants); immunofluorescence |
Nature cell biology |
High |
16648843 16648846
|
| 2006 |
LGN modulates GIRK channel activity in a Gαi/Go-dependent manner: LGN increases basal GIRK current but reduces receptor-activated GIRK currents. This effect is mediated through the N-terminal TPR domain of LGN, which likely releases sequestered endogenous LGN. In hippocampal neurons, LGN hyperpolarizes resting potential through increased basal GIRK activity; LGN RNAi reduces basal GIRK activity. |
Electrophysiology (patch-clamp); LGN domain overexpression; lentiviral RNAi in hippocampal neurons |
Neuron |
High |
16701207
|
| 2006 |
In Drosophila neuroblasts, Loco (a GoLoco protein) and Pins act synergistically as GDIs for Gαi to release free Gβγ, which is required for asymmetric spindle and daughter cell size. Simultaneous removal of Loco and Pins phenocopies Gβ13F or Gγ1 mutants. Loco's RGS domain also accelerates GTPase activity of Gαi, providing a second mode of regulation. |
Genetic epistasis (double mutants); in vitro GDI assay; RGS GTPase acceleration assay |
Genes & development |
High |
15937221
|
| 2007 |
Drosophila Pins (LGN ortholog) forms a 'closed' autoinhibited state via intramolecular GoLoco-TPR interactions. Gαi binding to GoLoco 1 (GL1) recruits Pins to the apical cortex without opening Pins or recruiting Mud. Gαi and Mud bind cooperatively to GL2/3 and TPR domains respectively, activating the full spindle orientation pathway. These multiple activity states link cortical polarity to spindle orientation. |
Biochemical binding assays; genetic epistasis; live imaging; domain mutant analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
17726110
|
| 2007 |
LGN (GPSM2) is required for planar divisions in chick neuroepithelium; it localizes at the cell cortex and spindle poles of neural progenitors. Interfering with LGN function randomizes the division plane, causing one daughter to exit the neuroepithelium prematurely and proliferate aberrantly, without affecting cell fate. This demonstrates LGN controls spindle movements/orientation in vertebrate neural progenitors. |
In ovo electroporation (dominant-negative LGN); immunofluorescence; BrdU lineage analysis |
Nature neuroscience |
High |
17934458
|
| 2007 |
Knockout of LGN (GPSM2) in mouse neuroepithelial cells randomizes the orientation of normally planar cell divisions, causing loss of the apical membrane from some daughter cells and converting them into abnormally localized progenitors, without affecting neuronal production rate. LGN is dispensable for the proliferation vs. differentiation decision but essential for maintaining neuroepithelial self-renewal via planar spindle orientation. |
LGN conditional knockout (gene targeting); BrdU/EdU labeling; immunofluorescence; clonal analysis |
Nature cell biology |
High |
18084280
|
| 2010 |
A nonsense mutation in GPSM2 (early truncation) causes nonsyndromic hearing loss DFNB82 in humans. In mouse inner ear, GPSM2 is localized to apical surfaces of hair cells and supporting cells, most highly expressed during embryonic development, establishing GPSM2 as essential for normal hearing development. |
Whole exome sequencing; homozygosity mapping; immunolocalization in mouse inner ear |
American journal of human genetics |
Medium |
20602914
|
| 2010 |
During epithelial mitosis, Par3/aPKC excludes LGN (Pins) from the apical cortex by aPKC-mediated phosphorylation of Pins on Ser401, which recruits 14-3-3 protein. 14-3-3 binding inhibits Pins association with Gαi, causing Pins to dissociate from the apical cortex. A Pins S401A mutant mislocalizes over the entire cortex and causes spindle misorientation and multi-lumen cysts. |
siRNA knockdown; phosphorylation site mutagenesis (S401A); 14-3-3 binding assay; 3D cyst culture; immunofluorescence |
Current biology : CB |
High |
20933426
|
| 2010 |
LGN localizes to the lateral cell cortex (excluded from apical cortex) of dividing MDCK cells. Depleting LGN, preventing cortical localization, or disrupting its interaction with NuMA or Gα proteins causes spindle misorientation and abnormal cystogenesis (multiple lumens). Apical exclusion of LGN is mediated by aPKC. Artificial mistargeting of LGN to the apical membrane rotates the spindle ~90° and disrupts cystogenesis. |
siRNA knockdown; dominant-negative constructs; apical membrane targeting of LGN; 3D cyst culture; immunofluorescence |
The Journal of cell biology |
High |
20385777
|
| 2010 |
Ric-8A and Gαi cooperate to recruit LGN (GPSM2), NuMA, and dynein to the cell cortex of mammalian cells during mitosis. Pertussis toxin (blocking Ric-8A-Gαi interaction), Ric-8A knockdown, or Gαi knockdown each impaired cortical localization of LGN, NuMA, and dynein, and disturbed integrin-dependent mitotic spindle orientation. Reduced Ric-8A prolonged mitosis and decreased spindle movements. |
siRNA knockdown; pertussis toxin treatment; immunofluorescence; live imaging (GFP-tubulin HeLa cells) |
Molecular and cellular biology |
High |
20479129
|
| 2010 |
GPSM2 (LGN) is phosphorylated on Thr450 by the serine/threonine kinase PBK/TOPK during mitosis. LGN/GPSM2 localizes to the spindle at metaphase and to the midzone/midbody in cytokinesis. Overexpression of the T450A phospho-dead mutant induces aberrant chromosomal segregation and growth suppression of breast cancer cells; siRNA knockdown of GPSM2 causes incomplete cell division. |
Western blot (phospho-specific); siRNA knockdown; T450A mutant overexpression; immunocytochemistry; synchronization assays |
Genes, chromosomes & cancer |
Medium |
20589935
|
| 2011 |
Crystal structures of LGN in complex with NuMA and mInsc (mammalian Inscuteable) reveal that NuMA and mInsc interact with LGN TPR domain through distinct but overlapping interfaces. Structural and biochemical studies demonstrate that NuMA and mInsc binding to LGN are mutually exclusive, with mInsc binding preferentially (higher affinity). This suggests Par3/mInsc/LGN and NuMA/LGN/Gαi complexes play sequential and partially overlapping roles. |
X-ray crystallography; isothermal titration calorimetry; competitive binding assays; cell biology (localization studies) |
Molecular cell |
High |
21816348
|
| 2011 |
Crystal structure of Drosophila Pins (LGN ortholog) TPR domain in complex with Inscuteable reveals modular binding interface with three contact modules on Insc running antiparallel to the TPR superhelix. Structure-based mutagenesis defines critical residues. mInsc binds LGN with highest affinity (Kd ~2.4 nM), effectively displacing NuMA and other interactors; mInsc-LGN interaction is required for stabilization of LGN and intracellular localization of mInsc. |
X-ray crystallography (2.6 Å); structure-based mutagenesis; isothermal titration calorimetry; cell biology |
Proceedings of the National Academy of Sciences of the United States of America |
High |
22074847
|
| 2011 |
Crystal structure of Drosophila Pins (LGN ortholog) in complex with Inscuteable, combined with in vitro competition assays, demonstrates that Insc competes with NuMA for LGN TPR binding and has higher affinity. Insc can open the LGN conformational switch. The positively charged EPE-motif contact patch on LGN is shared by both Insc and NuMA. |
X-ray crystallography; in vitro competition assays; isothermal titration calorimetry |
Proceedings of the National Academy of Sciences of the United States of America |
High |
22171003
|
| 2011 |
LGN and NuMA form a lateral belt at the cortex of chick neuroepithelial cells during metaphase. FRAP and live imaging show LGN/NuMA cortical localization is dynamic. The LGN/NuMA/Gαi complex is required for active spindle movements and planar maintenance of the spindle. Lateral restriction of LGN/NuMA is instructive for planar spindle alignment. |
3D live imaging; FRAP; immunofluorescence; dominant-negative LGN; siRNA |
The Journal of cell biology |
High |
21444683
|
| 2011 |
In Drosophila, Wee B/Canoe directly binds the Pins TPR domain; this interaction recruits Canoe to the cortex and is required for activation of the Pins(TPR)-Mud spindle orientation pathway. Canoe RA domains bind RanGTP, and both Canoe(RA) domains and RanGTP are required to recruit Mud to the cortex and activate spindle orientation. |
Direct binding assay; induced cell polarity system; genetic epistasis; immunofluorescence |
The Journal of cell biology |
Medium |
22024168
|
| 2012 |
Mutations in GPSM2 (two single-base deletions, one nonsense mutation, one splice-site mutation) cause Chudley-McCullough syndrome (CMS), characterized by sensorineural hearing loss and brain malformations including frontal polymicrogyria, corpus callosum agenesis, and gray matter heterotopia. This links GPSM2 function in mitotic spindle orientation to the etiology of brain malformations and hearing loss. |
Homozygosity mapping; whole-exome sequencing; brain imaging of affected individuals |
American journal of human genetics |
Medium |
22578326
|
| 2012 |
Crystal structures of LGN GoLoco 3 (GL3) and GL4 in complex with Gαi·GDP reveal the structural basis of GoLoco/Gαi interaction. A highly conserved 'double Arg finger' sequence (RΨ(D/E)(D/E)QR) is responsible for GDP binding. Only a few residues C-terminal to the conserved GL sequence are required for Gαi·GDP interaction. LGN C-terminal GL domain binds four Gαi·GDP molecules; all four GL motifs are potent GDIs. |
X-ray crystallography; isothermal titration calorimetry; fluorescence-based GDI assay |
The Journal of biological chemistry |
High |
22952234
|
| 2013 |
The crystal structure of a truncated LGN reveals its autoinhibited conformation: two consecutive GoLoco (GL) motifs (GL12 or GL34) form minimal TPR-binding units, with GL34 forming parallel α-helices that bind the concave surface of TPR4-7, preventing LGN from binding other targets. GL motifs bind TPRs by a mode distinct from GL/Gαi·GDP interactions. |
X-ray crystallography; binding assays; domain truncation analysis |
Structure (London, England : 1993) |
High |
23665171
|
| 2013 |
LGN associates with cytoplasmic dynein heavy chain (DYNC1H1) in a Gαi-regulated manner. LGN is required for mitotic cortical localization of dynein, which in turn also modulates cortical LGN accumulation. FRAP analysis shows cortical LGN is dynamic and turns over via astral microtubule- and dynein-dependent transport. Actin filaments counteract dynein-mediated cortical release of Gαi/LGN/NuMA, maintaining cortical retention. |
Co-immunoprecipitation; FRAP; siRNA knockdown; cytoskeletal drug treatments; immunofluorescence |
Molecular biology of the cell |
High |
23389635
|
| 2013 |
Par1b promotes the apicolateral accumulation of LGN and capture of NuMA-positive astral microtubules in mitotic hepatocytes to orient the mitotic spindle, resulting in asymmetric inheritance of apical plasma membrane domains between daughter cells. |
siRNA knockdown; immunofluorescence; live imaging; 3D culture |
PLoS biology |
Medium |
24358023
|
| 2014 |
Direct interaction between Dlg1 and LGN promotes cortical localization of the LGN complex and is required for planar spindle orientation in the chick neuroepithelium and human cells on adhesive micropatterns. Live imaging shows Dlg1 is required for directed spindle movements during metaphase. |
Direct binding assay; siRNA knockdown; live imaging; immunofluorescence; dominant-negative experiments |
The Journal of cell biology |
High |
25202028
|
| 2014 |
Par3, mInsc, and Gαi3 cooperate to polarize LGN and promote perpendicular (asymmetric) divisions in murine epidermis. Loss of both Gnai3 and mInsc phenocopies loss of LGN (mostly planar divisions), demonstrating that Par3-mInsc and Gαi3 act cooperatively upstream of LGN to control its apical localization and division orientation. |
Conditional knockouts; in vivo lentiviral RNAi; immunofluorescence; division angle quantification |
Nature cell biology |
High |
25016959
|
| 2014 |
SLK kinase directly activates ERM proteins (ezrin/radixin/moesin) at mitotic entry in mammalian cells. Activated ERMs promote polarized cortical association of LGN and NuMA, which is required for spindle orientation. Impairing ERM activation in apical progenitors of the mouse embryonic neocortex severely disturbs spindle orientation in vivo. |
siRNA knockdown; phospho-specific antibodies; micropatterned adhesive substrates; in vivo mouse neocortex experiments; immunofluorescence |
The Journal of cell biology |
High |
24958772
|
| 2015 |
The GoLoco motifs of GPSM2/LGN are essential for hearing. Mice with truncation of the C-terminal GoLoco motifs (LgnΔC) are profoundly deaf, show hair bundle misorientation and severe stereocilia malformations. Gαi and aPKC depend on LGN for proper localization in hair cells. LGN functions as a PCP effector downstream of core PCP proteins; kinocilium positioning is required for LGN/Gαi/aPKC apical localization. |
Mouse knockout (targeted GoLoco truncation); auditory brainstem response; scanning EM; immunofluorescence; in vitro translation |
Mammalian genome |
High |
26662512
|
| 2016 |
Afadin directly and concomitantly binds both F-actin and LGN. Crystal structure of human Afadin in complex with LGN reveals structural similarity to the LGN-NuMA complex. In mitosis, Afadin is necessary for cortical accumulation of LGN and NuMA above spindle poles in an F-actin-dependent manner. Afadin acts as a molecular hub anchoring the dynein/LGN/NuMA machinery to cortical F-actin. |
X-ray crystallography; direct binding assays; siRNA knockdown; 3D cyst culture; immunofluorescence |
Nature structural & molecular biology |
High |
26751642
|
| 2016 |
SAPCD2 is a novel LGN-interacting protein that negatively regulates LGN cortical localization, likely by competing with NuMA for LGN binding. Loss of SAPCD2 randomizes spindle orientation in epithelial cells and retinal progenitors in vivo, and triples the number of asymmetric terminal divisions in the developing retina. |
Co-immunoprecipitation; siRNA knockdown; in vivo mouse retinal experiments; division angle quantification; immunofluorescence |
Developmental cell |
High |
26766442
|
| 2017 |
E-cadherin functions as an instructive cue for division orientation by directly binding LGN at cell-cell adhesions. LGN adopts a 3D structure similar to cadherin-bound catenins and binds the E-cadherin cytosolic tail. On mitotic entry, NuMA competes LGN from E-cadherin to locally form the LGN/NuMA complex, stabilizing cortical astral microtubule associations at adhesions to orient the spindle. |
Direct binding assay; immunofluorescence; siRNA knockdown; competition assay (NuMA vs E-cadherin for LGN) |
Nature communications |
High |
28045117
|
| 2017 |
Phosphorylation of VE-cadherin Y658 by Src-family kinases induces dissociation of p120ctn, enabling LGN to bind the VE-cadherin cytoplasmic tail at endothelial cell junctions. LGN binding to phospho-Y658 VE-cadherin is required for multiple endothelial flow responses including inflammatory signaling at disturbed flow and flow-dependent vascular remodeling. |
Phosphomimetic and phospho-dead VE-cadherin mutants; Co-IP; siRNA knockdown; in vivo vascular remodeling assays |
Current biology : CB |
High |
28712573
|
| 2017 |
GPSM2 (Gpsm2) and its partner Gαi3 define an ~200 nm nanodomain at stereocilia tips in auditory and vestibular hair cells. Gpsm2 localization at stereocilia tips requires Gαi3, myosin 15 (Myo15a), and whirlin (Whrn). Loss of Gpsm2 disrupts stereocilia elongation and actin dynamics in growth cones (shown by single-molecule tracking). Absence of Gpsm2 or Gαi3 causes deafness and balance defects. |
Mouse knockout; single-molecule tracking (live imaging); STED nanoscopy; auditory/vestibular functional assays; genetic epistasis |
Nature communications |
High |
28387217
|
| 2018 |
Crystal structure of Drosophila LGN (Pins) in complex with the asymmetric domain of Inscuteable reveals a tetrameric arrangement of intertwined molecules. Insc:LGN tetramers form stable cores of Par3-Insc-LGN-GαiGDP complexes that cannot be dissociated by NuMA. In mammary stem cells, Insc bound to LGN:GαiGDP drives asymmetric fate and reverts aberrant symmetric divisions induced by p53 loss, independent of microtubule motor recruitment. |
X-ray crystallography; SEC-SAXS; in vitro complex stability assay; mammary stem cell functional assays; RNAi |
Nature communications |
High |
29523789
|
| 2019 |
GPSM2-GNAI forms a module that confers first-row (tallest stereocilia) identity in the hair bundle. WHRN-GPSM2-GNAI is an extra module recruited to a pre-existing MYO15A-EPS8 complex only in the first (tallest) row. GPSM2 and GNAI are required to stabilize larger amounts of MYO15A-EPS8 in tall-row stereocilia. In GPSM2 or GNAI mutants, bundles retain an embryonic-like generic stereocilia organization. Genetic epistasis demonstrates GPSM2, GNAI, MYO15A, and WHRN operate in series in the same pathway. |
Comprehensive genetic epistasis in mouse auditory epithelium; immunofluorescence; time-course protein distribution analysis in multiple mutant backgrounds |
Current biology : CB |
High |
30827920
|
| 2011 |
In Drosophila, robust spindle alignment by Pins (LGN) is achieved through ultrasensitive activation by Gαi (apparent Hill coefficient 3.1). GoLoco domains GL1 and GL2 act as 'decoys' competing against activation at GL3, generating ultrasensitivity and ensuring Pins-Mud (NuMA) recruitment occurs over a narrow Gαi concentration range. A non-ultrasensitive Pins mutant fails to robustly couple spindle position to cell polarity in neuroblasts. |
Reconstituted spindle orientation pathway assay; Hill coefficient analysis; domain mutant neuroblast experiments |
Molecular cell |
High |
21855794
|